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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Isoleucine (HMDB00172)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-27 14:51:18
Accession Number HMDB00172
Secondary Accession Numbers Not Available
Common Name L-Isoleucine
Description Branched chain amino acids (BCAA) are essential amino acids whose carbon structure is marked by a branch point. These three amino acids are critical to human life and are particularly involved in stress, energy and muscle metabolism. BCAA supplementation as therapy, both oral and intravenous, in human health and disease holds great promise. "BCAA" denotes valine, isoleucine and leucine which are branched chain essential amino acids. Despite their structural similarities, the branched amino acids have different metabolic routes, with valine going solely to carbohydrates, leucine solely to fats and isoleucine to both. The different metabolism accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg and 16 mg/kg of valine, leucine and isoleucine respectively. Furthermore, these amino acids have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. BCAA are decreased in patients with liver disease, such as hepatitis, hepatic coma, cirrhosis, extrahepatic biliary atresia or portacaval shunt; aromatic amino acids (AAA)-tyrosine, tryptophan and phenylalanine, as well as methionine-are increased in these conditions. Valine, in particular, has been established as a useful supplemental therapy to the ailing liver. All the BCAA probably compete with AAA for absorption into the brain. Supplemental BCAA with vitamin B6 and zinc help normalize the BCAA:AAA ratio. The BCAA are not without side effects. Leucine alone, for example, exacerbates pellagra and can cause psychosis in pellagra patients by increasing excretion of niacin in the urine. Leucine may lower brain serotonin and dopamine. A dose of 3 g of isoleucine added to the niacin regime has cleared leucine-aggravated psychosis in schizophrenic patients. Isoleucine may have potential as an antipsychotic treatment. Leucine is more highly concentrated in foods than other amino acids. A cup of milk contains 800 mg of leucine and only 500 mg of isoleucine and valine. A cup of wheat germ has about 1.6 g of leucine and 1 g of isoleucine and valine. The ratio evens out in eggs and cheese. One egg and an ounce of most cheeses each contain about 400 mg of leucine and 400 mg of valine and isoleucine. The ratio of leucine to other BCAA is greatest in pork, where leucine is 7 to 8 g and the other BCAA together are only 3 to 4 g. (http://www.dcnutrition.com)
Synonyms
  1. (2S,3S)-2-Amino-3-methylpentanoate
  2. (2S,3S)-2-Amino-3-methylpentanoic acid
  3. (2S,3S)-2-amino-3-methyl-Pentanoate
  4. (2S,3S)-2-amino-3-methyl-Pentanoic acid
  5. (2S,3S)-a-Amino-b-methyl-n-valerate
  6. (2S,3S)-a-Amino-b-methyl-n-valeric acid
  7. (2S,3S)-a-Amino-b-methylvalerate
  8. (2S,3S)-a-Amino-b-methylvaleric acid
  9. (2S,3S)-alph-Amino-beta-methylvalerate
  10. (2S,3S)-alph-Amino-beta-methylvaleric acid
  11. (2S,3S)-alpha-Amino-beta-merthyl-n-valerate
  12. (2S,3S)-alpha-Amino-beta-merthyl-n-valeric acid
  13. (2S,3S)-alpha-Amino-beta-merthylvalerate
  14. (2S,3S)-alpha-Amino-beta-merthylvaleric acid
  15. (2S,3S)-alpha-Amino-beta-methyl-n-valerate
  16. (2S,3S)-alpha-Amino-beta-methyl-n-valeric acid
  17. (2S,3S)-alpha-Amino-beta-methylvalerate
  18. (2S,3S)-alpha-Amino-beta-methylvaleric acid
  19. (S)-Isoleucine
  20. (S,S)-Isoleucine
  21. 2-Amino-3-methylpentanoate
  22. 2-Amino-3-methylpentanoic acid
  23. 2-Amino-3-methylvalerate
  24. 2-Amino-3-methylvaleric acid
  25. 2S,3S-Isoleucine
  26. Ile
  27. Isoleucine
  28. L-(+)-Isoleucine
  29. L-Ile
  30. [S-(R*,R*)]-2-Amino-3-methylpentanoate
  31. [S-(R*,R*)]-2-Amino-3-methylpentanoic acid
  32. erythro-L-Isoleucine
  33. iso-leucine
Chemical IUPAC Name 2-amino-3-methylpentanoic acid
Chemical Formula C6H13NO2
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
  • alpha-aminoacid
Biofunction
  • Essential amino acids
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Valine, leucine and isoleucine biosynthesis
Application
Source
  • Exogenous
Average Molecular Weight 131.173
Monoisotopic Molecular Weight 131.094635
Isomeric SMILES CC[C@H](C)[C@H](N)C(O)=O
Canonical SMILES CCC(C)C(N)C(O)=O
KEGG Compound ID C00407 Link Image
BioCyc ID ILE Link Image
BiGG ID 34887 Link Image
Wikipedia Link Ile Link Image
NuGOwiki Link HMDB00172 Link Image
Metagene Link HMDB00172 Link Image
METLIN ID 5193 Link Image
PubChem Compound 791 Link Image
PubChem Substance 10367061 Link Image
ChEBI ID 17191 Link Image
CAS Registry Number 73-32-5
InChI Identifier InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1
Synthesis Reference Marvel, C. S. L-Isoleucine. Organic Syntheses (1941), 21 60-4.
