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Human Metabolome Database Version 2.5

 

Showing metabocard for Acetoacetic acid (HMDB00060)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-13 00:30:49
Accession Number HMDB00060
Secondary Accession Numbers Not Available
Common Name Acetoacetic acid
Description It is a weak organic acid and can be produced in the human liver under certain conditions of poor metabolism leading to excessive fatty acid breakdown (diabetes mellitus leading to diabetic ketoacidosis), it is then partially converted to acetone by decarboxylation and excreted either in urine or through respiration. Persistent mild hyperketonemia is a common finding in newborns. These compounds serve as an indispensable source of energy for extrahepatic tissues, especially the brain and lung of developing rats. Another important function of ketone bodies is to provide acetoacetyl-CoA and acetyl-CoA for synthesis of cholesterol, fatty acids, and complex lipids. During the early postnatal period, acetoacetate (AcAc) and beta-hydroxybutyrate are preferred over glucose as substrates for synthesis of phospholipids and sphingolipids in accord with requirements for brain growth and myelination. Thus, during the first 2 wk of postnatal development, when the accumulation of cholesterol and phospholipids accelerates, the proportion of ketone bodies incorporated into these lipids increases. On the other hand, an increased proportion of ketone bodies are utilized for cerebroside synthesis during the period of active myelination. In the lung, AcAc serves better than glucose as a precursor for the synthesis of lung phospholipids. The synthesized lipids, particularly dipalmityl phosphatidylcholine, are incorporated into surfactant, and thus have a potential role in supplying adequate surfactant lipids to maintain lung function during the early days of life. (PMID 3884391) The acid is also present in the metabolism of those undergoing starvation or prolonged physical exertion as part of gluconeogenesis. When ketone bodies are measured by way of urine concentration, acetoacetic acid, along with beta-hydroxybutyric acid or acetone, is what is detected.
Synonyms
  1. 3-Ketobutyrate
  2. 3-Oxo-butanoate
  3. 3-Oxo-butanoic acid
  4. 3-Oxobutyrate
  5. 3-Oxobutyric acid
  6. Acetoacetate
  7. diacetate
  8. diacetic acid
  9. 3-Ketobutyric acid
Chemical IUPAC Name 3-oxobutanoic acid
Chemical Formula C4H6O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Keto-Acids
Sub Class
  • Short chain keto-acids
Family
  • Mammalian Metabolite
Species
  • ketone
  • carboxylic acid
Biofunction
  • Component of Butanoate metabolism
  • Component of Tyrosine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 102.089
Monoisotopic Molecular Weight 102.031693
Isomeric SMILES CC(=O)CC(O)=O
Canonical SMILES CC(=O)CC(O)=O
KEGG Compound ID C00164 Link Image
BioCyc ID 3-KETOBUTYRATE Link Image
BiGG ID 1485291 Link Image
Wikipedia Link Acetoacetic acid Link Image
NuGOwiki Link HMDB00060 Link Image
Metagene Link HMDB00060 Link Image
METLIN ID 276 Link Image
PubChem Compound 96 Link Image
PubChem Substance 3464 Link Image
ChEBI ID 15344 Link Image
CAS Registry Number 541-50-4
InChI Identifier InChI=1/C4H6O3/c1-3(5)2-4(6)7/h2H2,1H3,(H,6,7)
Synthesis Reference Lopez-Soriano, F. J.; Argiles, J. M. A simple method for the preparation of acetoacetate. Analytical Letters (1985), 18(B5), 589-92.
Melting Point (Experimental) 36.5 oC
Experimental Water Solubility 1000 mg/mL at 20 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 240.00002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.47 [Predicted by ALOGPS]; 0 [Predicted by PubChem via XLOGP]; -0.98 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1QCO 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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Fibroblasts
Liver
Lymphocyte
Neuron
Spleen
Concentrations (Normal)
Biofluid Blood
Value 21.0 (0.0-86.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 1700 (1500-1900) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Biofluid CSF
Value 26.2 +/- 12.3 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 6.0 +/- 6.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid CSF
Value 12.0 +/- 14.0 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 Urine
Value 0.15 (0.01-0.58) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 0.20 (0.020-0.82) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Lee SH, Kim SO, Chung BC: Gas chromatographic-mass spectrometric determination of urinary oxoacids using O-(2,3,4,5,6-pentafluorobenzyl)oxime-trimethylsilyl ester derivatization and cation-exchange chromatography. J Chromatogr B Biomed Sci Appl. 1998 Nov 20;719(1-2):1-7. [PubMed Link Image]
Biofluid Urine
Value 33.0(0.00-67.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. [PubMed Link Image]
Biofluid Urine
Value 1.00 (0.00-2.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 3030.0 +/- 20.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments With ketoacidosis
