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Human Metabolome Database Version 2.5

 

Showing metabocard for Homocysteine (HMDB00742)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-15 09:49:59
Accession Number HMDB00742
Secondary Accession Numbers HMDB00165
Common Name Homocysteine
Description Homocysteine is a sulfur-containing amino acid that arises during methionine metabolism. Although its concentration in plasma is only about 10 micromolar (uM), even moderate hyperhomocysteinemia is associated with increased incidence of cardiovascular disease and Alzheimer's disease. Elevations in plasma homocysteine are commonly found as a result of vitamin deficiencies, polymorphisms of enzymes of methionine metabolism, and renal disease. Pyridoxal, folic acid, riboflavin, and Vitamin B(12) are all required for methionine metabolism, and deficiency of each of these vitamins result in elevated plasma homocysteine. A polymorphism of methylenetetrahydrofolate reductase (C677T), which is quite common in most populations with a homozygosity rate of 10-15 %, is associated with moderate hyperhomocysteinemia, especially in the context of marginal folate intake. Plasma homocysteine is inversely related to plasma creatinine in patients with renal disease. This is due to an impairment in homocysteine removal in renal disease. The role of these factors, and of modifiable lifestyle factors, in affecting methionine metabolism and in determining plasma homocysteine levels is discussed. Homocysteine is an independent cardiovascular disease (CVD) risk factor modifiable by nutrition and possibly exercise. Homocysteine was first identified as an important biological compound in 1932 and linked with human disease in 1962 when elevated urinary homocysteine levels were found in children with mental retardation. This condition, called homocysteinuria, was later associated with premature occlusive CVD, even in children. These observations led to research investigating the relationship of elevated homocysteine levels and CVD in a wide variety of populations including middle age and elderly men and women with and without traditional risk factors for CVD. (PMID 17136938, 15630149)
Synonyms
  1. (+-)-homocysteine
  2. (S)-2-amino-4-mercapto-Butanoic acid
  3. 2-Amino-4-mercaptobutyric acid
  4. 2-amino-4-mercapto-Butanoic acid
  5. 2-amino-4-mercapto-Butyric acid
  6. 2-amino-4-mercapto-DL-Butyrate
  7. 2-amino-4-mercapto-DL-Butyric acid
  8. 2-amino-4-sulfanylbutanoic acid
  9. D,l-homocysteine
  10. DL-2-Amino-4-mercaptobutyric acid
  11. DL-2-amino-4-mercapto-Butyric acid
  12. DL-Homocysteine
  13. DL-homocysteine (free base)
  14. HCY
  15. Homo-CYS
  16. L-2-amino-4-mercapto-Butyric acid
  17. L-Homocysteine
  18. Usaf B-12
  19. homocysteine
  20. (S)-2-amino-4-mercapto-Butanoate
  21. 2-amino-4-mercapto-Butanoate
  22. 2-amino-4-sulfanylbutanoate
Chemical IUPAC Name 2-amino-4-sulfanylbutanoic acid
Chemical Formula C4H9NO2S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • thiol (sulfanyl compound)
  • alkylthiol
  • alpha-aminoacid
Biofunction
  • Essential amino acid
  • Component of Glycine, serine and threonine metabolism
  • Component of Methionine metabolism
  • Component of Selenoamino acid metabolism
  • Component of Ubiquinone biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 135.185
Monoisotopic Molecular Weight 135.035400
Isomeric SMILES NC(CCS)C(O)=O
Canonical SMILES NC(CCS)C(O)=O
KEGG Compound ID C05330 Link Image
BioCyc ID HOMO-CYS Link Image
BiGG ID 45588 Link Image
Wikipedia Link Homocysteine Link Image
NuGOwiki Link HMDB00742 Link Image
Metagene Link HMDB00742 Link Image
METLIN ID 3256 Link Image
PubChem Compound 778 Link Image
PubChem Substance 8144236 Link Image
ChEBI ID 17230 Link Image
CAS Registry Number 454-29-5
InChI Identifier InChI=1/C4H9NO2S/c5-3(1-2-8)4(6)7/h3,8H,1-2,5H2,(H,6,7)
Synthesis Reference Karrenbauer, Michael; Kleemann, Axel; Luessling, Theodor; Schaefer, Fritz. D,L-Homocysteine (I). Ger. (1984), 4 pp.
Melting Point (Experimental) 232-233 oC
Experimental Water Solubility 148 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 14.8 mg/mL [Predicted by ALOGPS]; 114 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.29 [Predicted by ALOGPS]; -2.2 [Predicted by PubChem via XLOGP]; -2.56 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adipose Tissue
Artery
Brain
Fibroblasts
Intestine
Kidney
Liver
Muscle
Nerve Cells
Neuron
Pancreas
Placenta
Platelet
Concentrations (Normal)
Biofluid Blood
Value 9.11 +/- 2.99 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Bleich S, Otto M, Zerr I, Kropp S, Kretzschmar HA, Wiltfang J: Creutzfeldt-Jakob disease and homocysteine levels in plasma and cerebrospinal fluid. Gerontology. 2005 Mar-Apr;51(2):142-4. [PubMed Link Image]
Biofluid Blood
Value 9.4 (7.3-16.2) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Blood
Value 9.8 (7.6-14.9) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Biofluid Blood
Value 5.00 +/- 1.6 uM
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 10.4 +/- 2.3 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 9.00 +/- 2.2 uM
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 9.00 +/- 2.00 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid CSF
Value 0.15 +/- 0.07 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Bleich S, Otto M, Zerr I, Kropp S, Kretzschmar HA, Wiltfang J: Creutzfeldt-Jakob disease and homocysteine levels in plasma and cerebrospinal fluid. Gerontology. 2005 Mar-Apr;51(2):142-4. [PubMed Link Image]
Biofluid CSF
Value 20.7 +/- 1.7 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Selley ML, Close DR, Stern SE: The effect of increased concentrations of homocysteine on the concentration of (E)-4-hydroxy-2-nonenal in the plasma and cerebrospinal fluid of patients with Alzheimer's disease. Neurobiol Aging. 2002 May-Jun;23(3):383-8. [PubMed Link Image]
Biofluid CSF
Value 0.057 +/- 0.035 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid CSF
Value 0.12 +/- 0.08 uM
Age Elderly:>65 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid CSF
Value 0.09 (0.06-0.16) uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Urine
Value 2.00 +/- 1.65 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Urine
Value 1.5 +/- 0.69 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Urine
Value 1.78 +/- 0.73 umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Urine
Value 1.95 +/- 1.47 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 9.22 +/- 1.81 uM
Age Adult:>18 yrs old
Sex N/A
Condition Creutzfeldt-Jakob disease
Comments Not Available
References
  • Bleich S, Otto M, Zerr I, Kropp S, Kretzschmar HA, Wiltfang J: Creutzfeldt-Jakob disease and homocysteine levels in plasma and cerebrospinal fluid. Gerontology. 2005 Mar-Apr;51(2):142-4. [PubMed Link Image]