Melting Point (Experimental) 285.5 oC
Experimental Water Solubility 34.4 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]; 35 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 114.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -1.70 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.73 [Predicted by ALOGPS]; -1.6 [Predicted by PubChem via XLOGP] 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 1H74 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 62.0 (48.0-76.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 40.0 +/- 20.0 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 69.0 +/- 13.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 64.0 +/- 13.0 uM
Age Children:1-13 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 84.0 +/- 18.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 44.0 +/- 6.0 uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 93. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 81.0 +/- 18.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 93. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 56.0 +/- 12.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 93. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid CSF
Value 3.9 +/- 1.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 5.77 (3.30-8.24) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
Biofluid CSF
Value 13.5 (8.8-18.2) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
Biofluid CSF
Value 8.4 +/- 2.6 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 8.4 +/- 2.5 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 4.3 +/- 3.4 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 7.0 +/- 5.0 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid CSF
Value 5.5 +/- 0.64 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 3.75 +/- 2.75 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 1.579 (0.789-2.368) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 0.94 +/- 0.67 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.8 +/- 1.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 3.0 +/- 1.5 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1.64 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Biofluid Urine
Value 1.41 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Based on one measurement
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 40.3 (38.0-42.6) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 42.7 (38.1-47.3) uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE) Acute Tonic-Clonic Seizures: increased
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 1495.2 +/- 373.0 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Blood
Value 166.0 +/- 5.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments Non-diabetic patients with chronic heart failure
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid Blood
Value 58.5 (26.00-91.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Maple syrup urine disease
Comments Not Available
References
Biofluid Blood
Value 6100.00 (200.00-12000.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Maple syrup urine disease
Comments Not Available
References
Biofluid CSF
Value 7.1 +/- 4.2 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 5.9 +/- 4.0 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 6.0 +/- 0.65 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid CSF
Value 2.4 +/- 0.65 uM
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Biofluid Urine
Value 0.13 +/- 0.04 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Heart failure
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Maple syrup urine disease
Schizophrenia
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Transcription/Translation SMP00019 Link Image
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  2. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  3. He XY, Yang SY: Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids. Endocr Metab Immune Disord Drug Targets. 2006 Mar;6(1):95-102. [PubMed Link Image]
  4. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  5. Vaalasti A, Suomalainen H, Kuokkanen K, Rechardt L: Neuropeptides in cutaneous neurofibromas of von Recklinghausen's disease. J Cutan Pathol. 1990 Dec;17(6):371-3. [PubMed Link Image]
  6. Eriste E, Norberg A, Bonetto V, Nepomuceno D, Lovenberg TW, Sillard R, Jornvall H: A C-terminally elongated form of PHI from porcine intestine. Cell Mol Life Sci. 1999 Nov 15;56(7-8):709-13. [PubMed Link Image]