References
  • Tasker RC, Lutman D, Peters MJ: Hyperventilation in severe diabetic ketoacidosis. Pediatr Crit Care Med. 2005 Jul;6(4):405-11. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 1000 (800-1200) uM
Age Adult:>18 yrs old
Sex Both
Condition Anoxia
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Biofluid CSF
Value 248 +/- 179 uM
Age Children:1-13 yrs old
Sex N/A
Condition Glucose transporter type 1 deficiency syndrome
Comments Not Available
References
  • Klepper J, Diefenbach S, Kohlschutter A, Voit T: Effects of the ketogenic diet in the glucose transporter 1 deficiency syndrome. Prostaglandins Leukot Essent Fatty Acids. 2004 Mar;70(3):321-7. [PubMed Link Image]
Biofluid CSF
Value 322.0 (240.0-404.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Meningitis
Comments Bacterial
References
  • Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
Biofluid Urine
Value 237.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Diabetes mellitus type 2
Comments Not Available
References
  • Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. [PubMed Link Image]
Biofluid Urine
Value 10025.00 (50.00-20000.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Ketosis
Comments Not Available
References
Associated Disorders
Condition References
Anoxia
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Diabetes mellitus type 2
Glucose transporter type 1 deficiency syndrome
  • Klepper J, Diefenbach S, Kohlschutter A, Voit T: Effects of the ketogenic diet in the glucose transporter 1 deficiency syndrome. Prostaglandins Leukot Essent Fatty Acids. 2004 Mar;70(3):321-7. [PubMed Link Image]
Ketosis
Meningitis
  • Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
OMIM ID
  • 125853 Link Image (Diabetes mellitus type 2)
  • 606777 Link Image (Glucose transporter type 1 deficiency syndrome)
Pathways
Name SMPDB Link KEGG Link
Butyrate Metabolism SMP00073 Link Image map00650 Link Image
Fatty Acid Biosynthesis SMP00456 Link Image
Ketone Body Metabolism SMP00071 Link Image map00072 Link Image
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
Tyrosine Metabolism SMP00006 Link Image map00350 Link Image
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Heller MJ, Adams PW, Orosz CG: Evaluation of an automated method of percent reactive antibody determination. Hum Immunol. 1992 Nov;35(3):179-87. [PubMed Link Image]
  2. Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
  3. Subramanian A, Gupta A, Saxena S, Gupta A, Kumar R, Nigam A, Kumar R, Mandal SK, Roy R: Proton MR CSF analysis and a new software as predictors for the differentiation of meningitis in children. NMR Biomed. 2005 Jun;18(4):213-25. [PubMed Link Image]
  4. Tasker RC, Lutman D, Peters MJ: Hyperventilation in severe diabetic ketoacidosis. Pediatr Crit Care Med. 2005 Jul;6(4):405-11. [PubMed Link Image]
  5. Oligny LL, Lough J: Hepatic sinusoidal ectasia. Hum Pathol. 1992 Aug;23(8):953-6. [PubMed Link Image]
  6. 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]
  7. Galey JB, Destree O, Dumats J, Genard S, Tachon P: Protection against oxidative damage by iron chelators: effect of lipophilic analogues and prodrugs of N,N'-bis(3,4,5-trimethoxybenzyl)ethylenediamine- N,N'-diacetic acid (OR10141). J Med Chem. 2000 Apr 6;43(7):1418-21. [PubMed Link Image]
  8. Saibara T, Onishi S, Sone J, Yamamoto N, Shimahara Y, Mori K, Ozawa K, Yamamoto Y: Arterial ketone body ratio as a possible indicator for liver transplantation in fulminant hepatic failure. Transplantation. 1991 Apr;51(4):782-6. [PubMed Link Image]
  9. Mahowald ML, Handwerger BS, Capertone EM Jr, Douglas SD: A comparative study of procedures for sheep erythrocyte-human-T-lymphocyte rosette formation. J Immunol Methods. 1977;15(3):239-45. [PubMed Link Image]
  10. Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
  11. Sato T, Oouchi M, Nagakubo H, Chiba T, Ogawa S, Sato C, Sugimura K, Fukuda M: Effect of pravastatin on plasma ketone bodies in diabetics with hypercholesterolemia. Tohoku J Exp Med. 1998 May;185(1):25-9. [PubMed Link Image]
  12. Nicholson JK, Foxall PJ, Spraul M, Farrant RD, Lindon JC: 750 MHz 1H and 1H-13C NMR spectroscopy of human blood plasma. Anal Chem. 1995 Mar 1;67(5):793-811. [PubMed Link Image]
  13. Krejsa CM, Schieven GL: Detection of oxidative stress in lymphocytes using dichlorodihydrofluorescein diacetate. Methods Mol Biol. 2000;99:35-47. [PubMed Link Image]
  14. Fritzsche I, Buhrdel P, Melcher R, Bohme HJ: Stability of ketone bodies in serum in dependence on storage time and storage temperature. Clin Lab. 2001;47(7-8):399-403. [PubMed Link Image]
  15. Polsky-Fisher SL, Cao H, Lu P, Gibson CR: Effect of cytochromes P450 chemical inhibitors and monoclonal antibodies on human liver microsomal esterase activity. Drug Metab Dispos. 2006 Aug;34(8):1361-6. Epub 2006 May 23. [PubMed Link Image]
  16. Fulop M, Murthy V, Michilli A, Nalamati J, Qian Q, Saitowitz A: Serum beta-hydroxybutyrate measurement in patients with uncontrolled diabetes mellitus. Arch Intern Med. 1999 Feb 22;159(4):381-4. [PubMed Link Image]
