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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Methyl-2-oxovaleric acid (HMDB00491)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-09 10:45:23
Accession Number HMDB00491
Secondary Accession Numbers HMDB01962; HMDB02254; HMDB03736
Common Name 3-Methyl-2-oxovaleric acid
Description 3-Methyl-2-oxovaleric acid is a metabolite of isoleucine in man, animals and bacteria. It is the alpha-keto acid analogue of isoleucine. 3-Methyl-2-oxovaleric acid is produced from isoleucine by cytosolic branched chain aminotransferase 1 (EC:2.6.1.42), whereupon it is further degraded by branched chain keto acid dehydrogenase E1 to 2-Methyl-1-hydroxybutyl-ThPP. It is used as a clinical marker for maple syrup urine disease (MSUD). MSUD is caused by a deficiency of the branched-chain -keto acid dehydrogenase compex resulting in an accumulation of branched-chain amino acids and the corresponding -keto-and -hydroxy acids in blood, urine and cerebrospinal fluid causing neurological damage and mental retardation.
Synonyms
  1. (r)-3-methyl-2-oxopentanoate
  2. 2-Oxo-3-methyl-n-valerate
  3. 2-Oxo-3-methyl-n-valeric acid
  4. 2-Oxo-3-methylpentanoate
  5. 2-Oxo-3-methylpentanoic acid
  6. 2-Oxo-3-methylvalerate
  7. 2-Oxo-3-methylvaleric acid
  8. 2-Oxoisoleucine
  9. 2-oxokolavenate
  10. 2-oxokolavenic acid
  11. 3-Methyl-2-oxopentanoate
  12. 3-Methyl-2-oxopentanoic acid
  13. 3-Methyl-2-oxovalerate
  14. 3-Methyl-2-oxovaleric
  15. 3-methyl-2-oxo-Valerate
  16. 3-methyl-2-oxo-Valeric acid
  17. 3-methyl-2-oxo-pentanoate
  18. 3-methyl-2-oxo-pentanoic acid
  19. a-Keto-b-methylvalerate
  20. a-Keto-b-methylvaleric acid
  21. a-Oxo-b-methyl-n-valerate
  22. a-Oxo-b-methyl-n-valeric acid
  23. a-Oxo-b-methylvalerate
  24. a-Oxo-b-methylvaleric acid
  25. a-keto-b-Methyl-n-valerate
  26. a-keto-b-Methyl-n-valeric acid
  27. alpha-keto-beta-methylvaleric acid
  28. alpha-Keto-beta-methylvalerate
  29. alpha-Oxo-beta-methyl-n-valerate
  30. alpha-Oxo-beta-methyl-n-valeric acid
  31. alpha-Oxo-beta-methylvalerate
  32. alpha-Oxo-beta-methylvaleric acid
  33. alpha-keto-beta-Methyl-n-valerate
  34. alpha-keto-beta-Methyl-n-valeric acid
  35. (S)-3-methyl-2-oxopentanoic acid
  36. (S)-3-methyl-2-oxopentanoate
  37. (r)-3-methyl-2-oxopentanoic acid
  38. (3R)-3-Methyl-2-oxopentanoic acid
  39. (3R)-3-Methyl-2-oxopentanoate
Chemical IUPAC Name (3S)-3-methyl-2-oxo-pentanoic acid
Chemical Formula C6H10O3
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
  • Essential amino acid
Application
—
Source
  • Endogenous
Average Molecular Weight 130.142
Monoisotopic Molecular Weight 130.062988
Isomeric SMILES CCC(C)C(=O)C(O)=O
Canonical SMILES CCC(C)C(=O)C(O)=O
KEGG Compound ID C00671 Link Image
BioCyc ID 2-KETO-3-METHYL-VALERATE Link Image
BiGG ID 35662 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00491 Link Image
Metagene Link HMDB00491 Link Image
METLIN ID 5478 Link Image
PubChem Compound 439286 Link Image
PubChem Substance 3940 Link Image
ChEBI ID 15614 Link Image
CAS Registry Number 1460-34-0
InChI Identifier InChI=1/C6H10O3/c1-3-4(2)5(7)6(8)9/h4H,3H2,1-2H3,(H,8,9)
Synthesis Reference Kondo, Shigeo; Sudo, Tetsuji; Ogiwara, Mitsuo; Takeuchi, Hiroshi. a-Oxo-b-methyl-n-valeric acid and its salts. Jpn. Kokai Tokkyo Koho (1979), 3 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility 915.5 mg/mL [sodium salt, HMP experimental] Source: PhysProp