  7. Jalan R, Olde Damink SW, Lui HF, Glabus M, Deutz NE, Hayes PC, Ebmeier K: Oral amino acid load mimicking hemoglobin results in reduced regional cerebral perfusion and deterioration in memory tests in patients with cirrhosis of the liver. Metab Brain Dis. 2003 Mar;18(1):37-49. [PubMed Link Image]
  8. Hervieu G, Segretain D, Nahon JL: Developmental and stage-dependent expression of melanin-concentrating hormone in mammalian germ cells. Biol Reprod. 1996 Jun;54(6):1161-72. [PubMed Link Image]
  9. Suk FM, Lin MH, Newman M, Pan S, Chen SH, Liu JD, Shih C: Replication advantage and host factor-independent phenotypes attributable to a common naturally occurring capsid mutation (I97L) in human hepatitis B virus. J Virol. 2002 Dec;76(23):12069-77. [PubMed Link Image]
  10. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  11. De Miranda J, Panizzutti R, Foltyn VN, Wolosker H: Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14542-7. Epub 2002 Oct 22. [PubMed Link Image]
  12. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed Link Image]
  13. Blomstrand E, Eliasson J, Karlsson HK, Kohnke R: Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise. J Nutr. 2006 Jan;136(1 Suppl):269S-73S. [PubMed Link Image]
  14. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. [PubMed Link Image]
  15. Sato T, Shimada Y, Nagasawa N, Nakanishi S, Jingami H: Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state. J Biol Chem. 2003 Feb 7;278(6):4314-21. Epub 2002 Nov 19. [PubMed Link Image]
  16. Edvinsson L: Innervation and effects of dilatory neuropeptides on cerebral vessels. New aspects. Blood Vessels. 1991;28(1-3):35-45. [PubMed Link Image]
  17. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Branched-chain-amino-acid aminotransferase, cytosolic
  2. Branched-chain-amino-acid aminotransferase, mitochondrial
  3. Isoleucyl-tRNA synthetase, cytoplasmic
  4. Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
  5. cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
  6. cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
  7. Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
  8. Isoleucyl-tRNA synthetase, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5536
Enzyme 1 Name Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 1 Synonyms
  1. BCAT(c)
  2. Protein ECA39
Enzyme 1 Gene Name BCAT1
Enzyme 1 Protein Sequence >Branched-chain-amino-acid aminotransferase, cytosolic
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
Enzyme 1 Number of Residues 386
Enzyme 1 Molecular Weight 42965.8
Enzyme 1 Theoretical pI 4.95
Enzyme 1 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • branched chain family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine
Enzyme 1 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 38176287 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P54687 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name BCAT1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1161 bp
ATGAAGGATTGCAGTAACGGATGCTCCGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAG
GTGGTGGGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAA
AAACCAGACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTG
GAGTGGTCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCA
TTGCACCCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCA
TTTCGAGGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATG
TATCGCTCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGT
ATTCAACAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTG
TATATTCGTCCTACATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAA
GCCCTGCTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAAT
CCAGTGTCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGAC
TGCAAGATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGCAGTAGATAAT
GGGTGTCAGCAGGTCCTGTGGCTCTATGGAGAGGACCATCAGATCACTGAAGTGGGAACT
ATGAATCTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCA
CTAGATGGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAG
TGGGGTGAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTG
GAGGGGAACAGAGTGAGAGAGATGTTTGGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTT
TCTGATATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAG
CTGGCAAGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGAC
TGGACAATTGTGCTATCCTGA
Enzyme 1 GenBank Gene ID NM_005504.6 Link Image
Enzyme 1 GeneCard ID BCAT1 Link Image
Enzyme 1 GenAtlas ID BCAT1 Link Image
Enzyme 1 HGNC ID HGNC:976 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 12p12.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [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. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. 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]