  17. Tanaka Y, Ohdan H, Onoe T, Mitsuta H, Tashiro H, Itamoto T, Asahara T: Low incidence of acute rejection after living-donor liver transplantation: immunologic analyses by mixed lymphocyte reaction using a carboxyfluorescein diacetate succinimidyl ester labeling technique. Transplantation. 2005 May 15;79(9):1262-7. [PubMed Link Image]
  18. Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. [PubMed Link Image]
  19. de Araujo Burgos MG, Bion FM, Campos F: [Lactation and alcohol: clinical and nutritional effects] Arch Latinoam Nutr. 2004 Mar;54(1):25-35. [PubMed Link Image]
  20. Walker V, Mills GA, Mellor JM, Langley GJ, Farrant RD: A novel pyrroline-5-carboxylic acid and acetoacetic acid adduct in hyperprolinaemia type II. Clin Chim Acta. 2003 May;331(1-2):7-17. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor
  2. Aldehyde dehydrogenase, mitochondrial precursor
  3. D-beta-hydroxybutyrate dehydrogenase, mitochondrial precursor
  4. Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor
  5. Fumarylacetoacetase
  6. Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor
  7. Alcohol dehydrogenase iron-containing 1
  8. Acetoacetyl-CoA synthetase
  9. 3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1
  10. 3-hydroxybutyrate dehydrogenase type 2
  11. cDNA, FLJ94596, Homo sapiens fumarylacetoacetate hydrolase (fumarylacetoacetase)(FAH), mRNA (Fumarylacetoacetate hydrolase (Fumarylacetoacetase), isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5238
Enzyme 1 Name Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor
Enzyme 1 Synonyms
  1. HMG-CoA lyase
  2. HL
  3. 3-hydroxy-3-methylglutarate-CoA lyase
Enzyme 1 Gene Name HMGCL
Enzyme 1 Protein Sequence >Hydroxymethylglutaryl-CoA lyase, mitochondrial precursor
MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLI
DMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAG
AKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKI
SPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQ
ALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLL
EAGNFICQALNRKTSSKVAQATCKL
Enzyme 1 Number of Residues 325
Enzyme 1 Molecular Weight 34361
Enzyme 1 Theoretical pI 8.71
Enzyme 1 GO Classification
Function
  • carbon-carbon lyase activity
  • catalytic activity
  • hydroxymethylglutaryl-CoA lyase activity
  • lyase activity
  • oxo-acid-lyase activity
Process
Component
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl- CoA + acetoacetate
Enzyme 1 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-23
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 184503 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P35914 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HMGCL_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >978 bp
ATGGCAGCAATGAGGAAGGCGCTTCCGCGGCGACTGGTGGGCTTGGCGTCCCTCCGGGCT
GTCAGCACCTCATCTATGGGCACTTTACCAAAGCGGGTGAAAATTGTGGAAGTTGGTCCC
CGAGATGGACTACAAAATGAAAAGAATATCGTATCTACTCCAGTGAAAATCAAGCTGATA
GACATGCTTTCTGAAGCAGGACTCTCTGTTATAGAAACCACCAGCTTTGTGTCTCCTAAG
TGGGTTCCCCAGATGGGTGACCACACTGAAGTCTTGAAGGGCATTCAGAAGTTTCCTGGC
ATCAACTACCCAGTCCTGACCCCAAATTTGAAAGGCTTCGAGGCAGCGGTTGCTGCTGGA
GCCAAGGAAGTAGTCATCTTTGGAGCTGCCTCAGAGCTCTTCACCAAGAAGAACATCAAT
TGTTCCATAGAGGAGAGTTTTCAGAGGTTTGACGCAATCCTGAAGGCAGCGCAGTCAGCC
AATATTTCTGTGCGGGGGTACGTCTCCTGTGCTCTTGGCTGCCCTTATGAAGGGAAGATC
TCCCCAGCTAAAGTAGCTGAGGTCACCAAGAAGTTCTACTCAATGGGCTGCTACGAGATC
TCCCTGGGGGACACCATTGGTGTGGGCACCCCAGGGATCATGAAAGACATGCTATCTGCT
GTCATGCAGGAAGTGCCTCTGGCTGCCCTGGCTGTCCACTGCCATGACACCTATGGTCAA
GCCCTGACCAACACCTTGATGGCCCTGCAGATGGGAGTGAGTGTCGTGGACTCTTCTGTG
GCAGGACTTGGAGGCTGTCCCTACGCACAGGGGGCATCAGGAAACTTGGCCACAGAAGAC
CTGGTCTACATGCTAGAGGGCTTGGGCATTCACACGGGTGTGAATCTCCAGAAGCTTCTG
GAAGCTGGAAACTTTATCTGTCAAGCCCTGAACAGAAAAACTAGCTCCAAAGTGGCTCAG
GCTACCTGTAAACTCTGA
Enzyme 1 GenBank Gene ID L07033 Link Image
Enzyme 1 GeneCard ID HMGCL Link Image
Enzyme 1 GenAtlas ID HMGCL Link Image
Enzyme 1 HGNC ID HGNC:5005 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p36.1-p35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Mitchell GA, Robert MF, Hruz PW, Wang S, Fontaine G, Behnke CE, Mende-Mueller LM, Schappert K, Lee C, Gibson KM, et al.: 3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency. J Biol Chem. 1993 Feb 25;268(6):4376-81. [PubMed Link Image]
  2. Wang SP, Robert MF, Gibson KM, Wanders RJ, Mitchell GA: 3-Hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene (HMGCL) cloning and detection of large gene deletions in two unrelated HL-deficient patients. Genomics. 1996 Apr 1;33(1):99-104. [PubMed Link Image]
  3. Roberts JR, Mitchell GA, Miziorko HM: Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue. J Biol Chem. 1996 Oct 4;271(40):24604-9. [PubMed Link Image]
  4. Mitchell GA, Ozand PT, Robert MF, Ashmarina L, Roberts J, Gibson KM, Wanders RJ, Wang S, Chevalier I, Plochl E, Miziorko H: HMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q. Am J Hum Genet. 1998 Feb;62(2):295-300. [PubMed Link Image]