Biofluid Blood
Value 12.5 +/- 5.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Sickle cell anemia
Comments Homozygous sickle cell disease
References
  • van der Dijs FP, Schnog JJ, Brouwer DA, Velvis HJ, van den Berg GA, Bakker AJ, Duits AJ, Muskiet FD, Muskiet FA: Elevated homocysteine levels indicate suboptimal folate status in pediatric sickle cell patients. Am J Hematol. 1998 Nov;59(3):192-8. [PubMed Link Image]
Biofluid Blood
Value 12.9 (8.2-28.2) uM
Age Adult:>18 yrs old
Sex N/A
Condition Dementia
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Blood
Value 10.7 (7.6-14.4) uM
Age Adult:>18 yrs old
Sex N/A
Condition Multiple sclerosis
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Blood
Value 10.2 (7.0-17.4) uM
Age Adult:>18 yrs old
Sex N/A
Condition Stroke
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Blood
Value 11.9 (7.0-19.1) uM
Age Adult:>18 yrs old
Sex N/A
Condition Peripheral neuropathy
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid Blood
Value 21.0 (18.5-25.7) uM
Age Adult:>18 yrs old
Sex Both
Condition Chronic renal failure
Comments Not Available
References
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Biofluid Blood
Value 25.5 (16.9-32.6) uM
Age Adult:>18 yrs old
Sex Both
Condition Continuous ambulatory peritoneal dialysis
Comments Not Available
References
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Biofluid Blood
Value 29.7 (25.7-38.2) uM
Age Adult:>18 yrs old
Sex Both
Condition Hemodialysis
Comments Not Available
References
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Biofluid Blood
Value 125.00 (50.00-200.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Homocystinuria
Comments Not Available
References
Biofluid Blood
Value 6.00 (4.8-7.40) uM
Age Adult:>18 yrs old
Sex Both
Condition Homocystinuria
Comments Not Available
References
Biofluid Blood
Value 15.1 uM
Age Adult:>18 yrs old
Sex Both
Condition Parkinson's disease
Comments Not Available
References
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Biofluid Blood
Value 13.9 N/A
Age Adult:>18 yrs old
Sex Both
Condition Amyotrophic lateral sclerosis
Comments Not Available
References
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Biofluid Blood
Value 15.8 N/A
Age Adult:>18 yrs old
Sex Both
Condition Progressive supranuclear palsy
Comments Not Available
References
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Biofluid CSF
Value 0.10 (0.06–0.32) uM
Age Adult:>18 yrs old
Sex N/A
Condition Dementia
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid CSF
Value 14.2 +/- 1.7 uM
Age Elderly:>65 yrs old
Sex N/A
Condition Alzheimer's disease
Comments Not Available
References
  • Selley ML, Close DR, Stern SE: The effect of increased concentrations of homocysteine on the concentration of (E)-4-hydroxy-2-nonenal in the plasma and cerebrospinal fluid of patients with Alzheimer's disease. Neurobiol Aging. 2002 May-Jun;23(3):383-8. [PubMed Link Image]
Biofluid CSF
Value 0.13 +/- 0.03 uM
Age Adult:>18 yrs old
Sex N/A
Condition Creutzfeldt-Jakob disease
Comments Not Available
References
Biofluid CSF
Value 0.12 +/- 0.062 uM
Age Elderly:>65 yrs old
Sex N/A
Condition Alzheimer's disease
Comments Not Available
References
  • Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
Biofluid CSF
Value 0.08 (0.05-0.16) uM
Age Adult:>18 yrs old
Sex N/A
Condition Multiple sclerosis
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid CSF
Value 0.08 (0.06-0.15) uM
Age Adult:>18 yrs old
Sex N/A
Condition Stroke
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid CSF
Value 0.11 (0.07-0.18) uM
Age Adult:>18 yrs old
Sex N/A
Condition Peripheral neuropathy
Comments Not Available
References
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Biofluid CSF
Value 0.216 +/- 0.122 uM
Age Adult:>18 yrs old
Sex N/A
Comments Not Available
References
  • Smach MA, Jacob N, Golmard JL, Charfeddine B, Lammouchi T, Ben Othman L, Dridi H, Bennamou S, Limem K: Folate and homocysteine in the cerebrospinal fluid of patients with Alzheimer's disease or dementia: a case control study. Eur Neurol. 2011;65(5):270-8. doi: 10.1159/000326301. Epub 2011 Apr 8. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
Amyotrophic lateral sclerosis
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Chronic renal failure
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Continuous ambulatory peritoneal dialysis
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Creutzfeldt-Jakob disease
Dementia
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Hemodialysis
  • McGregor DO, Dellow WJ, Lever M, George PM, Robson RA, Chambers ST: Dimethylglycine accumulates in uremia and predicts elevated plasma homocysteine concentrations. Kidney Int. 2001 Jun;59(6):2267-72. [PubMed Link Image]
Homocystinuria
Multiple sclerosis
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Parkinson's disease
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Peripheral neuropathy
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
Progressive supranuclear palsy
  • Levin J, Botzel K, Giese A, Vogeser M, Lorenzl S: Elevated levels of methylmalonate and homocysteine in Parkinson's disease, progressive supranuclear palsy and amyotrophic lateral sclerosis. Dement Geriatr Cogn Disord. 2010 Jul;29(6):553-9. Epub 2010 Jul 3. [PubMed Link Image]
Sickle cell anemia
  • van der Dijs FP, Schnog JJ, Brouwer DA, Velvis HJ, van den Berg GA, Bakker AJ, Duits AJ, Muskiet FD, Muskiet FA: Elevated homocysteine levels indicate suboptimal folate status in pediatric sickle cell patients. Am J Hematol. 1998 Nov;59(3):192-8. [PubMed Link Image]
Stroke
  • Obeid R, Kasoha M, Knapp JP, Kostopoulos P, Becker G, Fassbender K, Herrmann W: Folate and methylation status in relation to phosphorylated tau protein(181P) and beta-amyloid(1-42) in cerebrospinal fluid. Clin Chem. 2007 Jun;53(6):1129-36. Epub 2007 Mar 23. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Betaine Metabolism SMP00123 Link Image map00260 Link Image
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Homocysteine Degradation SMP00455 Link Image
Methionine Metabolism SMP00033 Link Image map00270 Link Image
General References
  1. Yu CK, Lakasing L, Papageorghiou AT, Spencer K, Nicolaides KH: Uterine artery Doppler and mid-trimester maternal plasma homocysteine in subsequent pre-eclampsia. J Matern Fetal Neonatal Med. 2004 Aug;16(2):134-9. [PubMed Link Image]
  2. Giladi N, Mordechovich M, Gruendlinger L, Shabtai H, Merims D, Naor S, Baltadzhieva R, Hausdorff JM, Gur AY, Bornstein NM: "Brain Screen": A self-referral, screening program for strokes, falls and dementia risk factors. J Neurol. 2006 Mar;253(3):307-15. Epub 2005 Oct 10. [PubMed Link Image]