  5. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5763
Enzyme 2 Name Branched-chain-amino-acid aminotransferase, mitochondrial
Enzyme 2 Synonyms
  1. BCAT(m)
  2. Placental protein 18
  3. PP18
Enzyme 2 Gene Name BCAT2
Enzyme 2 Protein Sequence >Branched-chain-amino-acid aminotransferase, mitochondrial
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 2 Number of Residues 392
Enzyme 2 Molecular Weight 44287.4
Enzyme 2 Theoretical pI 8.82
Enzyme 2 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • branched chain family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids
Enzyme 2 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 13699234 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O15382 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BCAT2_HUMAN Link Image
Enzyme 2 PDB ID 1KTA Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1179 bp
ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCACGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCCTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCACATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA
Enzyme 2 GenBank Gene ID AF268047 Link Image
Enzyme 2 GeneCard ID BCAT2 Link Image
Enzyme 2 GenAtlas ID BCAT2 Link Image
Enzyme 2 HGNC ID HGNC:977 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 19q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed Link Image]
  2. Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [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]
  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. Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [PubMed Link Image]
  6. 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]
  7. Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed Link Image]
  8. Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed Link Image]
  9. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed Link Image]
  10. Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5886
Enzyme 3 Name Isoleucyl-tRNA synthetase, cytoplasmic
Enzyme 3 Synonyms
  1. Isoleucine--tRNA ligase
  2. IRS
  3. IleRS
Enzyme 3 Gene Name IARS
Enzyme 3 Protein Sequence >Isoleucyl-tRNA synthetase, cytoplasmic
MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF
Enzyme 3 Number of Residues 1262
Enzyme 3 Molecular Weight 144496.9
Enzyme 3 Theoretical pI 6.03
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • isoleucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • isoleucyl-tRNA aminoacylation
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 3 General Function Involved in nucleotide binding
Enzyme 3 Specific Function ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle [RN:R03656]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158259489 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P41252 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SYIC_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >3789 bp
ATGCTTCAACAAGTTCCAGAAAACATAAATTTTCCTGCTGAAGAAGAGAAAATCTTGGAG
TTTTGGACTGAATTTAATTGTTTTCAGGAATGCTTAAAGCAATCAAAACATAAACCAAAA
TTTACCTTCTATGATGGTCCTCCTTTTGCAACTGGACTGCCTCACTATGGACATATACTT
GCGGGTACAATTAAAGATATAGTTACAAGATATGCTCACCAGAGTGGGTTTCATGTTGAC
AGAAGATTTGGATGGGATTGCCATGGCTTACCTGTGGAATATGAAATTGATAAGACACTG
GGAATCAGAGGACCAGAGGATGTGGCCAAAATGGGGATTACAGAGTATAACAATCAGTGC
CGAGCAATTGTGATGAGATATTCTGCTGAGTGGAAGTCTACTGTTAGCAGACTTGGCCGA
TGGATTGACTTTGACAATGACTATAAAACTCTGTATCCACAATTCATGGAATCAGTCTGG
TGGGTCTTCAAACAACTCTATGATAAAGGCCTTGTTTATAGAGGTGTGAAAGTCATGCCC
TTCTCTACGGCATGTAACACTCCACTTTCCAACTTCGAGTCACACCAGAATTATAAGGAT
GTTCAAGATCCTTCAGTATTTGTAACTTTCCCTTTGGAAGAAGATGAAACTGTATCTTTA
GTTGCTTGGACAACCACTCCCTGGACTCTACCTAGTAACCTTGCTGTGTGTGTTAATCCA
GAAATGCAATATGTGAAAATTAAAGATGTTGCCAGAGGACGATTACTCATTTTAATGGAA
GCCAGATTGTCAGCCCTCTATAAATTGGAGAGTGACTATGAGATCCTTGAAAGATTTCCT
GGTGCCTATCTTAAAGGCAAGAAGTACAGGCCCCTGTTTGACTATTTCCTGAAGTGTAAA
GAGAATGGCGCTTTCACTGTGCTTGTTGACAACTATGTGAAGGAAGAAGAAGGCACAGGG
GTTGTCCACCAAGCTCCTTACTTCGGTGCTGAGGACTATCGGGTCTGTATGGACTTTAAC
ATTATTCGGAAAGACTCACTCCCTGTTTGCCCTGTGGATGCTTCAGGCTGCTTCACAACG
GAGGTGACAGATTTCGCAGGACAGTATGTGAAGGATGCTGACAAAAGTATCATCAGGACT
TTGAAGGAACAAGGCCGACTTCTGGTTGCCACCACCTTCACTCACAGCTACCCTTTTTGC
TGGAGATCAGACACTCCTCTAATTTACAAAGCAGTGCCCAGCTGGTTTGTGCGAGTGGAG
AACATGGTGGACCAGCTCCTAAGGAACAATGACCTGTGCTACTGGGTCCCAGAGTTGGTA
CGAGAAAAACGATTTGGAAATTGGCTGAAAGATGCACGTGACTGGACAATTTCCAGAAAC
AGATACTGGGGCACCCCCATCCCACTGTGGGTCAGCGATGACTTTGAGGAGGTGGTATGC
ATTGGGTCAGTGGCGGAACTTGAAGAACTGTCAGGAGCAAAGATCTCAGATCTCCACAGA
GAGAGTGTTGACCACCTGACCATTCCTTCACGCTGTGGGAAGGGATCCTTGCACCGCATC