Predicted Water Solubility 9.86 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.00 [Predicted by ALOGPS]; 0.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 22.7 +/- 4.6 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 Blood
Value 18.0 (8.0-31.0) 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 CSF
Value 2.0 +/- 2.0 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 Urine
Value 0.24 (0.11 - 0.55) umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
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 0.54 (0.12 - 1.42) 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]
Concentrations (Abnormal)
Biofluid Blood
Value 142.0 +/- 9.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Maple syrup urine disease
Comments Not Available
References
  • Schadewaldt P, Hammen HW, Ott AC, Wendel U: Renal clearance of branched-chain L-amino and 2-oxo acids in maple syrup urine disease. J Inherit Metab Dis. 1999 Aug;22(6):706-22. [PubMed Link Image]
Biofluid Urine
Value 209.0 +/- 35.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Maple syrup urine disease
Comments Not Available
References
  • Schadewaldt P, Hammen HW, Ott AC, Wendel U: Renal clearance of branched-chain L-amino and 2-oxo acids in maple syrup urine disease. J Inherit Metab Dis. 1999 Aug;22(6):706-22. [PubMed Link Image]
Associated Disorders
Condition References
Maple syrup urine disease
  • Schadewaldt P, Hammen HW, Ott AC, Wendel U: Renal clearance of branched-chain L-amino and 2-oxo acids in maple syrup urine disease. J Inherit Metab Dis. 1999 Aug;22(6):706-22. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Wendel U, Even G, Langenbeck U, Schadewaldt P, Hummel W: Determination of (S)- and (R)-2-oxo-3-methylvaleric acid in plasma of patients with maple syrup urine disease. Clin Chim Acta. 1992 Jun 15;208(1-2):85-91. [PubMed Link Image]
  2. Przyrembel H, Bremer HJ, Duran M, Bruinvis L, Ketting D, Wadman SK, Baumgartner R, Irle U, Bachmann C: Propionyl-CoA carboxylase deficiency with overflow of metabolites of isoleucine catabolism at all levels. Eur J Pediatr. 1979 Jan 18;130(1):1-14. [PubMed Link Image]
Metabolic Enzymes
  1. 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial precursor
  2. 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial precursor
  3. Branched-chain-amino-acid aminotransferase, cytosolic
  4. cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
Enzyme 1 [top]
Enzyme 1 ID 5534
Enzyme 1 Name 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial precursor
Enzyme 1 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
  2. BCKDH E1-beta
Enzyme 1 Gene Name BCKDHB
Enzyme 1 Protein Sequence >2-oxoisovalerate dehydrogenase subunit beta, mitochondrial precursor 
MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDP
EPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVF
NTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEP
KILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRV
CGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
Enzyme 1 Number of Residues 392
Enzyme 1 Molecular Weight 43123
Enzyme 1 Theoretical pI 6.24
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 1 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-19
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 179362 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21953 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ODBB_HUMAN Link Image
Enzyme 1 PDB ID 1X80 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1179 bp 