  3. Terzolo M, Allasino B, Bosio S, Brusa E, Daffara F, Ventura M, Aroasio E, Sacchetto G, Reimondo G, Angeli A, Camaschella C: Hyperhomocysteinemia in patients with Cushing's syndrome. J Clin Endocrinol Metab. 2004 Aug;89(8):3745-51. [PubMed Link Image]
  4. Laxdal E, Eide GE, Amundsen SR, Dregelid EB, Pedersen G, Jonung T, Aune S: Homocysteine levels, haemostatic risk factors and restenosis after carotid thrombendarterectomy. Eur J Vasc Endovasc Surg. 2004 Sep;28(3):323-8. [PubMed Link Image]
  5. Akoglu B, Wondra K, Caspary WF, Faust D: Determinants of fasting total serum homocysteine levels in liver transplant recipients. Exp Clin Transplant. 2006 Jun;4(1):462-6. [PubMed Link Image]
  6. Krantz JS, Mack WJ, Hodis HN, Liu CR, Liu CH, Kaufman FR: Early onset of subclinical atherosclerosis in young persons with type 1 diabetes. J Pediatr. 2004 Oct;145(4):452-7. [PubMed Link Image]
  7. Selley ML, Close DR, Stern SE: The effect of increased concentrations of homocysteine on the concentration of (E)-4-hydroxy-2-nonenal in the plasma and cerebrospinal fluid of patients with Alzheimer's disease. Neurobiol Aging. 2002 May-Jun;23(3):383-8. [PubMed Link Image]
  8. Serot JM, Barbe F, Arning E, Bottiglieri T, Franck P, Montagne P, Nicolas JP: Homocysteine and methylmalonic acid concentrations in cerebrospinal fluid: relation with age and Alzheimer's disease. J Neurol Neurosurg Psychiatry. 2005 Nov;76(11):1585-7. [PubMed Link Image]
  9. Hershcovici T, Schechner V, Orlin J, Harell D, Beigel Y: Effect of different LDL-apheresis methods on parameters involved in atherosclerosis. J Clin Apher. 2004;19(2):90-7. [PubMed Link Image]
  10. Muller T, Renger K, Kuhn W: Levodopa-associated increase of homocysteine levels and sural axonal neurodegeneration. Arch Neurol. 2004 May;61(5):657-60. [PubMed Link Image]
  11. Eskes TK: Homocysteine and human reproduction. Clin Exp Obstet Gynecol. 2000;27(3-4):157-67. [PubMed Link Image]
  12. Winkelmayer WC, Kramar R, Curhan GC, Chandraker A, Endler G, Fodinger M, Horl WH, Sunder-Plassmann G: Fasting plasma total homocysteine levels and mortality and allograft loss in kidney transplant recipients: a prospective study. J Am Soc Nephrol. 2005 Jan;16(1):255-60. Epub 2004 Nov 24. [PubMed Link Image]
  13. Park BH, Kim YJ, Park JS, Lee HY, Ha EH, Min JW, Park HS: [Folate and homocysteine levels during pregnancy affect DNA methylation in human placenta] J Prev Med Pub Health. 2005 Nov;38(4):437-42. [PubMed Link Image]
  14. Hossain GS, van Thienen JV, Werstuck GH, Zhou J, Sood SK, Dickhout JG, de Koning AB, Tang D, Wu D, Falk E, Poddar R, Jacobsen DW, Zhang K, Kaufman RJ, Austin RC: TDAG51 is induced by homocysteine, promotes detachment-mediated programmed cell death, and contributes to the cevelopment of atherosclerosis in hyperhomocysteinemia. J Biol Chem. 2003 Aug 8;278(32):30317-27. Epub 2003 May 8. [PubMed Link Image]
  15. Schafer SA, Mussig K, Stefan N, Haring HU, Fritsche A, Balletshofer BM: Plasma homocysteine concentrations in young individuals at increased risk of type 2 diabetes are associated with subtle differences in glomerular filtration rate but not with insulin resistance. Exp Clin Endocrinol Diabetes. 2006 Jun;114(6):306-9. [PubMed Link Image]
  16. Tchantchou F: Homocysteine increase folate oxidative brain homocysteine metabolism and various consequences of folate deficiency. J Alzheimers Dis. 2006 Aug;9(4):421-7. [PubMed Link Image]
  17. Siroka R, Trefil L, Rajdl D, Racek J, Rusnakova H, Cibulka R, Eiselt J, Filipovsky J: Asymmetric dimethylarginine, homocysteine and renal function--is there a relation? Clin Chem Lab Med. 2005;43(10):1147-50. [PubMed Link Image]
  18. Onalan R, Onalan G, Gunenc Z, Karabulut E: Combining 2nd-trimester maternal serum homocysteine levels and uterine artery Doppler for prediction of preeclampsia and isolated intrauterine growth restriction. Gynecol Obstet Invest. 2006;61(3):142-8. Epub 2005 Dec 20. [PubMed Link Image]
  19. Robinson G, Narasimhan S, Weatherall M, Beasley R: Raised plasma homocysteine levels in alcoholism: increasing the risk of heart disease and dementia? N Z Med J. 2005 Jun 3;118(1216):U1490. [PubMed Link Image]
  20. Gulsen M, Yesilova Z, Bagci S, Uygun A, Ozcan A, Ercin CN, Erdil A, Sanisoglu SY, Cakir E, Ates Y, Erbil MK, Karaeren N, Dagalp K: Elevated plasma homocysteine concentrations as a predictor of steatohepatitis in patients with non-alcoholic fatty liver disease. J Gastroenterol Hepatol. 2005 Sep;20(9):1448-55. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Methionine synthase
  2. Betaine--homocysteine S-methyltransferase 1
  3. Putative adenosylhomocysteinase 3
  4. Adenosylhomocysteinase
  5. Putative adenosylhomocysteinase 2
  6. Cystathionine beta-synthase
  7. Betaine--homocysteine S-methyltransferase 2
  8. cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
Enzyme 1 [top]
Enzyme 1 ID 5392
Enzyme 1 Name Methionine synthase
Enzyme 1 Synonyms
  1. 5-methyltetrahydrofolate--homocysteine methyltransferase
  2. Vitamin-B12 dependent methionine synthase
  3. MS
Enzyme 1 Gene Name MTR
Enzyme 1 Protein Sequence >Methionine synthase
MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD
Enzyme 1 Number of Residues 1265
Enzyme 1 Molecular Weight 140525.9
Enzyme 1 Theoretical pI 5.27
Enzyme 1 GO Classification
Function
  • S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • cobalamin binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methionine synthase activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • vitamin binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • pteridine and derivative metabolic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • intracellular
Enzyme 1 General Function Involved in cobalamin binding
Enzyme 1 Specific Function Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine [RN:R00946]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q99707 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name METH_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3798 bp
ATGTCACCCGCGCTCCAAGACCTGTCGCAACCCGAAGGTCTGAAGAAAACCCTGCGGGAT
GAGATCAATGCCATTCTGCAGAAGAGGATTATGGTGCTGGATGGAGGGATGGGGACCATG
ATCCAGCGGGAGAAGCTAAACGAAGAACACTTCCGAGGTCAGGAATTTAAAGATCATGCC
AGGCCGCTGAAAGGCAACAATGACATTTTAAGTATAACTCAGCCTGATGTCATTTACCAA
ATCCATAAGGAATACTTGCTGGCTGGGGCAGATATCATTGAAACAAATACTTTTAGCAGC
ACTAGTATTGCCCAAGCTGACTATGGCCTTGAACACTTGGCCTACCGGATGAACATGTGC
TCTGCAGGAGTGGCCAGAAAAGCTGCCGAGGAGGTAACTCTCCAGACAGGAATTAAGAGG
TTTGTGGCAGGGGCTCTGGGTCCGACTAATAAGACACTCTCTGTGTCCCCATCTGTGGAA
AGGCCGGATTATAGGAACATCACATTTGATGAGCTTGTTGAAGCATACCAAGAGCAGGCC
AAAGGACTTCTGGATGGCGGGGTTGATATCTTACTCATTGAAACTATTTTTGATACTGCC