TCTGAAGTGTTTGACTGTTGGTTTGAGAGTGGCAGCATGCCCTATGCTCAGGTTCATTAC
CCGTTTGAAAACAAGAGGGAGTTTGAGGATGCTTTTCCTGCAGATTTCATTGCCGAGGGC
ATCGACCAAACCAGAGGATGGTTTTATACCCTGCTGGTGCTGGCCACGGCCCTCTTTGGA
CAACCGCCTTTCAAGAACGTAATTGTGAATGGGCTTGTCCTGGCAAGTGATGGCCAAAAA
ATGAGCAAACGGAAAAAGAATTATCCAGATCCAGTTTCCATCATCCAGAAGTATGGTGCT
GATGCCCTCAGATTATATCTGATTAACTCCCCTGTGGTGAGAGCAGAAAACCTCCGCTTT
AAAGAAGAGGGTGTGCGGGACGTCCTTAAGGATGTACTGCTCCCATGGTACAATGCCTAT
CGCTTCTTAATCCAGAACGTTCTGAGGCTCCAGAAGGAGGAAGAAATAGAATTTCTCTAC
AATGAGAACACGGTTAGAGAAAGCCCCAACATTACAGACCGGTGGATCCTGTCCTTCATG
CAGTCTCTCATTGGCTTCTTTGAGACTGAAATGGCAGCTTATAGGCTTTATACTGTGGTG
CCTCGCCTGGTCAAGTTTGTAGATATTCTGACCAATTGGTATGTTAGAATGAACCGCAGA
AGATTAAAGGGTGAAAATGGGATGGAGGATTGTGTCATGGCCCTAGAAACCTTGTTTAGT
GTTCTGCTTTCTCTTTGCAGACTTATGGCTCCCTACACACCTTTTCTCACTGAATTGATG
TACCAGAATCTAAAGGTGCTGATTGACCCTGTTTCTGTTCAGGACAAGGACACACTCAGC
ATTCACTACCTCATGCTGCCCCGTGTTCGAGAAGAATTGATTGACAAGAAAACAGAGAGT
GCAGTATCTCAGATGCAGTCTGTGATTGAACTTGGAAGAGTGATCAGAGACCGAAAAACT
ATTCCCATAAAGTATCCTTTGAAAGAAATTGTGGTTATCCATCAAGATCCAGAAGCTCTT
AAAGATATCAAGTCTTTGGAGAAGTATATCATTGAGGAACTCAATGTTCGAAAAGTTACA
CTGTCTACAGATAAAAACAAGTATGGCATTCGGCTAAGGGCAGAACCAGATCACATGGTC
CTGGGGAAGCGTCTGAAGGGAGCCTTTAAGGCAGTGATGACGTCCATCAAGCAGTTGAGC
AGTGAGGAGCTGGAGCAGTTCCAGAAGACTGGGACCATTGTTGTGGAAGGCCATGAATTG
CACGATGAAGACATCCGCCTCATGTACACCTTTGATCAGGCCACAGGTGGGACTGCGCAA
TTTGAAGCACACTCAGATGCTCAGGCTTTGGTCCTCTTAGATGTCACTCCTGACCAGTCA
ATGGTAGATGAAGGAATGGCTCGGGAAGTCATCAATCGCATACAGAAACTTCGCAAAAAG
TGCAATCTGGTTCCAACTGATGAAATCACAGTGTACTATAAAGCAAAGTCTGAAGGAACA
TATCTGAATAGTGTTATTGAAAGCCACACAGAGTTCATATTTACCACCATAAAGGCTCCC
TTGAAACCATATCCAGTTTCTCCATCGGATAAAGTCCTTATTCAAGAAAAAACACAGTTG
AAGGGATCTGAACTGGAAATTACACTCACCAGAGGATCTTCCCTTCCTGGTCCTGCTTGT
GCATATGTCAATCTTAACATTTGTGCAAATGGCAGTGAACAAGGTGGAGTATTGCTCCTG
GAAAATCCAAAAGGTGACAATAGGTTGGACCTTTTAAAGCTGAAGAGTGTTGTCACTAGC
ATTTTTGGTGTGAAAAATACAGAGCTGGCTGTCTTCCATGATGAAACAGAAATACAAAAC
CAAACTGACTTACTGAGTCTTAGTGGAAAAACACTTTGTGTGACTGCAGGATCGGCTCCC
TCTCTGATCAACAGTTCTAGTACTCTTCTTTGTCAGTATATCAACCTACAGCTCCTGAAT
GCAAAGCCACAAGAGTGTTTAATGGGGACAGTGGGCACTCTCCTGCTTGAAAACCCACTT
GGGCAGAATGGGCTCACCCACCAAGGTCTTCTGTATGAAGCAGCCAAGGTGTTTGGCCTT
CGGAGCAGGAAGCTAAAGCTGTTTCTGAATGAGACCCAAACGCAGGAAATTACAGAAGAC
ATCCCCGTGAAGACTTTGAATATGAAGACTGTGTATGTTTCTGTGTTACCAACAACAGCA
GACTTCTAG
Enzyme 3 GenBank Gene ID AK293014 Link Image
Enzyme 3 GeneCard ID IARS Link Image
Enzyme 3 GenAtlas ID IARS Link Image
Enzyme 3 HGNC ID HGNC:5330 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9q21
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T: Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7435-9. [PubMed Link Image]
  2. Nichols RC, Raben N, Boerkoel CF, Plotz PH: Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative mRNA splicing, and the characteristics of an unusually long C-terminal extension. Gene. 1995 Apr 3;155(2):299-304. [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]
  4. 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]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  7. 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]
  8. 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]
  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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6936
Enzyme 4 Name Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Enzyme 4 Synonyms
  1. SBCAD
  2. 2-methyl branched chain acyl-CoA dehydrogenase
  3. 2-MEBCAD
  4. 2-methylbutyryl-coenzyme A dehydrogenase
  5. 2-methylbutyryl-CoA dehydrogenase
Enzyme 4 Gene Name ACADSB
Enzyme 4 Protein Sequence >Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDE
EMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLS
TVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAG
AGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRD
TPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQ
MLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAG
KPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQ
LNTIAKHIDAEY
Enzyme 4 Number of Residues 432
Enzyme 4 Molecular Weight 47485.0
Enzyme 4 Theoretical pI 7.00
Enzyme 4 GO Classification
Function
  • FAD or FADH2 binding
  • acyl-CoA dehydrogenase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • purine nucleoside binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 4 General Function Involved in acyl-CoA dehydrogenase activity
Enzyme 4 Specific Function Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID P45954 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACDSB_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1299 bp