  5. Muroi J, Yorifuji T, Uematsu A, Shigematsu Y, Onigata K, Maruyama H, Nobutoki T, Kitamura A, Nakahata T: Molecular and clinical analysis of Japanese patients with 3-hydroxy-3-methylglutaryl CoA lyase (HL) deficiency. Hum Genet. 2000 Oct;107(4):320-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5530
Enzyme 2 Name Aldehyde dehydrogenase, mitochondrial precursor
Enzyme 2 Synonyms
  1. ALDH class 2
  2. ALDHI
  3. ALDH-E2
Enzyme 2 Gene Name ALDH2
Enzyme 2 Protein Sequence >Aldehyde dehydrogenase, mitochondrial precursor
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Enzyme 2 Number of Residues 517
Enzyme 2 Molecular Weight 56382
Enzyme 2 Theoretical pI 7.05
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function An aldehyde + NAD(+) + H(2)O = an acid + NADH
Enzyme 2 Pathways
Enzyme 2 Reactions
  • an aldehyde + NAD+ + H2O = an acid + NADH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-24
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28606 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P05091 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ALDH2_HUMAN Link Image
Enzyme 2 PDB ID 1OF7 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
Enzyme 2 GenBank Gene ID X05409 Link Image
Enzyme 2 GeneCard ID ALDH2 Link Image
Enzyme 2 GenAtlas ID ALDH2 Link Image
Enzyme 2 HGNC ID HGNC:404 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q24.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed Link Image]
  2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed Link Image]
  3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed Link Image]
  4. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed Link Image]
  5. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed Link Image]
  6. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed Link Image]
  7. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed Link Image]
  8. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed Link Image]
  9. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed Link Image]
  10. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed Link Image]
  11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5800
Enzyme 3 Name D-beta-hydroxybutyrate dehydrogenase, mitochondrial precursor
Enzyme 3 Synonyms
  1. BDH
  2. 3-hydroxybutyrate dehydrogenase
Enzyme 3 Gene Name BDH1
Enzyme 3 Protein Sequence >D-beta-hydroxybutyrate dehydrogenase, mitochondrial precursor
MLATRLSRPLSRLPGKTLSACDRENGARRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLV
TGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEV
EKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL
PLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN
FIAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTDTSPVID
AVTHALTATTPYTRYHPMDYYWWLRMQIMTHLPGAISDMIYIR
Enzyme 3 Number of Residues 343
Enzyme 3 Molecular Weight 38158
Enzyme 3 Theoretical pI 9.24
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 177198 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q02338 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name BDH_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1032 bp
GGCCTGCGGCCTCCGCCACCCGGACGCTTCTCACGGCTCCCAGGAAAAACCCTAAGTGCC
TGTGATAGAGAAAATGGAGCAAGACGCCCACTATTGCTTGGTTCTACTTCCTTTATCCCG
ATTGGCCGTCGGACTTATGCCAGTGCGGCGGAGCCGGTTGGCAGCAAAGCTGTCCTGGTC
ACAGGCTGTGACTCTGGATTTGGGTTCTCATTGGCCAAGCATCTGCATTCAAAAGGCTTC
CTTGTGTTTGCTGGCTGCTTGATGAAGGACAAAGGCCATGATGGGGTCAAGGAGCTGGAC
AGCCTAAACAGTGACCGATTGAGAACCGTCCAGCTCAATGTCTTCAGAAGCGAAGAGGTG
GAGAAAGTGGTGGGAGATTGTCCGTTCGAGCCTGAAGGACCTGAGAAAGGCATGTGGGGG
CTCGTTAACAATGCCGGCATCTCAACGTTCGGGGAGGTGGAGTTCACCAGCCTGGAGACC
TACAAGCAGGTGGCAGAAGTGAACCTTTGGGGCACAGTGCGGATGACGAAATCCTTTCTC
CCCCTCATCCGAAGGGCCAAAGGCCGCGTCGTCAATATCAGCAGCATGCTGGGCCGCATG
GCCAACCCGGCCCGCTCCCCGTACTGCATCACCAAGTTCGGGGTAGAGGCTTTCTCGGAC
TGCCTGCGCTATGAGATGTACCCCCTGGGCGTGAAGGTCAGCGTGGTGGAGCCCGGCAAC
TTCATCGCTGCCACCAGCCTTTACAACCCTGAGAGCATTCAGGCCATCGCCAAGAAGATG
TGGGAGGAGCTGCCTGAGGTCGTGCGCAAGGACTACGGCAAGAAGTACTTTGATGAAAAG
ATCGCCAAGATGGAGACCTACTGCAGCAGTGGCTCCACAGACACGTCCCCTGTCATCGAT
GCTGTCACACACGCCCTGACCGCCACCACCCCCTACACCCGCTACCACCCCATGGACTAC
TACTGGTGGCTGCGAATGCAGATCATGACCCACTTGCCTGGAGCCATCTCCGACATGATC
TACATCCGCTGA
Enzyme 3 GenBank Gene ID M93107 Link Image
Enzyme 3 GeneCard ID BDH1 Link Image
Enzyme 3 GenAtlas ID BDH1 Link Image
Enzyme 3 HGNC ID HGNC:1027 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3q29
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Marks AR, McIntyre JO, Duncan TM, Erdjument-Bromage H, Tempst P, Fleischer S: Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. J Biol Chem. 1992 Aug 5;267(22):15459-63. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5985
Enzyme 4 Name Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor
Enzyme 4 Synonyms
  1. Somatic-type succinyl CoA:3-oxoacid CoA- transferase
  2. Scot-S
Enzyme 4 Gene Name OXCT1
Enzyme 4 Protein Sequence >Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor
MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVL
VGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENA
EFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSV
AIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAET
TVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDD
VRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEAD
ADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMV
KGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDK
KKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN
Enzyme 4 Number of Residues 520
Enzyme 4 Molecular Weight 56158
Enzyme 4 Theoretical pI 7.52
Enzyme 4 GO Classification
Function
  • CoA-transferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Lipid transport and metabolism
Enzyme 4 Specific Function Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate
Enzyme 4 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 4 Reactions
  • succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-22
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1519052 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P55809 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SCOT_HUMAN Link Image
Enzyme 4 PDB ID 1OOY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1563 bp
ATGGCGGCTCTCAAACTCCTCTCCTCCGGGCTTCGGCTCTGCGCCTCTGCCCGCGGATCT
GGGGCAACCTGGTACAAGGGATGTGTTTGTTCCTTTTCCACCAGTGCTCATCGCCATACC
AAGTTTTATACAGATCCAGTAGAAGCTGTAAAAGACATCCCTGATGGTGCCACGGTTTTG
GTTGGTGGTTTTGGGCTATGTGGAATTCCAGAGAATCTTATAGATGCTTTACTGAAAACT
GGAGTAAAAGGACTAACTGCAGTCAGCAACAATGCAGGGGTTGACAATTTTGGTTTGGGG
CTTTTGCTTCGGTCGAAGCAGATAAAACGCATGGTCTCTTCATATGTGGGAGAAAATGCA
GAATTTGAACGACAGTACTTATCTGGTGAATTAGAAGTGGAGCTGACACCACAGGGCACA
CTTGCAGAGAGGATCCGTGCAGGCGGGGCTGGAGTTCCTGCATTTTACACCCCAACAGGG
TATGGGACCCTGGTACAAGAAGGAGGATCGCCCATCAAATACAACAAAGATGGCAGTGTT
GCCATTGCCAGTAAGCCAAGAGAGGTGAGGGAGTTCAATGGTCAGCACTTTATTTTGGAG
GAAGCAATTACAGGGGATTTTGCTTTGGTGAAAGCCTGGAAGGCGGACCGAGCAGGAAAC
GTGATTTTCAGGAAAAGTGCAAGGAATTTCAACTTGCCAATGTGCAAAGCTGCAGAAACC
ACAGTGGTAGAGGTTGAAGAAATTGTGGATATTGGAGCATTTGCTCCAGAAGACATCCAT
ATTCCTCAGATTTATGTACATCGCCTTATAAAGGGAGAAAAATATGAGAAAAGAATTGAG
CGTTTATCAATCCGGAAAGAGGGAGATGGGGAAGCCAAATCTGCTAAACCTGGAGATGAC
GTAAGGGAACGAATCATCAAGAGGGCCGCTCTTGAGTTTGAGGATGGCATGTATGCTAAT
TTGGGCATAGGAATCCCTCTCCTGGCCAGCAATTTTATCAGCCCAAATATAACTGTTCAT
CTTCAAAGTGAAAATGGAGTTCTGGGTTTGGGTCCATATCCACGACAACATGAAGCTGAT
GCAGATCTCATCAATGCAGGCAAGGAAACAGTTACTATTCTTCCAGGAGCCTCTTTTTTC
TCCAGCGATGAATCATTTGCAATGATTAGAGGTGGACACGTCGATCTGACAATGCTAGGA
GCGATGCAGGTTTCCAAATATGGTGACCTGGCTAACTGGATGATACCTGGGAAGATGGTG
AAAGGAATGGGAGGTGCTATGGATTTAGTGTCCAGTGCGAAAACCAAAGTGGTGGTCACC
ATGGAGCATTCTGCAAAGGGAAATGCACATAAAATCATGGAGAAATGTACATTACCATTG
ACTGGAAAGCAATGTGTCAACCGCATTATTACTGAAAAGGCTGTGTTTGATGTGGACAAG
AAGAAAGGGTTGACTCTGATTGAGCTCTGGGAAGGCCTGACAGTGGATGACGTACAAAAG
AGTACTGGGTGTGATTTTGCAGTTTCACCAAAACTCATGCCAATGCAGCAGATCGCAAAT
TGA
Enzyme 4 GenBank Gene ID U62961 Link Image
Enzyme 4 GeneCard ID OXCT1 Link Image
Enzyme 4 GenAtlas ID OXCT1 Link Image
Enzyme 4 HGNC ID HGNC:8527 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5p13.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kassovska-Bratinova S, Fukao T, Song XQ, Duncan AM, Chen HS, Robert MF, Perez-Cerda C, Ugarte M, Chartrand C, Vobecky S, Kondo N, Mitchell GA: Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient. Am J Hum Genet. 1996 Sep;59(3):519-28. [PubMed Link Image]
  2. Fukao T, Mitchell GA, Song XQ, Nakamura H, Kassovska-Bratinova S, Orii KE, Wraith JE, Besley G, Wanders RJ, Niezen-Koning KE, Berry GT, Palmieri M, Kondo N: Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. Genomics. 2000 Sep 1;68(2):144-51. [PubMed Link Image]
  3. Song XQ, Fukao T, Watanabe H, Shintaku H, Hirayama K, Kassovska-Bratinova S, Kondo N, Mitchell GA: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings. Hum Mutat. 1998;12(2):83-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5986
Enzyme 5 Name Fumarylacetoacetase
Enzyme 5 Synonyms
  1. Fumarylacetoacetate hydrolase
  2. Beta-diketonase
  3. FAA
Enzyme 5 Gene Name FAH
Enzyme 5 Protein Sequence >Fumarylacetoacetase
MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQD
VFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPAT
IGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQM
KPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLS
VNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFG
SMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS
Enzyme 5 Number of Residues 419
Enzyme 5 Molecular Weight 46375
Enzyme 5 Theoretical pI 6.94
Enzyme 5 GO Classification
Function
  • catalytic activity
  • fumarylacetoacetase activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function 4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 4-fumarylacetoacetate + H2O = acetoacetate + fumarate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 182393 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P16930 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name FAAA_HUMAN Link Image
Enzyme 5 PDB ID 1QQJ Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1260 bp