AATGCCAAGGCAGCCTTGTTTGCACTCCAAAATCTTTTTGAGGAGAAATATGCTCCCCGG
CCTATCTTTATTTCAGGGACGATCGTTGATAAAAGTGGGCGGACTCTTTCCGGACAGACA
GGAGAGGGATTTGTCATCAGCGTGTCTCATGGAGAACCACTCTGCATTGGATTAAATTGT
GCTTTGGGTGCAGCTGAGATGAGACCTTTTATTGAAATAATTGGAAAATGTACAACAGCC
TATGTCCTCTGTTATCCCAATGCAGGTCTTCCCAACACCTTTGGTGACTATGATGAAACG
CCTTCTATGATGGCCAAGCACCTAAAGGATTTTGCTATGGATGGCTTGGTCAATATAGTT
GGAGGATGCTGTGGGTCAACACCAGATCATATCAGGGAAATTGCTGAAGCTGTGAAAAAT
TGTAAGCCTAGAGTTCCACCTGCCACTGCTTTTGAAGGACATATGTTACTGTCTGGTCTA
GAGCCCTTCAGGATTGGACCGTACACCAACTTTGTTAACATTGGAGAGCGCTGTAATGTT
GCAGGATCAAGGAAGTTTGCTAAACTCATCATGGCAGGAAACTATGAAGAAGCCTTGTGT
GTTGCCAAAGTGCAGGTGGAAATGGGAGCCCAGGTGTTGGATGTCAACATGGATGATGGC
ATGCTAGATGGTCCAAGTGCAATGACCAGATTTTGCAACTTAATTGCTTCCGAGCCAGAC
ATCGCAAAGGTACCTTTGTGCATCGACTCCTCCAATTTTGCTGTGATTGAAGCTGGGTTA
AAGTGCTGCCAAGGGAAGTGCATTGTCAATAGCATTAGTCTGAAGGAAGGAGAGGACGAC
TTCTTGGAGAAGGCCAGGAAGATTAAAAAGTATGGAGCTGCTATGGTGGTCATGGCTTTT
GATGAAGAAGGACAGGCAACAGAAACAGACACAAAAATCAGAGTGTGCACCCGGGCCTAC
CATCTGCTTGTGAAAAAACTGGGCTTTAATCCAAATGACATTATTTTTGACCCTAATATC
CTAACCATTGGGACTGGAATGGAGGAACACAACTTGTATGCCATTAATTTTATCCATGCA
ACAAAAGTCATTAAAGAAACATTACCTGGAGCCAGAATAAGTGGAGGTCTTTCCAACTTG
TCCTTCTCCTTCCGAGGAATGGAAGCCATTCGAGAAGCAATGCATGGGGTTTTCCTTTAC
CATGCAATCAAGTCTGGCATGGACATGGGGATAGTGAATGCTGGAAACCTCCCTGTGTAT
GATGATATCCATAAGGAACTTCTGCAGCTCTGTGAAGATCTCATCTGGAATAAAGACCCT
GAGGCCACTGAGAAGCTCTTACGTTATGCCCAGACTCAAGGCACAGGAGGGAAGAAAGTC
ATTCAGACTGATGAGTGGAGAAATGGCCCTGTCGAAGAACGCCTTGAGTATGCCCTTGTG
AAGGGCATTGAAAAACATATTATTGAGGATACTGAGGAAGCCAGGTTAAACCAAAAAAAA
TATCCCCGACCTCTCAATATAATTGAAGGACCCCTGATGAATGGAATGAAAATTGTTGGT
GATCTTTTTGGAGCTGGAAAAATGTTTCTACCTCAGGTTATAAAGTCAGCCCGGGTTATG
AAGAAGGCTGTTGGCCACCTTATCCCTTTCATGGAAAAAGAAAGAGAAGAAACCAGAGTG
CTTAACGGCACAGTAGAAGAAGAGGACCCTTACCAGGGCACCATCGTGCTGGCCACTGTT
AAAGGCGACGTGCACGACATAGGCAAGAACATAGTTGGAGTAGTCCTTGGCTGCAATAAT
TTCCGAGTTATTGATTTAGGAGTCATGACTCCATGTGATAAGATACTGAAAGCTGCTCTT
GACCACAAAGCAGATATAATTGGCCTGTCAGGACTCATCACTCCTTCCCTGGATGAAATG
ATTTTTGTTGCCAAGGAAATGGAGAGATTAGCTATAAGGATTCCATTGTTGATTGGAGGA
GCAACCACTTCAAAAACCCACACAGCAGTTAAAATAGCTCCGAGATACAGTGCACCTGTA
ATCCATGTCCTGGACGCGTCCAAGAGTGTGGTGGTGTGTTCCCAGCTGTTAGATGAAAAT
CTAAAGGATGAATACTTTGAGGAAATCATGGAAGAATATGAAGATATTAGACAGGACCAT
TATGAGTCTCTCAAGGAGAGGAGATACTTACCCTTAAGTCAAGCCAGAAAAAGTGGTTTC
CAAATGGATTGGCTGTCTGAACCTCACCCAGTGAAGCCCACGTTTATTGGGACCCAGGTC
TTTGAAGACTATGACCTGCAGAAGCTGGTGGACTACATTGACTGGAAGCCTTTCTTTGAT
GTCTGGCAGCTCCGGGGCAAGTACCCGAATCGAGGCTTCCCCAAGATATTTAACGACAAA
ACAGTAGGTGGAGAGGCCAGGAAGGTCTACGATGATGCCCACAATATGCTGAACACACTG
ATTAGTCAAAAGAAACTCCGGGCCCGGGGTGTGGTTGGGTTCTGGCCAGCACAGAGTATC
CAAGACGACATTCACCTGTACGCAGAGGCTGCTGTGCCCCAGGCTGCAGAGCCCATAGCC
ACTTTCTATGGGTTAAGGCAACAGGCTGAGAAGGACTCTGCCAGCACGGAGCCATACTAC
TGCCTCTCAGACTTCATCGCTCCCTTGCATTCTGGCATCCGTGACTACCTGGGCCTGTTT
GCCGTTGCCTGCTTTGGGGTAGAAGAGCTGAGCAAGGCCTATGAGGATGATGGTGACGAC
TACAGCAGCATCATGGTCAAGGCGCTGGGGGACCGGCTGGCAGAGGCCTTTGCAGAAGAG
CTCCATGAAAGAGTTCGCCGAGAACTGTGGGCCTACTGTGGCAGTGAGCAGCTGGACGTC
GCAGACCTGCGAAGGTTGCGGTACAAGGGCATCCGCCCGGCTCCTGGCTACCCCAGCCAG
CCCGACCACACCGAGAAGCTCACCATGTGGAGACTCGCAGACATCGAGCAGTCTACAGGC
ATTAGGTTAACAGAATCATTAGCAATGGCACCTGCTTCAGCAGTCTCAGGCCTCTACTTC
TCCAATTTGAAGTCCAAATATTTTGCTGTGGGGAAGATTTCCAAGGATCAGGTTGAGGAT
TATGCATTGAGGAAGAACATATCTGTGGCTGAGGTTGAGAAATGGCTTGGACCCATTTTG
GGATATGATACAGACTAA
Enzyme 1 GenBank Gene ID U71285 Link Image
Enzyme 1 GeneCard ID MTR Link Image
Enzyme 1 GenAtlas ID MTR Link Image
Enzyme 1 HGNC ID HGNC:7468 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1q43
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Leclerc D, Campeau E, Goyette P, Adjalla CE, Christensen B, Ross M, Eydoux P, Rosenblatt DS, Rozen R, Gravel RA: Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum Mol Genet. 1996 Dec;5(12):1867-74. [PubMed Link Image]
  2. Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD: Cloning, mapping and RNA analysis of the human methionine synthase gene. Hum Mol Genet. 1996 Dec;5(12):1851-8. [PubMed Link Image]
  3. Chen LH, Liu ML, Hwang HY, Chen LS, Korenberg J, Shane B: Human methionine synthase. cDNA cloning, gene localization, and expression. J Biol Chem. 1997 Feb 7;272(6):3628-34. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gulati S, Baker P, Li YN, Fowler B, Kruger W, Brody LC, Banerjee R: Defects in human methionine synthase in cblG patients. Hum Mol Genet. 1996 Dec;5(12):1859-65. [PubMed Link Image]
  7. Doolin MT, Barbaux S, McDonnell M, Hoess K, Whitehead AS, Mitchell LE: Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am J Hum Genet. 2002 Nov;71(5):1222-6. Epub 2002 Oct 9. [PubMed Link Image]
  8. O'Leary VB, Mills JL, Pangilinan F, Kirke PN, Cox C, Conley M, Weiler A, Peng K, Shane B, Scott JM, Parle-McDermott A, Molloy AM, Brody LC: Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association. Mol Genet Metab. 2005 Jul;85(3):220-7. Epub 2005 Mar 17. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5831
Enzyme 2 Name Betaine--homocysteine S-methyltransferase 1
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name BHMT
Enzyme 2 Protein Sequence >Betaine--homocysteine S-methyltransferase 1
MPPVGGKKAKKGILERLNAGEIVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLH
REFLRAGSNVMQTFTFYASEDKLENRGNYVLEKISGQEVNEAACDIARQVADEGDALVAG
GVSQTPSYLSCKSETEVKKVFLQQLEVFMKKNVDFLIAEYFEHVEEAVWAVETLIASGKP
VAATMCIGPEGDLHGVPPGECAVRLVKAGASIIGVNCHFDPTISLKTVKLMKEGLEAARL
KAHLMSQPLAYHTPDCNKQGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCC
GFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWVRARARKEYWENLRIASG
RPYNPSMSKPDGWGVTKGTAELMQQKEATTEQQLKELFEKQKFKSQ
Enzyme 2 Number of Residues 406
Enzyme 2 Molecular Weight 44998.2
Enzyme 2 Theoretical pI 7.04
Enzyme 2 GO Classification
Function
  • S-methyltransferase activity
  • betaine-homocysteine S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in zinc ion binding
Enzyme 2 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Enzyme 2 Pathways
Enzyme 2 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4530461 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q93088 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BHMT1_HUMAN Link Image
Enzyme 2 PDB ID 1LT8 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1221 bp
ATGCCACCCGTTGGGGGCAAAAAGGCCAAGAAGGGCATCCTAGAACGTTTAAATGCTGGA
GAGATTGTGATTGGAGATGGAGGGTTTGTCTTTGCACTGGAGAAGAGGGGCTACGTAAAG
GCAGGACCCTGGACTCCTGAAGCTGCTGTGGAGCACCCAGAAGCAGTTCGCCAGCTTCAT
CGAGAGTTCCTCAGAGCTGGCTCAAACGTCATGCAGACCTTCACCTTCTATGCGAGTGAA
GACAAGCTGGAGAACAGGGGCAACTATGTCTTAGAGAAGATATCTGGGCAGGAAGTCAAT
GAAGCTGCTTGCGACATCGCCCGACAAGTGGCTGATGAAGGAGATGCTTTGGTAGCAGGA
GGAGTGAGTCAGACACCTTCATACCTTAGCTGCAAGAGTGAAACTGAAGTCAAAAAAGTA
TTTCTGCAACAGTTAGAGGTCTTTATGAAGAAGAACGTGGACTTCTTGATTGCAGAGTAT
TTTGAACACGTTGAAGAAGCTGTGTGGGCAGTTGAAACCTTGATAGCATCCGGTAAACCT
GTGGCAGCAACCATGTGCATTGGCCCAGAAGGAGATTTGCATGGCGTGCCCCCCGGCGAG