ATGGAGGGCCTGGCAGTGCGGTTGCTGCGCGGCAGCAGGCTGCTAAGAAGAAATTTCCTG
ACTTGTTTGTCTTCTTGGAAGATTCCTCCTCATGTCTCAAAATCTTCCCAGTCAGAAGCT
CTACTCAATATAACAAATAATGGAATACACTTTGCTCCCCTGCAAACATTTACAGATGAG
GAAATGATGATAAAGAGTTCAGTTAAAAAATTTGCTCAGGAACAAATTGCACCTTTGGTT
TCAACCATGGATGAAAATTCGAAAATGGAGAAATCAGTAATACAAGGATTATTTCAACAA
GGGTTGATGGGTATTGAAGTTGACCCAGAATATGGAGGCACAGGAGCTTCTTTTTTATCC
ACTGTGCTCGTGATAGAGGAATTAGCCAAAGTTGATGCATCTGTGGCTGTCTTTTGTGAG
ATCCAGAACACATTAATTAACACACTGATTAGAAAACATGGAACAGAAGAACAAAAGGCC
ACCTATTTGCCTCAGCTCACTACAGAAAAAGTAGGAAGTTTCTGCCTTTCAGAGGCTGGA
GCAGGTAGTGACTCATTTGCTTTGAAGACCAGAGCTGATAAAGAGGGAGATTATTATGTC
CTCAATGGATCAAAGATGTGGATCAGCAGTGCTGAGCATGCAGGGCTCTTTCTGGTGATG
GCAAATGTAGACCCTACCATTGGATATAAGGGAATTACCTCCTTCTTAGTAGATCGTGAT
ACTCCGGGCCTTCATATAGGGAAACCTGAAAACAAATTGGGGCTCAGAGCTTCTTCCACC
TGCCCGTTAACATTCGAAAATGTCAAGGTTCCAGAAGCCAATATCTTGGGACAAATTGGA
CATGGCTATAAGTATGCCATAGGGAGTCTCAATGAAGGTAGAATAGGAATTGCTGCACAG
ATGCTGGGACTGGCGCAAGGATGTTTTGACTACACTATTCCATATATTAAAGAAAGGATA
CAATTTGGCAAAAGACTATTTGATTTTCAGGGCCTCCAACACCAAGTGGCTCACGTGGCC
ACCCAGCTGGAAGCTGCAAGATTACTAACATACAATGCTGCTAGGCTTTTAGAAGCTGGA
AAGCCATTCATAAAAGAAGCGTCAATGGCCAAATACTATGCATCAGAGATTGCAGGACAA
ACAACGAGTAAATGTATCGAGTGGATGGGGGGAGTAGGCTACACCAAAGATTACCCTGTG
GAGAAATACTTCCGAGATGCAAAGATTGGTACGATATATGAAGGAGCTTCCAACATCCAG
TTGAACACCATTGCAAAGCATATCGATGCAGAATACTGA
Enzyme 4 GenBank Gene ID U12778 Link Image
Enzyme 4 GeneCard ID ACADSB Link Image
Enzyme 4 GenAtlas ID ACADSB Link Image
Enzyme 4 HGNC ID HGNC:91 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 10q26.13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B: Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 1994 Nov 15;24(2):280-7. [PubMed Link Image]
  2. Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F: Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. [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. 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]
  5. 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]
  6. Gibson KM, Burlingame TG, Hogema B, Jakobs C, Schutgens RB, Millington D, Roe CR, Roe DS, Sweetman L, Steiner RD, Linck L, Pohowalla P, Sacks M, Kiss D, Rinaldo P, Vockley J: 2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism. Pediatr Res. 2000 Jun;47(6):830-3. [PubMed Link Image]
  7. Madsen PP, Kibaek M, Roca X, Sachidanandam R, Krainer AR, Christensen E, Steiner RD, Gibson KM, Corydon TJ, Knudsen I, Wanders RJ, Ruiter JP, Gregersen N, Andresen BS: Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping. Hum Genet. 2006 Feb;118(6):680-90. Epub 2005 Nov 30. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13126
Enzyme 5 Name cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
Enzyme 5 Synonyms
  1. IARS, transcript variant short, mRNA
  2. Isoleucine-tRNA synthetase, isoform CRA_e
Enzyme 5 Gene Name IARS
Enzyme 5 Protein Sequence >cDNA FLJ77250, highly similar to Homo sapiens isoleucine-tRNA synthetase
MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHIL
AGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQC
RAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMP
FSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNP
EMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCK
ENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTT
EVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVE
NMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVC
IGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHY
PFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQK
MSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAY
RFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVV
PRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELM
YQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKT
IPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMV
LGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQ
FEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGT
YLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPAC
AYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQN
QTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPL
GQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTA
DF
Enzyme 5 Number of Residues 1262
Enzyme 5 Molecular Weight 144500
Enzyme 5 Theoretical pI 6.03
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Translation, ribosomal structure and biogenesis
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158259489 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8KAE9 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8KAE9_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK293014 Link Image