ATGTCCTTCATCCCGGTGGCCGAGGATTCCGACTTCCCCATCCACAACCTGCCCTACGGC
GTCTTCTCGACCAGAGGCGACCCAAGACCGAGGATAGGTGTGGCCATTGGCGACCAGATC
CTGGACCTCAGCATCATCAAGCACCTCTTTACTGGTCCTGTCCTCTCCAAACACCAGGAT
GTCTTCAATCAGCCTACACTCAACAGCTTCATGGGCCTGGGTCAGGCTGCCTGGAAGGAG
GCGAGAGTGTTCTTGCAGAACTTGCTGTCTGTGAGCCAAGCCAGGCTCAGAGATGACACC
GAACTTCGGAAGTGTGCATTCATCTCCCAGGCTTCTGCCACGATGCACCTTCCAGCCACC
ATAGGAGACTACACAGACTTCTATTCCTCTCGGCAGCATGCTACCAACGTCGGAATCATG
TTCAGGGACAAGGAGAATGCGTTGATGCCAAATTGGCTGCACTTACCAGTGGGCTACCAT
GGCCGTGCCTCCTCTGTCGTGGTGTCTGGCACCCCAATCCGAAGGCCCATGGGACAGATG
AAACCTGATGACTCTAAGCCTCCCGTATATGGTGCCTGCAAGCTCTTGGACATGGAGCTG
GAAATGGCTTTTTTTGTAGGCCCTGGAAACAGATTGGGAGAGCCGATCCCCATTTCCAAG
GCCCATGAGCACATTTTTGGAATGGTCCTTATGAACGACTGGAGTGCACGAGACATTCAG
AAGTGGGAGTATGTCCCTCTCGGGCCATTCCTTGGGAAGAGTTTTGGGACCACTGTCTCT
CCGTGGGTGGTGCCCATGGATGCTCTCATGCCCTTTGCTGTGCCCAACCCGAAGCAGGAC
CCCAGGCCCCTGCCGTATCTGTGCCATGACGAGCCCTACACATTTGACATCAACCTCTCT
GTTAACCTGAAAGGAGAAGGAATGAGCCAGGCGGCTACCATATGCAAGTCCAATTTTAAG
TACATGTACTGGACGATGCTGCAGCAGCTCACTCACCACTCTGTCAACGGCTGCAACCTG
CGGCCGGGGGACCTCCTGGCTTCTGGGACCATCAGCGGGCCGGAGCCAGAAAACTTCGGC
TCCATGTTGGAACTGTCGTGGAAGGGAACGAAGCCCATAGACCTGGGGAATGGTCAGACC
AGGAAGTTTCTGCTGGACGGGGATGAAGTCATCATAACAGGGTACTGCCAGGGGGATGGT
TACCGCATCGGCTTTGGCCAGTGTGCTGGAAAAGTGCTGCCTGCTCTCCTGCCATCATGA
Enzyme 5 GenBank Gene ID M55150 Link Image
Enzyme 5 GeneCard ID FAH Link Image
Enzyme 5 GenAtlas ID FAH Link Image
Enzyme 5 HGNC ID HGNC:3579 Link Image
Enzyme 5 Chromosome Location 15
Enzyme 5 Locus 15q23-q25
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Phaneuf D, Labelle Y, Berube D, Arden K, Cavenee W, Gagne R, Tanguay RM: Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15. Am J Hum Genet. 1991 Mar;48(3):525-35. [PubMed Link Image]
  2. Agsteribbe E, van Faassen H, Hartog MV, Reversma T, Taanman JW, Pannekoek H, Evers RF, Welling GM, Berger R: Nucleotide sequence of cDNA encoding human fumarylacetoacetase. Nucleic Acids Res. 1990 Apr 11;18(7):1887. [PubMed Link Image]
  3. Bergeron A, D'Astous M, Timm DE, Tanguay RM: Structural and functional analysis of missense mutations in fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia type 1. J Biol Chem. 2001 May 4;276(18):15225-31. Epub 2001 Jan 22. [PubMed Link Image]
  4. St-Louis M, Tanguay RM: Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview. Hum Mutat. 1997;9(4):291-9. [PubMed Link Image]
  5. Phaneuf D, Lambert M, Laframboise R, Mitchell G, Lettre F, Tanguay RM: Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. J Clin Invest. 1992 Oct;90(4):1185-92. [PubMed Link Image]
  6. Labelle Y, Phaneuf D, Leclerc B, Tanguay RM: Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity. Hum Mol Genet. 1993 Jul;2(7):941-6. [PubMed Link Image]
  7. Grompe M, al-Dhalimy M: Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I. Hum Mutat. 1993;2(2):85-93. [PubMed Link Image]
  8. Rootwelt H, Berger R, Gray G, Kelly DA, Coskun T, Kvittingen EA: Novel splice, missense, and nonsense mutations in the fumarylacetoacetase gene causing tyrosinemia type 1. Am J Hum Genet. 1994 Oct;55(4):653-8. [PubMed Link Image]
  9. Rootwelt H, Brodtkorb E, Kvittingen EA: Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I. Am J Hum Genet. 1994 Dec;55(6):1122-7. [PubMed Link Image]
  10. Rootwelt H, Chou J, Gahl WA, Berger R, Coskun T, Brodtkorb E, Kvittingen EA: Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase. Hum Genet. 1994 Jun;93(6):615-9. [PubMed Link Image]
  11. St-Louis M, Poudrier J, Phaneuf D, Leclerc B, Laframboise R, Tanguay RM: Two novel mutations involved in hereditary tyrosinemia type I. Hum Mol Genet. 1995 Feb;4(2):319-20. [PubMed Link Image]
  12. Hahn SH, Krasnewich D, Brantly M, Kvittingen EA, Gahl WA: Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1. Hum Mutat. 1995;6(1):66-73. [PubMed Link Image]
  13. Ploos van Amstel JK, Bergman AJ, van Beurden EA, Roijers JF, Peelen T, van den Berg IE, Poll-The BT, Kvittingen EA, Berger R: Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. Hum Genet. 1996 Jan;97(1):51-9. [PubMed Link Image]
  14. Bergman AJ, van den Berg IE, Brink W, Poll-The BT, Ploos van Amstel JK, Berger R: Spectrum of mutations in the fumarylacetoacetate hydrolase gene of tyrosinemia type 1 patients in northwestern Europe and Mediterranean countries. Hum Mutat. 1998;12(1):19-26. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5988
Enzyme 6 Name Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor
Enzyme 6 Synonyms
  1. Testis-specific succinyl CoA:3-oxoacid CoA- transferase
  2. SCOT-t
Enzyme 6 Gene Name OXCT2
Enzyme 6 Protein Sequence >Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor
MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVM
IGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENT
LCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHL
ALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADV
TAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDART
RIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADL
INAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGM
GGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKE
LTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP
Enzyme 6 Number of Residues 517
Enzyme 6 Molecular Weight 56141
Enzyme 6 Theoretical pI 7.15
Enzyme 6 GO Classification
Function
  • CoA-transferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate
Enzyme 6 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 6 Reactions
  • succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-21
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 118026874 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BYC2 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SCOT2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1554 bp
ATGGCGGCGCTGCGGCTCCTGGCGTCAGTGCTCGGGCGCGGGGTCCCCGCCGGCGGCTCA
GGGCTCGCGCTGTCCCAGGGCTGCGCCCGCTGCTTTGCCACCAGTCCCCGGCTCCGTGCC
AAGTTCTACGCGGACCCGGTGGAGATGGTGAAGGACATCTCTGACGGGGCGACCGTCATG
ATCGGGGGCTTCGGGCTCTGCGGGATCCCCGAGAACCTGATCGCCGCGCTGCTCAGGACC
CGCGTGAAAGACCTGCAGGTGGTCAGCAGCAACGTGGGCGTGGAGGACTTCGGCCTGGGC
CTCCTGCTGGCCGCCAGGCAGGTCCGTCGCATCGTCTGTTCCTACGTGGGCGAGAACACC
CTGTGCGAGAGCCAGTACCTGGCAGGAGAGCTGGAGCTGGAGCTCACGCCCCAGGGCACC
CTGGCCGAGCGCATCCGCGCGGGGGGCGCCGGGGTGCCCGCCTTCTACACCCCCACGGGC
TACGGGACCCTGGTCCAGGAAGGGGGCGCCCCCATCCGCTACACCCCGGACGGCCACCTG
GCGCTCATGAGCCAGCCCCGAGAGGTGAGGGAGTTCAACGGCGACCACTTCCTTTTGGAG
CGCGCCATCCGGGCAGACTTCGCCCTGGTGAAAGGGTGGAAGGCCGACCGGGCAGGAAAC
GTGGTCTTCAGGAGAAGCGCCCGCAATTTCAACGTGCCCATGTGCAAAGCTGCAGACGTC
ACGGCGGTGGAGGTGGAAGAGATCGTGGAGGTGGGGGCTTTCCCCCCAGAAGACATCCAC
GTTCCTAACATTTATGTAGATCGCGTGATAAAGGGGCAGAAATACGAGAAACGAATTGAG
CGCTTAACGATCCTGAAAGAGGAAGATGGAGACGCTGGAAAGGAAGAGGACGCCAGGACG
CGCATCATCAGACGCGCAGCTCTGGAATTTGAGGACGGCATGTACGCCAATCTGGGCATA
GGCATCCCCCTGCTGGCCAGCAACTTCATCAGTCCCAGCATGACTGTCCATCTTCACAGT
GAGAACGGGATCCTGGGCCTGGGCCCGTTTCCCACGGAAGATGAGGTGGATGCCGACCTC
ATCAATGCAGGCAAGCAGACGGTCACGGTGCTTCCCGGGGGCTGCTTCTTCGCCAGCGAC
GACTCCTTCGCCATGATCCGAGGGGGACACATCCAACTAACCATGCTTGGAGCCATGCAG
GTTTCCAAATACGGCGACCTGGCGAACTGGATGATCCCTGGCAAGAAGGTGAAAGGCATG
GGCGGTGCCATGGACTTGGTGTCCAGTCAGAAGACCAGAGTGGTGGTCACCATGCAGCAC
TGCACAAAGGACAACACCCCCAAGATCATGGAGAAATGCACCATGCCGCTGACCGGGAAG
CGGTGCGTGGACCGCATCATCACCGAGAAGGCCGTGTTTGACGTGCACAGGAAGAAAGAG
CTGACGCTGAGGGAGCTCTGGGAGGGCCTGACGGTGGACGACATCAAAAAGAGCACGGGG
TGTGCCTTTGCTGTGTCCCCGAACCTCAGGCCCATGCAGCAGGTGGCACCCTGA
Enzyme 6 GenBank Gene ID AB050193 Link Image
Enzyme 6 GeneCard ID OXCT2 Link Image
Enzyme 6 GenAtlas ID OXCT2 Link Image
Enzyme 6 HGNC ID HGNC:18606 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p34
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 9419
Enzyme 7 Name Alcohol dehydrogenase iron-containing 1
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name ADHFE1
Enzyme 7 Protein Sequence >Alcohol dehydrogenase iron-containing 1
MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAV
TKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFM
EAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP
LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG
FDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRN
PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLS
VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGL
AAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY
Enzyme 7 Number of Residues 467
Enzyme 7 Molecular Weight 50308
Enzyme 7 Theoretical pI Not Available
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • 3,4-Dihydroxymandelaldehyde + H+ + Nicotinamide adenine dinucleotide - reduced <==> 3,4-Dihydroxyphenylethyleneglycol + Nicotinamide adenine dinucleotide
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 25989126 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q8IWW8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q8IWW8_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 AY033237 Link Image
Enzyme 7 GeneCard ID Not Available
Enzyme 7 GenAtlas ID ADHFE1 Link Image
Enzyme 7 HGNC ID HGNC:16354 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002 Oct;13(5):301-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 9698
Enzyme 8 Name Acetoacetyl-CoA synthetase
Enzyme 8 Synonyms
  1. Protein sur-5 homolog
Enzyme 8 Gene Name AACS
Enzyme 8 Protein Sequence >Acetoacetyl-CoA synthetase
MSKEERPGREEILECQVMWEPDSKKNTQMDRFRAAVGAACGLALESYDDLYHWSVESYSD
FWAEFWKFSGIVFSRVYDEVVDTSKGIADVPEWFKGSRLNYAENLLRHKENDRVALYIAR
EGKEEIVKVTFEELRQEVALFAAAMRKMGVKKGDRVVGYLPNSEHAVEAMLAAASIGAIW
SSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHNHMEKLQQVVKGLPDLKKVVVIP
YVSSRENIDLSKIPNSVFLDDFLATGTSEQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCM
VHSAGGTLIQHLKEHLLHGNMTSSDILLCYTTVGWMMWNWMVSLLATGAAMVLYDGSPLV
PTPNVLWDLVDRIGITVLVTGAKWLSVLEEKAMKPVETHSLQMLHTILSTGSPLKAQSYE
YVYRCIKSSILLGSISGGTDIISCFMGHNFSLPVYKGEIQARNLGMAVEAWNEEGKAVWG
ESGELVCTKPIPCQPTHFWNDENGNKYRKAYFSKFPGIWAHGDYCRINPKTGGIVMLGRS
DGTLNPNGVRFGSSEIYNIVESFEEVEDSLCVPQYNKYREERVILFLKMASGHAFQPDLV
KRIRDAIRMGLSARHVPSLILETKGIPYTLNGKKVEVAVKQIIAGKAVEQGGAFSNPETL
DLYRDIPELQGF
Enzyme 8 Number of Residues 672
Enzyme 8 Molecular Weight 75145
Enzyme 8 Theoretical pI Not Available
Enzyme 8 GO Classification