TGTGCAGTGCGCCTGGTGAAAGCAGGAGCATCCATCATTGGTGTGAACTGCCACTTTGAC
CCCACCATTAGTTTAAAAACAGTGAAGCTCATGAAGGAGGGCTTGGAGGCTGCCCGACTG
AAAGCTCACCTGATGAGCCAGCCCTTGGCTTACCACACTCCTGACTGCAACAAGCAGGGA
TTCATCGATCTCCCAGAATTCCCATTTGGACTGGAACCCAGAGTTGCCACCAGATGGGAT
ATTCAAAAATACGCCAGAGAGGCCTACAACCTGGGGGTCAGGTACATTGGCGGGTGCTGT
GGATTTGAGCCCTACCACATCAGGGCAATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTT
TTGCCACCAGCTTCAGAAAAACATGGCAGCTGGGGAAGTGGTTTGGACATGCACACCAAA
CCCTGGGTTAGAGCAAGGGCCAGGAAGGAATACTGGGAGAATCTTCGGATAGCCTCAGGC
CGGCCATACAACCCTTCAATGTCAAAGCCAGATGGCTGGGGAGTGACCAAAGGAACAGCC
GAGCTGATGCAGCAGAAAGAAGCCACAACTGAGCAGCAGCTGAAAGAGCTCTTTGAAAAA
CAAAAATTCAAATCACAGTAG
Enzyme 2 GenBank Gene ID AF118378 Link Image
Enzyme 2 GeneCard ID BHMT Link Image
Enzyme 2 GenAtlas ID BHMT Link Image
Enzyme 2 HGNC ID HGNC:1047 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q13.1-q15
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Garrow TA: Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J Biol Chem. 1996 Sep 13;271(37):22831-8. [PubMed Link Image]
  2. Park EI, Garrow TA: Interaction between dietary methionine and methyl donor intake on rat liver betaine-homocysteine methyltransferase gene expression and organization of the human gene. J Biol Chem. 1999 Mar 19;274(12):7816-24. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sunden SL, Renduchintala MS, Park EI, Miklasz SD, Garrow TA: Betaine-homocysteine methyltransferase expression in porcine and human tissues and chromosomal localization of the human gene. Arch Biochem Biophys. 1997 Sep 1;345(1):171-4. [PubMed Link Image]
  5. Millian NS, Garrow TA: Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch Biochem Biophys. 1998 Aug 1;356(1):93-8. [PubMed Link Image]
  6. Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML: Betaine-homocysteine methyltransferase: zinc in a distorted barrel. Structure. 2002 Sep;10(9):1159-71. [PubMed Link Image]
  7. Weisberg IS, Park E, Ballman KV, Berger P, Nunn M, Suh DS, Breksa AP 3rd, Garrow TA, Rozen R: Investigations of a common genetic variant in betaine-homocysteine methyltransferase (BHMT) in coronary artery disease. Atherosclerosis. 2003 Apr;167(2):205-14. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5933
Enzyme 3 Name Putative adenosylhomocysteinase 3
Enzyme 3 Synonyms
  1. AdoHcyase 3
  2. S-adenosyl-L-homocysteine hydrolase 3
  3. S-adenosylhomocysteine hydrolase-like protein 2
Enzyme 3 Gene Name AHCYL2
Enzyme 3 Protein Sequence >Putative adenosylhomocysteinase 3
MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERP
PVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVK
KQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNS
KGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTA
VLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVE
GWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVN
DSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYV
TEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGH
SNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITA
TTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNK
NGPFKPNYYRY
Enzyme 3 Number of Residues 611
Enzyme 3 Molecular Weight 66720.6
Enzyme 3 Theoretical pI 7.39
Enzyme 3 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 3 General Function Involved in adenosylhomocysteinase activity
Enzyme 3 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 24308043 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96HN2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SAHH3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1836 bp
ATGTCGGTGCAGGTTGTGTCAGCCGCGGCTGCCGCCAAGGTGCCTGAGGTGGAGCTGAAG
GACCTGAGCCCCTCCGAGGCGGAGTCGCAACTAGGACTGAGCACGGCCGCCGTGGGCGCC
ATGGCCCCCCCGGCGGGCGGTGGAGACCCTGAGGCTCCAGCTCCCGCCGCGGAGCGGCCC
CCGGTCCCCGGCCCGGGCTCGGGGCCCGCCGCCGCTCTCAGCCCCGCCGCCGGGAAGGTG
CCTCAGGCGTCGGCCATGAAGCGGAGCGACCCACATCACCAGCACCAGCGGCACCGCGAC
GGCGGCGAGGCCCTGGTCAGCCCCGACGGCACCGTCACCGAGGCGCCGCGCACAGTCAAG
AAGCAGATCCAGTTTGCTGACCAGAAGCAAGAATTCAACAAACGTCCCACCAAAATTGGA
CGTCGCTCTTTGTCTCGTTCCATTTCTCAGTCATCTACTGACAGCTACAGCTCAGCGGCT
TCATATACAGATAGCTCTGATGATGAGACATCGCCCAGGGACAAGCAGCAAAAGAACTCT
AAGGGAAGCAGTGACTTCTGTGTTAAGAACATCAAACAGGCAGAGTTTGGACGAAGAGAA
ATTGAAATTGCTGAACAAGAAATGCCTGCATTGATGGCTTTGAGGAAGAGAGCTCAAGGA
GAAAAGCCTTTGGCTGGAGCCAAAATCGTGGGTTGCACACACATCACTGCTCAGACTGCT
GTGCTTATGGAAACTCTGGGTGCTCTGGGGGCCCAGTGCCGATGGGCTGCCTGCAACATC
TATTCCACTCTCAATGAAGTGGCTGCTGCTCTAGCAGAAAGTGGATTTCCTGTTTTTGCC
TGGAAGGGAGAGTCAGAAGATGACTTTTGGTGGTGTATCGATAGATGTGTGAATGTGGAG
GGCTGGCAGCCAAACATGATCTTGGATGATGGAGGGGATCTTACCCACTGGATTTATAAA
AAGTATCCCAACATGTTTAAGAAAATCAAGGGCATAGTAGAGGAGAGTGTTACTGGAGTT
CACAGGCTGTACCAACTGTCCAAAGCTGGGAAGCTGTGTGTTCCAGCCATGAATGTCAAT
GACTCAGTCACCAAACAGAAATTTGACAACCTCTACTGTTGCCGTGAATCAATTCTTGAT
GGACTTAAAAGGACAACAGACATGATGTTTGGTGGAAAGCAAGTGGTAGTCTGTGGCTAT
GGAGAGGTGGGGAAAGGGTGCTGTGCTGCCCTGAAAGCCATGGGCTCCATTGTGTATGTA
ACTGAAATTGACCCCATCTGTGCCCTGCAAGCCTGTATGGATGGATTTCGACTGGTGAAA
TTAAATGAGGTCATCCGACAAGTGGACATTGTTATTACCTGTACAGGTAACAAGAATGTG
GTAACCAGAGAGCACTTGGACCGTATGAAGAATAGCTGCATCGTTTGTAACATGGGACAT
TCCAACACAGAGATTGACGTGGCGAGTCTGCGGACACCAGAACTGACCTGGGAGCGAGTG
AGATCTCAAGTTGACCATGTGATATGGCCTGATGGCAAGAGGATAGTACTGCTGGCAGAG
GGCCGCCTGCTGAACCTTAGCTGCTCCACAGTGCCTACATTTGTGCTCTCAATCACTGCT
ACTACTCAGGCTCTTGCCTTGATAGAGCTTTACAATGCTCCTGAGGGTCGCTATAAGCAG
GATGTCTACCTGTTGCCCAAGAAGATGGATGAGTATGTGGCCAGCCTACACCTGCCTACC
TTTGATGCCCACTTGACAGAGCTGACAGATGAACAGGCCAAGTATCTGGGACTCAACAAG
AATGGGCCCTTCAAGCCTAATTACTACAGGTATTAA
Enzyme 3 GenBank Gene ID NM_015328.3 Link Image
Enzyme 3 GeneCard ID AHCYL2 Link Image
Enzyme 3 GenAtlas ID AHCYL2 Link Image
Enzyme 3 HGNC ID HGNC:22204 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7q32.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5934
Enzyme 4 Name Adenosylhomocysteinase
Enzyme 4 Synonyms
  1. AdoHcyase
  2. S-adenosyl-L-homocysteine hydrolase
Enzyme 4 Gene Name AHCY
Enzyme 4 Protein Sequence >Adenosylhomocysteinase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 4 Number of Residues 432
Enzyme 4 Molecular Weight 47715.7
Enzyme 4 Theoretical pI 6.29
Enzyme 4 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 4 General Function Involved in adenosylhomocysteinase activity
Enzyme 4 Specific Function Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine
Enzyme 4 Pathways
Enzyme 4 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 178277 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P23526 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SAHH_HUMAN Link Image
Enzyme 4 PDB ID 1LI4 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1299 bp
ATGTCTGACAAACTGCCCTACAAAGTCGCCGACATCGGCCTGGCTGCCTGGGGACGCAAG
GCCCTGGACATTGCTGAGAACGAGATGCCGGGCCTGATGCGTATGCGGGAGCGGTACTCG
GCCTCCAAGCCACTGAAGGGCGCCCGCATCGCTGGCTGCCTGCACATGACCGTGGAGACG