Enzyme 5 GeneCard ID A8KAE9 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16424
Enzyme 6 Name cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name BCAT2
Enzyme 6 Protein Sequence >cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
Enzyme 6 Number of Residues 392
Enzyme 6 Molecular Weight 44288
Enzyme 6 Theoretical pI 8.82
Enzyme 6 GO Classification
Function
  • branched-chain-amino-acid transaminase activity
  • catalytic activity
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • branched chain family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Amino acid transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID B2RB87 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name B2RB87_HUMAN Link Image
Enzyme 6 PDB ID 1KTA Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AK314548 Link Image
Enzyme 6 GeneCard ID B2RB87 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location 19
Enzyme 6 Locus 19q13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16441
Enzyme 7 Name Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name IARS2
Enzyme 7 Protein Sequence >Isoleucyl-tRNA synthetase 2, mitochondrial (Isoleucine-tRNA synthetase 2, mitochondrial)
MRWGLRPRGPGAAALATARSLWGTPRLPCSPGWQGATKRLLVRSVSGASNHQPNSNSGRY
RDTVLLPQTSFPMKLLGRQQPDTELEIQQKCGFSELYSWQRERKVKTEFCLHDGPPYANG
DPHVGHALNKILKDIANRFHMMNGSKIHFVPGWDCHGLPIEIKVLSELGREAQNLSAMEI
RKKARSFAKAAIEKQKSAFIRWGIMADWNNCYYTFDGKYEAKQLRTFYQMYDKGLVYRSY
KPVFWSPSSRTALAEAELEYNPEHVSRSIYVKFPLLKPSPKLASLIDGSSPVSILVWTTQ
PWTIPANEAVCYMPESKYAVVKCSKSGDLYVLAADKVASVASTLETTFETISTLSGVDLE
NGTCSHPLIPDKASPLLPANHVTMAKGTGLVHTAPAHGMEDYGVASQHNLPMDCLVDEDG
VFTDVAGPELQNKAVLEEGTDVVIKMLQTAKNLLKEEKLVHSYPYDWRTKKPVVIRASKQ
WFINITDIKTAAKELLKKVKFIPGSALNGMVEMMDRRPYWCISRQRVWGVPIPVFHHKTK
DEYLINSQTTEHIVKLVEQHGSDIWWTLPPEQLLPKEVLSEVGGPDALEYVPGQDILDIW
FDSGTSWSYVLPGPDQRADLYLEGKDQLGGWFQSSLLTSVAARKRAPYKTVIVHGFTLGE
KGEKMSKSLGNVIHPDVVVNGGQDQSKEPPYGADVLRWWVADSNVFTEVAIGPSVLNAAR
DDISKLRNTLRFLLGNVADFNPETDSIPVNDMYVIDQYMLHLLQDLANKITELYKQYDFG
KVVRLLRTFYTRELSNFYFSIIKDRLYCEKENDPKRRSCQTALVEILDVIVRSFAPILPH
LAEEVFQHIPYIKEPKSVFRTGWISTSSIWKKPGLEEAVESACAMRDSFLGSIPGKNAAE
YKVITVIEPGLLFEIIEMLQSEETSSTSQLNELMMASESTLLAQEPREMTADVIELKGKF
LINLEGGDIREESSYKVIVMPTTKEKCPRCWKYTAESSDTLCPRCAEVVSGK
Enzyme 7 Number of Residues 1012
Enzyme 7 Molecular Weight 113793
Enzyme 7 Theoretical pI 7.20
Enzyme 7 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • isoleucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • transition metal ion binding
  • zinc ion binding
Process
  • RNA metabolism
  • cellular metabolism
  • isoleucyl-tRNA aminoacylation
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
Component
Enzyme 7 General Function Translation, ribosomal structure and biogenesis
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2RPG8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2RPG8_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID BC137438 Link Image
Enzyme 7 GeneCard ID B2RPG8 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16933
Enzyme 8 Name Isoleucyl-tRNA synthetase, mitochondrial
Enzyme 8 Synonyms
  1. Isoleucine--tRNA ligase
  2. IleRS
Enzyme 8 Gene Name IARS2
Enzyme 8 Protein Sequence >Isoleucyl-tRNA synthetase, mitochondrial
MRWGLRPRGPGAAALATARSLWGTPRLPCSPGWQGATKRLLVRSVSGASNHQPNSNSGRY
RDTVLLPQTSFPMKLLGRQQPDTELEIQQKCGFSELYSWQRERKVKTEFCLHDGPPYANG
DPHVGHALNKILKDIANRFHMMNGSKIHFVPGWDCHGLPIEIKVLSELGREAQNLSAMEI
RKKARSFAKAAIEKQKSAFIRWGIMADWNNCYYTFDGKYEAKQLRTFYQMYDKGLVYRSY
KPVFWSPSSRTALAEAELEYNPEHVSRSIYVKFPLLKPSPKLASLIDGSSPVSILVWTTQ
PWTIPANEAVCYMPESKYAVVKCSKSGDLYVLAADKVASVASTLETTFETISTLSGVDLE
NGTCSHPLIPDKASPLLPANHVTMAKGTGLVHTAPAHGMEDYGVASQHNLPMDCLVDEDG
VFTDVAGPELQNKAVLEEGTDVVIKMLQTAKNLLKEEKLVHSYPYDWRTKKPVVIRASKQ
WFINITDIKTAAKELLKKVKFIPGSALNGMVEMMDRRPYWCISRQRVWGVPIPVFHHKTK
DEYLINSQTTEHIVKLVEQHGSDIWWTLPPEQLLPKEVLSEVGGPDALEYVPGQDILDIW
FDSGTSWSYVLPGPDQRADLYLEGKDQLGGWFQSSLLTSVAARKRAPYKTVIVHGFTLGE
KGEKMSKSLGNVIHPDVVVNGGQDQSKEPPYGADVLRWWVADSNVFTEVAIGPSVLNAAR
DDISKLRNTLRFLLGNVADFNPETDSIPVNDMYVIDQYMLHLLQDLANKITELYKQYDFG
KVVRLLRTFYTRELSNFYFSIIKDRLYCEKENDPKRRSCQTALVEILDVIVRSFAPILPH
LAEEVFQHIPYIKEPKSVFRTGWISTSSIWKKPGLEEAVESACAMRDSFLGSIPGKNAAE
YKVITVIEPGLLFEIIEMLQSEETSSTSQLNELMMASESTLLAQEPREMTADVIELKGKF
LINLEGGDIREESSYKVIVMPTTKEKCPRCWKYTAESSDTLCPRCAEVVSGK
Enzyme 8 Number of Residues 1012
Enzyme 8 Molecular Weight 113790.6
Enzyme 8 Theoretical pI 7.20
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • aminoacyl-tRNA ligase activity
  • binding
  • catalytic activity
  • isoleucine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming aminoacyl-tRNA and related compounds