ATGGCGGTTGTAGCGGCGGCTGCCGGCTGGCTACTCAGGCTCAGGGCGGCAGGGGCTGAG
GGGCACTGGCGTCGGCTTCCTGGCGCGGGGCTGGCGCGGGGCTTTTTGCACCCCGCCGCG
ACTGTCGAGGATGCGGCCCAGAGGCGGCAGGTGGCTCATTTTACTTTCCAGCCAGATCCG
GAGCCCCGGGAGTACGGGCAAACTCAGAAAATGAATCTTTTCCAGTCTGTAACAAGTGCC
TTGGATAACTCATTGGCCAAAGATCCTACTGCAGTAATATTTGGTGAAGATGTTGCCTTT
GGTGGAGTCTTTAGATGCACTGTTGGCTTGCGAGACAAATATGGAAAAGATAGAGTTTTT
AATACCCCATTGTGTGAACAAGGAATTGTTGGATTTGGAATCGGAATTGCGGTCACTGGA
GCTACTGCCATTGCGGAAATTCAGTTTGCAGATTATATTTTCCCTGCATTTGATCAGATT
GTTAATGAAGCTGCCAAGTATCGCTATCGCTCTGGGGATCTTTTTAACTGTGGAAGCCTC
ACTATCCGGTCCCCTTGGGGCTGTGTTGGTCATGGGGCTCTCTATCATTCTCAGAGTCCT
GAAGCATTTTTTGCCCATTGCCCAGGAATCAAGGTGGTTATACCCAGAAGCCCTTTCCAG
GCCAAAGGACTTCTTTTGTCATGCATAGAGGATAAAAATCCTTGTATATTTTTTGAACCT
AAAATACTTTACAGGGCAGCAGCGGAAGAAGTCCCTATAGAACCATACAACATCCCACTG
TCCCAGGCCGAAGTCATACAGGAAGGGAGTGATGTTACTCTAGTTGCCTGGGGCACTCAG
GTTCATGTGATCCGAGAGGTAGCTTCCATGGCAAAAGAAAAGCTTGGAGTGTCTTGTGAA
GTCATTGATCTGAGGACTATAATACCTTGGGATGTGGACACAATTTGTAAGTCTGTGATC
AAAACAGGGCGACTGCTAATCAGTCACGAGGCTCCCTTGACAGGCGGCTTTGCATCGGAA
ATCAGCTCTACAGTTCAGGAGGAATGTTTCTTGAACCTAGAGGCTCCTATATCAAGAGTA
TGTGGTTATGACACACCATTTCCTCACATTTTTGAACCATTCTACATCCCAGACAAATGG
AAGTGTTATGATGCCCTTCGAAAAATGATCAACTATTGA
Enzyme 1 GenBank Gene ID M55575 Link Image
Enzyme 1 GeneCard ID BCKDHB Link Image
Enzyme 1 GenAtlas ID BCKDHB Link Image
Enzyme 1 HGNC ID HGNC:987 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6q13-q15
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Nobukuni Y, Mitsubuchi H, Endo F, Akaboshi I, Asaka J, Matsuda I: Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease. J Clin Invest. 1990 Jul;86(1):242-7. [PubMed Link Image]
  2. Chuang JL, Cox RP, Chuang DT: Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am J Hum Genet. 1996 Jun;58(6):1373-7. [PubMed Link Image]
  3. Chuang JL, Cox RP, Chuang DT: Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1990 Mar 26;262(2):305-9. [PubMed Link Image]
  4. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  5. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5535
Enzyme 2 Name 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial precursor
Enzyme 2 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
  2. BCKDH E1-alpha
  3. BCKDE1A
Enzyme 2 Gene Name BCKDHA
Enzyme 2 Protein Sequence >2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial precursor 
MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAE
FIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILY
ESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYG
NISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGA
ASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDG
NDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHP
ISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQL
RKQQESLARHLQTYGEHYPLDHFDK
Enzyme 2 Number of Residues 445
Enzyme 2 Molecular Weight 50472
Enzyme 2 Theoretical pI 8.41
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components:branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 2 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 2 Reactions
  • 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-32
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 29391 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P12694 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ODBA_HUMAN Link Image
Enzyme 2 PDB ID 1U5B Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1338 bp 
ATGGCGGTAGCGATCGCTGCAGCGAGGGTCTGGCGGCTAAACCGTGGTTTGAGCCAGGCT
GCCCTCCTGCTGCTGCGGCAGCCTGGGGCTCGGGGACTGGCTAGATCTCACCCCCCCAGG