GCCGTCCTCATTGAGACCCTCGTCACCCTGGGTGCTGAGGTGCAGTGGTCCAGCTGCAAC
ATCTTCTCCACCCAGAACCATGCGGCGGCTGCCATTGCCAAGGCTGGCATTCCGGTGTAT
GCCTGGAAGGGCGAAACGGACGAGGAGTACCTGTGGTGCATTGAGCAGACCCTGTACTTC
AAGGACGGGCCCCTCAACATGATTCTGGACGACGGGGGCGACCTCACCAACCTCATCCAC
ACCAAGTACCCGCAGCTTCTGCCAGGCATCCGAGGCATCTCTGAGGAGACCACGACTGGG
GTCCACAACCTCTACAAGATGATGGCCAATGGGATCCTCAAGGTGCCTGCCATCAATGTC
AATGACTCCGTCACCAAGAGCAAGTTTGACAACCTCTATGGCTGCCGGGAGTCCCTCATA
GATGGCATCAAGCGGGCCACAGATGTGATGATTGCCGGCAAGGTAGCGGTGGTAGCAGGC
TATGGTGATGTGGGCAAGGGCTGTGCCCAGGCCCTGCGGGGTTTCGGAGCCCGCGTCATC
ATCACCGAGATTGACCCCATCAACGCACTGCAGGCTGCCATGGAGGGCTATGAGGTGACC
ACCATGGATGAGGCCTGTCAGGAGGGCAACATCTTTGTCACCACCACAGGCTGTATTGAC
ATCATCCTTGGCCGGCACTTTGAGCAGATGAAGGATGATGCCATTGTGTGTAACATTGGA
CACTTTGACGTGGAGATCGATGTCAAGTGGCTCAACGAGAACGCCGTGGAGAAGGTGAAC
ATCAAGCCGCAGGTGGACCGGTATCGGTTGAAGAATGGGCGCCGCATCATCCTGCTGGCC
GAGGGTCGGCTGGTCAACCTGGGTTGTGCCATGGGCCACCCCAGCTTCGTGATGAGTAAC
TCCTTCACCAACCAGGTGATGGCGCAGATCGAGCTGTGGACCCATCCAGACAAGTACCCC
GTTGGGGTTCATTTCCTGCCCAAGAAGCTGGATGAGGCAGTGGCTGAAGCCCACCTGGGC
AAGCTGAATGTGAAGTTGACCAAGCTAACTGAGAAGCAAGCCCAGTACCTGGGCATGTCC
TGTGATGGCCCCTTCAAGCCGGATCACTACCGCTACTGA
Enzyme 4 GenBank Gene ID M61831 Link Image
Enzyme 4 GeneCard ID AHCY Link Image
Enzyme 4 GenAtlas ID AHCY Link Image
Enzyme 4 HGNC ID HGNC:343 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 20cen-q13.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Coulter-Karis DE, Hershfield MS: Sequence of full length cDNA for human S-adenosylhomocysteine hydrolase. Ann Hum Genet. 1989 May;53(Pt 2):169-75. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gupta RA, Yuan CS, Ault-Riche DB, Borchardt RT: Limited proteolysis of S-adenosylhomocysteine hydrolase: implications for the three-dimensional structure. Arch Biochem Biophys. 1995 Jun 1;319(2):365-71. [PubMed Link Image]
  6. Arredondo-Vega FX, Charlton JA, Edwards YH, Hopkinson DA, Whitehouse DB: Isozyme and DNA analysis of human S-adenosyl-L-homocysteine hydrolase (AHCY). Ann Hum Genet. 1989 May;53(Pt 2):157-67. [PubMed Link Image]
  7. Yuan CS, Borchardt RT: Photoaffinity labeling of human placental S-adenosylhomocysteine hydrolase with [2-3H]8-azido-adenosine. J Biol Chem. 1995 Jul 7;270(27):16140-6. [PubMed Link Image]
  8. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, Howell PL: Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol. 1998 May;5(5):369-76. [PubMed Link Image]
  11. Yang X, Hu Y, Yin DH, Turner MA, Wang M, Borchardt RT, Howell PL, Kuczera K, Schowen RL: Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry. 2003 Feb 25;42(7):1900-9. [PubMed Link Image]
  12. Gellekink H, den Heijer M, Kluijtmans LA, Blom HJ: Effect of genetic variation in the human S-adenosylhomocysteine hydrolase gene on total homocysteine concentrations and risk of recurrent venous thrombosis. Eur J Hum Genet. 2004 Nov;12(11):942-8. [PubMed Link Image]
  13. Baric I, Fumic K, Glenn B, Cuk M, Schulze A, Finkelstein JD, James SJ, Mejaski-Bosnjak V, Pazanin L, Pogribny IP, Rados M, Sarnavka V, Scukanec-Spoljar M, Allen RH, Stabler S, Uzelac L, Vugrek O, Wagner C, Zeisel S, Mudd SH: S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4234-9. Epub 2004 Mar 15. [PubMed Link Image]
  14. Buist NR, Glenn B, Vugrek O, Wagner C, Stabler S, Allen RH, Pogribny I, Schulze A, Zeisel SH, Baric I, Mudd SH: S-Adenosylhomocysteine hydrolase deficiency in a 26-year-old man. J Inherit Metab Dis. 2006 Aug;29(4):538-545. Epub 2006 May 30. [PubMed Link Image]
  15. Vugrek O, Beluzic R, Nakic N, Mudd SH: S-adenosylhomocysteine hydrolase (AHCY) deficiency: two novel mutations with lethal outcome. Hum Mutat. 2009 Apr;30(4):E555-65. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5935
Enzyme 5 Name Putative adenosylhomocysteinase 2
Enzyme 5 Synonyms
  1. AdoHcyase 2
  2. DC-expressed AHCY-like molecule
  3. S-adenosyl-L-homocysteine hydrolase 2
  4. S-adenosylhomocysteine hydrolase-like protein 1
Enzyme 5 Gene Name AHCYL1
Enzyme 5 Protein Sequence >Putative adenosylhomocysteinase 2
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGR
RSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREI
EIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIY
STQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKK
YPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDG
LKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKL
NEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVR
SQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQD
VYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
Enzyme 5 Number of Residues 530
Enzyme 5 Molecular Weight 58950.9
Enzyme 5 Theoretical pI 6.87
Enzyme 5 GO Classification
Function
  • adenosylhomocysteinase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • trialkylsulfonium hydrolase activity
Process
  • cellular metabolic process
  • metabolic process
  • one-carbon metabolic process
Component
Enzyme 5 General Function Involved in adenosylhomocysteinase activity
Enzyme 5 Specific Function S-adenosyl-L-homocysteine + H(2)O = L- homocysteine + adenosine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine [RN:R00192]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 16588687 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O43865 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SAHH2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1593 bp
ATGTCGATGCCTGACGCGATGCCGCTGCCCGGGGTCGGGGAGGAGCTGAAGCAGGCCAAG
GAGATCGAGGACGCCGAGAAGTACTCCTTCATGGCCACCGTCACCAAGGCGCCCAAGAAG
CAAATCCAGTTTGCTGATGACATGCAGGAGTTCACCAAATTCCCCACCAAAACTGGCCGA
AGATCTTTGTCTCGCTCGATCTCACAGTCCTCCACTGACAGCTACAGTTCAGCTGCATCC
TACACAGATAGCTCTGATGATGAGGTTTCTCCCCGAGAGAAGCAGCAAACCAACTCCAAG
GGCAGCAGCAATTTCTGTGTGAAGAACATCAAGCAGGCAGAATTTGGACGCCGGGAGATT
GAGATTGCAGAGCAAGACATGTCTGCTCTGATTTCACTCAGGAAACGTGCTCAGGGGGAG
AAGCCCTTGGCTGGTGCTAAAATAGTGGGCTGTACACACATCACAGCCCAGACAGCGGTG
TTGATTGAGACACTCTGTGCCCTGGGGGCTCAGTGCCGCTGGTCTGCTTGTAACATCTAC
TCAACTCAGAATGAAGTAGCTGCAGCACTGGCTGAGGCTGGAGTTGCAGTGTTCGCTTGG
AAGGGCGAGTCAGAAGATGACTTCTGGTGGTGTATTGACCGCTGTGTGAACATGGATGGG
TGGCAGGCCAACATGATCCTGGATGATGGGGGAGACTTAACCCACTGGGTTTATAAGAAG
TATCCAAACGTGTTTAAGAAGATCCGAGGCATTGTGGAAGAGAGCGTGACTGGTGTTCAC
AGGCTGTATCAGCTCTCCAAAGCTGGGAAGCTCTGTGTTCCGGCCATGAACGTCAATGAT
TCTGTTACCAAACAGAAGTTTGATAACTTGTACTGCTGCCGAGAATCCATTTTGGATGGC
CTGAAGAGGACCACAGATGTGATGTTTGGTGGGAAACAAGTGGTGGTGTGTGGCTATGGT
GAGGTAGGCAAGGGCTGCTGTGCTGCTCTCAAAGCTCTTGGAGCAATTGTCTACATTACC
GAAATCGACCCCATCTGTGCTCTGCAGGCCTGCATGGATGGGTTCAGGGTGGTAAAGCTA
AATGAAGTCATCCGGCAAGTCGATGTCGTAATAACTTGCACAGGAAATAAGAATGTAGTG
ACACGGGAGCACTTGGATCGCATGAAAAACAGTTGTATCGTATGCAATATGGGCCACTCC
AACACAGAAATCGATGTGACCAGCCTCCGCACTCCGGAGCTGACGTGGGAGCGAGTACGT
TCTCAGGTGGACCATGTCATCTGGCCAGATGGCAAACGAGTTGTCCTCCTGGCAGAGGGT