  • ligase activity, forming carbon-oxygen bonds
  • nucleoside binding
  • nucleotide binding
  • purine nucleoside binding
Process
  • RNA metabolic process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • cellular macromolecule metabolic process
  • isoleucyl-tRNA aminoacylation
  • macromolecule biosynthetic process
  • macromolecule metabolic process
  • metabolic process
  • ncRNA metabolic process
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolic process
  • translation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 8 General Function Involved in nucleotide binding
Enzyme 8 Specific Function ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle [RN:R03656]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 46852147 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9NSE4 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name SYIM_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >3039 bp
ATGCGTTGGGGGCTGCGCCCTCGCGGGCCGGGCGCGGCCGCCCTGGCCACTGCCCGAAGT
TTGTGGGGGACGCCCCGCCTTCCCTGCAGCCCGGGATGGCAAGGGGCGACGAAGAGGCTT
CTGGTGCGGTCGGTCTCCGGGGCCAGTAACCACCAGCCGAACTCGAATAGTGGCAGATAC
CGGGACACGGTGCTGCTGCCGCAGACGAGCTTCCCCATGAAGCTGCTGGGCCGCCAGCAG
CCGGACACGGAGCTGGAGATCCAGCAGAAATGTGGATTTTCAGAACTTTATTCATGGCAA
AGAGAAAGAAAAGTAAAGACAGAATTTTGCCTTCATGATGGACCTCCTTATGCAAACGGT
GACCCTCATGTTGGACATGCTTTAAATAAGATTTTGAAAGACATAGCCAATCGATTCCAT
ATGATGAATGGCTCCAAAATACATTTTGTGCCCGGCTGGGATTGTCATGGGTTGCCCATT
GAAATAAAAGTATTATCAGAACTTGGTAGAGAAGCTCAGAATCTTTCAGCTATGGAAATT
AGAAAGAAAGCTAGATCATTTGCTAAAGCAGCCATTGAGAAACAGAAATCAGCATTTATT
CGTTGGGGAATAATGGCAGATTGGAATAATTGCTACTATACATTTGATGGGAAGTATGAA
GCCAAACAGTTGAGAACTTTTTACCAAATGTATGATAAGGGCTTGGTTTATCGATCTTAC
AAACCTGTGTTTTGGTCTCCGTCATCTAGGACTGCATTGGCTGAAGCAGAACTTGAATAT
AATCCTGAGCATGTCAGTCGTTCAATATATGTAAAATTTCCTCTCTTAAAGCCTTCTCCA
AAATTGGCATCTCTTATAGATGGTTCATCTCCTGTTAGTATTTTGGTCTGGACCACACAA
CCTTGGACGATTCCAGCCAATGAAGCTGTTTGCTATATGCCTGAATCAAAGTATGCTGTT
GTGAAATGTTCTAAGTCTGGAGACCTCTACGTACTGGCGGCAGATAAAGTAGCATCTGTT
GCTTCTACTTTGGAAACAACATTTGAGACTATTTCAACACTTTCAGGTGTAGATTTGGAA
AATGGTACTTGCAGTCATCCATTAATTCCTGATAAAGCCTCTCCTCTTTTACCTGCAAAT
CATGTGACCATGGCAAAAGGAACGGGATTGGTTCACACAGCCCCAGCTCATGGTATGGAA
GACTACGGTGTAGCGTCTCAGCACAACCTGCCCATGGATTGTCTAGTGGACGAAGATGGA
GTTTTCACAGATGTTGCAGGTCCTGAACTTCAAAACAAGGCTGTCCTTGAAGAGGGAACT
GATGTGGTTATAAAGATGCTTCAGACTGCAAAGAATTTGTTGAAAGAGGAGAAATTGGTG
CATAGCTATCCGTATGACTGGAGGACCAAGAAACCTGTGGTTATTCGTGCCAGCAAGCAG
TGGTTTATAAACATCACGGATATTAAGACTGCAGCCAAGGAATTGTTAAAAAAGGTGAAA
TTTATTCCTGGATCAGCACTGAATGGCATGGTTGAAATGATGGACAGGCGGCCATATTGG
TGTATATCAAGGCAAAGAGTTTGGGGTGTTCCAATTCCTGTGTTTCATCATAAGACCAAG
GATGAATACTTGATCAACAGCCAAACCACTGAGCATATTGTTAAACTAGTGGAACAACAC
GGCAGTGATATCTGGTGGACTCTTCCCCCTGAACAACTTCTTCCAAAAGAAGTCTTATCT
GAGGTTGGTGGCCCTGATGCCTTGGAATATGTGCCAGGTCAGGATATTTTGGACATCTGG
TTTGATAGCGGAACTTCATGGTCTTATGTTCTTCCAGGTCCTGACCAAAGAGCAGATTTG
TACTTGGAAGGAAAAGACCAGCTCGGGGGTTGGTTTCAGTCATCCTTATTAACAAGTGTG
GCAGCAAGGAAGAGAGCACCTTATAAGACAGTGATTGTTCATGGATTTACCCTTGGAGAA
AAGGGAGAAAAGATGTCCAAGTCTCTTGGGAATGTCATTCATCCTGATGTTGTCGTTAAT
GGAGGACAAGATCAAAGCAAAGAGCCTCCGTATGGTGCTGATGTCCTTCGCTGGTGGGTA
GCTGATTCCAATGTCTTCACCGAAGTTGCAATTGGCCCATCCGTGCTCAATGCTGCCAGA
GATGATATTAGCAAGCTTAGGAATACACTTCGCTTTCTTTTGGGAAATGTGGCTGATTTC
AACCCAGAAACAGATTCCATCCCTGTAAACGATATGTATGTCATAGACCAGTACATGCTA
CACTTACTGCAGGATTTGGCAAACAAGATTACCGAATTATACAAACAATATGATTTTGGA
AAAGTTGTTCGGCTGTTACGGACGTTTTATACCAGAGAGCTCTCTAACTTTTATTTCAGT
ATAATCAAAGATAGGCTCTATTGTGAAAAGGAAAATGACCCCAAACGACGCTCTTGTCAG
ACTGCATTAGTTGAAATTTTGGATGTAATAGTTCGTTCTTTTGCTCCCATTCTTCCTCAC
CTGGCTGAAGAGGTGTTCCAGCACATACCTTATATTAAAGAGCCCAAGAGTGTTTTCCGT
ACTGGGTGGATTAGTACTAGTTCTATCTGGAAAAAGCCCGGGTTGGAAGAAGCTGTGGAG
AGTGCGTGTGCAATGCGAGACTCATTTCTTGGAAGCATCCCTGGCAAAAATGCAGCTGAG
TACAAGGTTATCACTGTGATAGAACCTGGACTGCTTTTTGAGATAATAGAGATGCTGCAG
TCTGAAGAGACTTCCAGCACCTCTCAGTTGAATGAATTAATGATGGCTTCTGAGTCAACT
TTACTGGCTCAGGAACCACGAGAGATGACTGCAGATGTAATCGAGCTTAAAGGGAAATTC
CTCATCAACTTAGAAGGTGGTGATATTCGTGAAGAGTCTTCCTATAAAGTAATTGTCATG
CCGACTACGAAAGAAAAATGCCCCCGTTGTTGGAAGTATACAGCGGAGTCTTCAGATACA
CTGTGTCCTCGATGTGCAGAAGTTGTCAGTGGAAAATAG
Enzyme 8 GenBank Gene ID NM_018060.3 Link Image
Enzyme 8 GeneCard ID IARS2 Link Image
Enzyme 8 GenAtlas ID IARS2 Link Image
Enzyme 8 HGNC ID HGNC:29685 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q41
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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]
  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]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. 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]
Enzyme 8 Metabolite References Not Available