Function
  • CoA-ligase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
Enzyme 8 General Function Lipid transport and metabolism
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways
Enzyme 8 Reactions
  • Acetoacetate + ATP + Coenzyme A <==> Acetoacetyl-CoA + AMP + Diphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 30354006 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q86V21 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q86V21_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID BC051862 Link Image
Enzyme 8 GeneCard ID Not Available
Enzyme 8 GenAtlas ID AACS Link Image
Enzyme 8 HGNC ID HGNC:21298 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
  2. Ohgami M, Takahashi N, Yamasaki M, Fukui T: Expression of acetoacetyl-CoA synthetase, a novel cytosolic ketone body-utilizing enzyme, in human brain. Biochem Pharmacol. 2003 Mar 15;65(6):989-94. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 10586
Enzyme 9 Name 3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name HMGCLL1
Enzyme 9 Protein Sequence >3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1
MGNVPSAVKHCLSYQQLLREHLWIGDSVAGALDPAQETSQLSGLPEFVKIVEVGPRDGLQ
NEKVIVPTDIKIEFINRLSQTGLSVIEVTSFVSSRWVPQMADHTEVMKGIHQYPGVRYPV
LTPNLQGFHHAVAAGATEISVFGAASESFSKKNINCSIEESMGKFEEVVKSARHMNIPAR
GYVSCALGCPYEGSITPQKVTEVSKRLYGMGCYEISLGDTIGVGTPGSMKRMLESVMKEI
PPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYML
NGLGLNTGVNLYKVMEAGDFICKAVNKTTNSKVAQASFNA
Enzyme 9 Number of Residues 340
Enzyme 9 Molecular Weight 36328
Enzyme 9 Theoretical pI Not Available
Enzyme 9 GO Classification
Function
  • catalytic activity
Process
Component
Enzyme 9 General Function Amino acid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • Hydroxymethylglutaryl-CoA --> Acetoacetate + Acetyl-CoA
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 34190590 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q8TB92 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q8TB92_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID BC024194 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID HMGCLL1 Link Image
Enzyme 9 HGNC ID HGNC:21359 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 12878
Enzyme 10 Name 3-hydroxybutyrate dehydrogenase type 2
Enzyme 10 Synonyms
  1. R-beta- hydroxybutyrate dehydrogenase
  2. Dehydrogenase/reductase SDR family member 6
  3. Oxidoreductase UCPA
Enzyme 10 Gene Name BDH2
Enzyme 10 Protein Sequence >3-hydroxybutyrate dehydrogenase type 2
MGRLDGKVIILTAAAQGIGQAAALAFAREGAKVIATDINESKLQELEKYPGIQTRVLDVT
KKKQIDQFANEVERLDVLFNVAGFVHHGTVLDCEEKDWDFSMNLNVRSMYLMIKAFLPKM
LAQKSGNIINMSSVASSVKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTV
DTPSLQERIQARGNPEEARNDFLKRQKTGRFATAEEIAMLCVYLASDESAYVTGNPVIID
GGWSL
Enzyme 10 Number of Residues 245
Enzyme 10 Molecular Weight 26724
Enzyme 10 Theoretical pI Not Available
Enzyme 10 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Lipid transport and metabolism
Enzyme 10 Specific Function (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH
Enzyme 10 Pathways
Enzyme 10 Reactions
  • (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+ [RN:R01361] ALL_REAC R01361
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 8895083 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9BUT1 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name BDH2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AF164790 Link Image
Enzyme 10 GeneCard ID Not Available
Enzyme 10 GenAtlas ID BDH2 Link Image
Enzyme 10 HGNC ID HGNC:32389 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16468
Enzyme 11 Name cDNA, FLJ94596, Homo sapiens fumarylacetoacetate hydrolase (fumarylacetoacetase)(FAH), mRNA (Fumarylacetoacetate hydrolase (Fumarylacetoacetase), isoform CRA_a)
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name FAH
Enzyme 11 Protein Sequence >cDNA, FLJ94596, Homo sapiens fumarylacetoacetate hydrolase (fumarylacetoacetase)(FAH), mRNA (Fumarylacetoacetate hydrolase (Fumarylacetoacetase), isoform CRA_a)
MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQD
VFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPAT
IGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQM
KPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLS
VNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFG
SMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS
Enzyme 11 Number of Residues 419
Enzyme 11 Molecular Weight 46375
Enzyme 11 Theoretical pI 6.94
Enzyme 11 GO Classification
Function
  • catalytic activity
  • fumarylacetoacetase activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
Enzyme 11 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B2R9X1 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2R9X1_HUMAN Link Image
Enzyme 11 PDB ID 1QQJ Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK313951 Link Image
Enzyme 11 GeneCard ID B2R9X1 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location 15
Enzyme 11 Locus 15q23-q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available