CAGCAGCAGCAGTTTTCATCTCTGGATGACAAGCCCCAGTTCCCAGGGGCCTCGGCGGAG
TTTATAGATAAGTTGGAATTCATCCAGCCCAACGTCATCTCTGGAATCCCCATCTACCGC
GTCATGGACCGGCAAGGCCAGATCATCAACCCCAGCGAGGACCCCCACCTGCCGAAGGAG
AAGGTGCTGAAGCTCTACAAGAGCATGACACTGCTTAACACCATGGACCGCATCCTCTAT
GAGTCTCAGCGGCAGGGCCGGATCTCCTTCTACATGACCAACTATGGTGAGGAGGGCACG
CACGTGGGGAGTGCCGCCGCCCTGGACAACACGGACCTGGTGTTTGGCCAGTACCGGGAG
GCAGGTGTGCTGATGTATCGGGACTACCCCCTGGAACTATTCATGGCCCAGTGCTATGGC
AACATCAGTGACTTGGGCAAGGGGCGCCAGATGCCTGTCCACTACGGCTGCAAGGAACGC
CACTTCGTCACTATCTCCTCTCCACTGGCCACGCAGATCCCTCAGGCGGTGGGGGCGGCG
TACGCAGCCAAGCGGGCCAATGCCAACAGGGTCGTCATCTGTTACTTCGGCGAGGGGGCA
GCCAGTGAGGGGGACGCCCATGCCGGCTTCAACTTCGCTGCCACACTTGAGTGCCCCATC
ATCTTCTTCTGCCGGAACAATGGCTACGCCATCTCCACGCCCACCTCTGAGCAGTATCGC
GGCGATGGCATTGCAGCACGAGGCCCCGGGTATGGCATCATGTCAATCCGCGTGGATGGT
AATGATGTGTTTGCCGTATACAACGCCACAAAGGAGGCCCGACGGCGGGCTGTGGCAGAG
AACCAGCCCTTTCTCATCGAGGCCATGACCTACAGGATCGGGCACCACAGCACCAGTGAC
GACAGTTCAGCGTACCGCTCGGTGGATGAGGTCAATTACTGGGATAAACAGGACCACCCC
ATCTCCCGGCTGCGGCACTATCTGCTGAGCCAAGGCTGGTGGGATGAGGAGCAGGAGAAG
GCCTGGAGGAAGCAGTCCCGCAGGAAGGTGATGGAGGCCTTTGAGCAGGCCGAGCGGAAG
CCCAAACCCAACCCCAACCTGCTCTTCTCAGACGTGTATCAGGAGATGCCCGCCCAGCTC
CGCAAGCAGCAGGAGTCTCTGGCCCGCCACCTGCAGACCTACGGGGAGCACTACCCACTG
GATCACTTCGATAAGTGA
Enzyme 2 GenBank Gene ID Z14093 Link Image
Enzyme 2 GeneCard ID BCKDHA Link Image
Enzyme 2 GenAtlas ID BCKDHA Link Image
Enzyme 2 HGNC ID HGNC:986 Link Image
Enzyme 2 Chromosome Location 19
Enzyme 2 Locus 19q13.1-q13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. McKean MC, Winkeler KA, Danner DJ: Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex. Biochim Biophys Acta. 1992 Nov 15;1171(1):109-12. [PubMed Link Image]
  2. Fisher CW, Chuang JL, Griffin TA, Lau KS, Cox RP, Chuang DT: Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex. J Biol Chem. 1989 Feb 25;264(6):3448-53. [PubMed Link Image]
  3. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1991 Jun 17;284(1):34-8. [PubMed Link Image]
  4. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex (1991) FEBS Letters 284, 34-38. FEBS Lett. 1991 Oct 21;291(2):376-7. [PubMed Link Image]
  5. Zhang B, Crabb DW, Harris RA: Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase. Gene. 1988 Sep 15;69(1):159-64. [PubMed Link Image]
  6. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed Link Image]
  7. AEvarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WG: Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure. 2000 Mar 15;8(3):277-91. [PubMed Link Image]
  8. Chuang JL, Fisher CR, Cox RP, Chuang DT: Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex. Am J Hum Genet. 1994 Aug;55(2):297-304. [PubMed Link Image]
  9. Zhang B, Edenberg HJ, Crabb DW, Harris RA: Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease. J Clin Invest. 1989 Apr;83(4):1425-9. [PubMed Link Image]
  10. Matsuda I, Nobukuni Y, Mitsubuchi H, Indo Y, Endo F, Asaka J, Harada A: A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients. Biochem Biophys Res Commun. 1990 Oct 30;172(2):646-51. [PubMed Link Image]
  11. Fisher CR, Fisher CW, Chuang DT, Cox RP: Occurrence of a Tyr393----Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population. Am J Hum Genet. 1991 Aug;49(2):429-34. [PubMed Link Image]
  12. Fisher CR, Chuang JL, Cox RP, Fisher CW, Star RA, Chuang DT: Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex. J Clin Invest. 1991 Sep;88(3):1034-7. [PubMed Link Image]
  13. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed Link Image]