CGTCTACTCAATTTGAGCTGCTCCACAGTTCCCACCTTTGTTCTGTCCATCACAGCCACA
ACACAGGCTTTGGCACTGATAGAACTCTATAATGCACCCGAGGGGCGATACAAGCAGGAT
GTGTACTTGCTTCCTAAGAAAATGGATGAATACGTTGCCAGCTTGCATCTGCCATCATTT
GATGCCCACCTTACAGAGCTGACAGATGACCAAGCAAAATATCTGGGACTCAACAAAAAT
GGGCCATTCAAACCTAATTATTACAGATACTAA
Enzyme 5 GenBank Gene ID AF315687 Link Image
Enzyme 5 GeneCard ID AHCYL1 Link Image
Enzyme 5 GenAtlas ID AHCYL1 Link Image
Enzyme 5 HGNC ID HGNC:344 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 1p13.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Dekker JW, Budhia S, Angel NZ, Cooper BJ, Clark GJ, Hart DN, Kato M: Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics. 2002 Mar;53(12):993-1001. Epub 2002 Feb 13. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Imabayashi H, Mori T, Gojo S, Kiyono T, Sugiyama T, Irie R, Isogai T, Hata J, Toyama Y, Umezawa A: Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis. Exp Cell Res. 2003 Aug 1;288(1):35-50. [PubMed Link Image]
  6. Pawlak A, Toussaint C, Levy I, Bulle F, Poyard M, Barouki R, Guellaen G: Characterization of a large population of mRNAs from human testis. Genomics. 1995 Mar 1;26(1):151-8. [PubMed Link Image]
  7. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  8. Cooper BJ, Key B, Carter A, Angel NZ, Hart DN, Kato M: Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development: a possible role for AHCYL1 in inositol phospholipid signaling. J Biol Chem. 2006 Aug 11;281(32):22471-84. Epub 2006 Jun 5. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6059
Enzyme 6 Name Cystathionine beta-synthase
Enzyme 6 Synonyms
  1. Beta-thionase
  2. Serine sulfhydrase
Enzyme 6 Gene Name CBS
Enzyme 6 Protein Sequence >Cystathionine beta-synthase
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
Enzyme 6 Number of Residues 551
Enzyme 6 Molecular Weight 60586.0
Enzyme 6 Theoretical pI 6.63
Enzyme 6 GO Classification
Function
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cofactor binding
  • cystathionine beta-synthase activity
  • hydro-lyase activity
  • lyase activity
  • pyridoxal phosphate binding
Process
  • L-serine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cysteine biosynthetic process
  • cysteine biosynthetic process from serine
  • cysteine biosynthetic process via cystathionine
  • metabolic process
  • serine family amino acid metabolic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 6 General Function Involved in cysteine biosynthetic process from serine
Enzyme 6 Specific Function Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury
Enzyme 6 Pathways
Enzyme 6 Reactions
  • L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 388716 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P35520 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CBS_HUMAN Link Image
Enzyme 6 PDB ID 1JBQ Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1656 bp
ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA
Enzyme 6 GenBank Gene ID L19501 Link Image
Enzyme 6 GeneCard ID CBS Link Image
Enzyme 6 GenAtlas ID CBS Link Image
Enzyme 6 HGNC ID HGNC:1550 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 21q22.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8. [PubMed Link Image]
  2. Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed Link Image]
  3. Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8. [PubMed Link Image]
  4. Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21. [PubMed Link Image]
  5. Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Kraus J, Packman S, Fowler B, Rosenberg LE: Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J Biol Chem. 1978 Sep 25;253(18):6523-8. [PubMed Link Image]
  9. Kabil O, Zhou Y, Banerjee R: Human cystathionine beta-synthase is a target for sumoylation. Biochemistry. 2006 Nov 14;45(45):13528-36. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed Link Image]
  12. Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed Link Image]
  13. Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed Link Image]
  14. Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed Link Image]
  15. Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. [PubMed Link Image]
  16. Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed Link Image]
  17. de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. [PubMed Link Image]
  18. Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. [PubMed Link Image]
  19. Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed Link Image]
  20. Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed Link Image]
  21. Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. [PubMed Link Image]
  22. Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. [PubMed Link Image]
  23. Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. [PubMed Link Image]
  24. Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed Link Image]
  25. Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. [PubMed Link Image]
  26. Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. [PubMed Link Image]
  27. Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. [PubMed Link Image]
  28. Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. [PubMed Link Image]
  29. Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. [PubMed Link Image]
  30. Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. [PubMed Link Image]
  31. Tsai MY, Wong PW, Garg U, Hanson NQ, Schwichtenberg K: Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients. Mol Diagn. 1997 Jun;2(2):129-133. [PubMed Link Image]
  32. Gordon RB, Cox AJ, Dawson PA, Emmerson BT, Kraus JP, Dudman NP: Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria. Mutations in brief no. 120. Online. Hum Mutat. 1998;11(4):332. [PubMed Link Image]
  33. Gallagher PM, Naughten E, Hanson NQ, Schwichtenberg K, Bignell M, Yuan M, Ward P, Yap S, Whitehead AS, Tsai MY: Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria. Mol Genet Metab. 1998 Dec;65(4):298-302. [PubMed Link Image]
  34. de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed Link Image]
  35. Gat-Yablonski G, Mandel H, Fowler B, Taleb O, Sela BA: Homocystinuria in the Arab population of Israel: identification of two novel mutations using DGGE analysis. Hum Mutat. 2000 Oct;16(4):372. [PubMed Link Image]
  36. Janosik M, Oliveriusova J, Janosikova B, Sokolova J, Kraus E, Kraus JP, Kozich V: Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria. Am J Hum Genet. 2001 Jun;68(6):1506-13. Epub 2001 May 15. [PubMed Link Image]
  37. Castro R, Heil SG, Rivera I, Jakobs C, de Almeida IT, Blom HJ: Molecular genetic analysis of the cystathionine beta-synthase gene in Portuguese homocystinuria patients: three novel mutations. Clin Genet. 2001 Aug;60(2):161-3. [PubMed Link Image]