  14. Chuang JL, Davie JR, Chinsky JM, Wynn RM, Cox RP, Chuang DT: Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patients. J Clin Invest. 1995 Mar;95(3):954-63. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5536
Enzyme 3 Name Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 3 Synonyms
  1. BCAT(c
  2. ECA39 protein
Enzyme 3 Gene Name BCAT1
Enzyme 3 Protein Sequence >Branched-chain-amino-acid aminotransferase, cytosolic 
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLSTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
Enzyme 3 Number of Residues 386
Enzyme 3 Molecular Weight 42953
Enzyme 3 Theoretical pI 4.95
Enzyme 3 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 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine
Enzyme 3 Pathways
  • Pantothenate and CoA Biosynthesis (map00770 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 3 Reactions
  • L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1036780 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P54687 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name BCAT1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1155 bp 
ATGGATTGCAGTAACGGATCGGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAGGTGGTG
GGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAAAAACCA
GACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTGGAGTGG
TCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCATTGCAC
CCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCATTTCGA
GGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATGTATCGC
TCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGTATTCAA
CAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTGTATATT
CGTCCTGCATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAAGCCCTG
CTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAATCCAGTG
TCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGACTGCAAG
ATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGACGTAGATAATGGGTGT
CAGCAGGTCCTGTGGCTCTATGGCAGAGACCATCAGATCACTGAAGTGGGAACTATGAAT
CTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCACTAGAT
GGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAGTGGGGT
GAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTGGAGGGG
AACAGAGTGAGAGAGATGTTTAGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTTTCTGAT
ATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAGCTGGCA
AGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGACTGGACA
ATTGTGCTATCCTGA
Enzyme 3 GenBank Gene ID U21551 Link Image
Enzyme 3 GeneCard ID BCAT1 Link Image
Enzyme 3 GenAtlas ID BCAT1 Link Image
Enzyme 3 HGNC ID HGNC:976 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12pter-q12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16424
Enzyme 4 Name cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name BCAT2
Enzyme 4 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 4 Number of Residues 392
Enzyme 4 Molecular Weight 44288
Enzyme 4 Theoretical pI 8.82
Enzyme 4 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 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
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 B2RB87 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2RB87_HUMAN Link Image
Enzyme 4 PDB ID 1KTA Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK314548 Link Image
Enzyme 4 GeneCard ID B2RB87 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 19
Enzyme 4 Locus 19q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available