  38. Maclean KN, Gaustadnes M, Oliveriusova J, Janosik M, Kraus E, Kozich V, Kery V, Skovby F, Rudiger N, Ingerslev J, Stabler SP, Allen RH, Kraus JP: High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations. Hum Mutat. 2002 Jun;19(6):641-55. [PubMed Link Image]
  39. Gaustadnes M, Wilcken B, Oliveriusova J, McGill J, Fletcher J, Kraus JP, Wilcken DE: The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment. Hum Mutat. 2002 Aug;20(2):117-26. [PubMed Link Image]
  40. Urreizti R, Balcells S, Rodes M, Vilarinho L, Baldellou A, Couce ML, Munoz C, Campistol J, Pinto X, Vilaseca MA, Grinberg D: Spectrum of CBS mutations in 16 homocystinuric patients from the Iberian Peninsula: high prevalence of T191M and absence of I278T or G307S. Hum Mutat. 2003 Jul;22(1):103. [PubMed Link Image]
  41. Kruger WD, Wang L, Jhee KH, Singh RH, Elsas LJ 2nd: Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype. Hum Mutat. 2003 Dec;22(6):434-41. [PubMed Link Image]
  42. Orendae M, Pronicka E, Kubalska J, Janosik M, Sokolova J, Linnebank M, Koch HG, Kozich V: Identification and functional analysis of two novel mutations in the CBS gene in Polish patients with homocystinuria. Hum Mutat. 2004 Jun;23(6):631. [PubMed Link Image]
  43. Linnebank M, Janosik M, Kozich V, Pronicka E, Kubalska J, Sokolova J, Linnebank A, Schmidt E, Leyendecker C, Klockgether T, Kraus JP, Koch HG: The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: Vitamin B6 nonresponsiveness and a common ancestral haplotype. Hum Mutat. 2004 Oct;24(4):352-3. [PubMed Link Image]
  44. Porto MP, Galdieri LC, Pereira VG, Vergani N, da Rocha JC, Micheletti C, Martins AM, Perez AB, Almeida VD: Molecular analysis of homocystinuria in Brazilian patients. Clin Chim Acta. 2005 Dec;362(1-2):71-8. Epub 2005 Jul 5. [PubMed Link Image]
  45. Lee SJ, Lee DH, Yoo HW, Koo SK, Park ES, Park JW, Lim HG, Jung SC: Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria. J Hum Genet. 2005;50(12):648-54. Epub 2005 Oct 5. [PubMed Link Image]
  46. Urreizti R, Asteggiano C, Cozar M, Frank N, Vilaseca MA, Grinberg D, Balcells S: Functional assays testing pathogenicity of 14 cystathionine-beta synthase mutations. Hum Mutat. 2006 Feb;27(2):211. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 9885
Enzyme 7 Name Betaine--homocysteine S-methyltransferase 2
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name BHMT2
Enzyme 7 Protein Sequence >Betaine--homocysteine S-methyltransferase 2
MAPAGRPGAKKGILERLESGEVVIGDGSFLITLEKRGYVKAGLWTPEAVIEHPDAVRQLH
MEFLRAGSNVMQTFTFSASEDNMESKWEDVNAAACDLAREVAGKGDALVAGGICQTSIYK
YQKDEARIKKLFRQQLEVFAWKNVDFLIAEYFEHVEEAVWAVEVLKESDRPVAVTMCIGP
EGDMHDITPGECAVRLVKAGASIVGVNCRFGPDTSLKTMELMKEGLEWAGLKAHLMVQPL
GFHAPDCGKEGFVDLPEYPFGLESRVATRWDIQKYAREAYNLGVRYIGGCCGFEPYHIRA
IAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRARARREYWENLLPASGRPFCPSLSK
PDF
Enzyme 7 Number of Residues 363
Enzyme 7 Molecular Weight 40353.8
Enzyme 7 Theoretical pI 5.68
Enzyme 7 GO Classification
Function
  • S-methyltransferase activity
  • betaine-homocysteine S-methyltransferase activity
  • binding
  • catalytic activity
  • cation binding
  • homocysteine S-methyltransferase activity
  • ion binding
  • metal ion binding
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine biosynthetic process
  • sulfur amino acid biosynthetic process
  • sulfur amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 7 General Function Involved in zinc ion binding
Enzyme 7 Specific Function Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline
Enzyme 7 Pathways
Enzyme 7 Reactions
  • trimethylammonioacetate + L-homocysteine = dimethylglycine + L-methionine [RN:R02821]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 11907831 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9H2M3 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name BHMT2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1092 bp
ATGGCACCTGCTGGACGCCCGGGGGCCAAGAAGGGGATTTTGGAGCGCCTGGAGAGTGGG
GAGGTTGTGATTGGAGATGGCAGCTTTCTCATTACTCTGGAGAAGAGAGGCTATGTGAAG
GCTGGGCTCTGGACTCCAGAGGCAGTGATAGAACACCCAGACGCAGTTCGTCAACTTCAC
ATGGAATTCTTGAGAGCAGGATCAAATGTCATGCAGACTTTTACCTTTTCTGCCAGTGAG
GACAATATGGAAAGCAAGTGGGAAGATGTAAATGCTGCTGCCTGTGACCTCGCCAGGGAA
GTGGCTGGCAAAGGTGATGCTTTGGTAGCAGGGGGGATCTGCCAGACATCAATATACAAA
TACCAGAAGGATGAAGCTAGAATTAAAAAACTTTTTCGACAACAGCTAGAAGTTTTTGCC
TGGAAAAATGTGGACTTCTTGATTGCAGAGTATTTTGAGCACGTTGAAGAAGCTGTGTGG
GCTGTGGAAGTCTTAAAAGAATCAGATAGACCCGTGGCAGTTACCATGTGCATAGGCCCA
GAGGGAGACATGCATGATATAACCCCCGGAGAATGTGCTGTGAGGCTGGTGAAGGCAGGG
GCTTCCATCGTTGGCGTGAACTGCCGCTTTGGGCCCGACACCAGCTTGAAGACGATGGAG
CTCATGAAGGAGGGTCTTGAGTGGGCAGGGCTGAAAGCGCACCTCATGGTGCAGCCTCTG
GGGTTCCACGCGCCTGACTGTGGCAAAGAGGGGTTTGTGGATCTCCCAGAATATCCCTTT
GGACTGGAGTCCAGAGTTGCCACCAGATGGGATATTCAAAAATACGCCAGAGAGGCCTAC
AACCTGGGGGTCAGGTACATTGGCGGGTGCTGTGGATTTGAGCCCTACCACATCAGGGCA
ATTGCAGAGGAGCTGGCCCCAGAAAGGGGCTTTTTGCCACCAGCTTCAGAAAAACACGGC
AGCTGGGGAAGTGGTTTGGACATGCACACCAAACCCTGGATTAGAGCAAGGGCTCGAAGG
GAGTATTGGGAGAATCTGCTGCCAGCTTCAGGCAGACCTTTCTGTCCTTCGCTGTCAAAG
CCAGACTTCTAA
Enzyme 7 GenBank Gene ID AF257473 Link Image
Enzyme 7 GeneCard ID BHMT2 Link Image
Enzyme 7 GenAtlas ID BHMT2 Link Image
Enzyme 7 HGNC ID HGNC:1048 Link Image
Enzyme 7 Chromosome Location 5
Enzyme 7 Locus 5q13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Chadwick LH, McCandless SE, Silverman GL, Schwartz S, Westaway D, Nadeau JH: Betaine-homocysteine methyltransferase-2: cDNA cloning, gene sequence, physical mapping, and expression of the human and mouse genes. Genomics. 2000 Nov 15;70(1):66-73. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13068
Enzyme 8 Name cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
Enzyme 8 Synonyms
  1. AHCY, mRNA
  2. S-adenosylhomocysteine hydrolase, isoform CRA_a
Enzyme 8 Gene Name AHCY
Enzyme 8 Protein Sequence >cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET
AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF
KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV
NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI
ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG
HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN
SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS
CDGPFKPDHYRY
Enzyme 8 Number of Residues 432
Enzyme 8 Molecular Weight 47717
Enzyme 8 Theoretical pI 6.29
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Coenzyme transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158261867 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A8K307 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K307_HUMAN Link Image
Enzyme 8 PDB ID 1LI4 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK290422 Link Image
Enzyme 8 GeneCard ID A8K307 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available