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Human Metabolome Database Version 2.5

 

Showing metabocard for Ketoleucine (HMDB00695)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-31 16:48:00
Accession Number HMDB00695
Secondary Accession Numbers HMDB00762
Common Name Ketoleucine
Description Ketoleucine is a metabolite that accumulates in Maple Syrup Urine Disease (MSUD) and shown to compromise brain energy metabolism by blocking the respiratory chain; this is of relevance to the understanding of the pathophysiology of the neurological dysfunction of MSUD patients. (PMID 14636955)
Synonyms
  1. 2-Ketoisocaproate
  2. 2-Ketoisocaproic acid
  3. 2-Oxo-4-methylpentanoate
  4. 2-Oxo-4-methylpentanoic acid
  5. 2-Oxo-4-methylvalerate
  6. 2-Oxo-4-methylvaleric acid
  7. 2-Oxoisocaproate
  8. 2-Oxoisocaproic acid
  9. 2-Oxoleucine
  10. 2-keto-4-Methylvalerate
  11. 2-keto-4-Methylvaleric acid
  12. 4-Methyl-2-oxopentanoate
  13. 4-Methyl-2-oxopentanoic acid
  14. 4-methyl-2-oxo-Valerate
  15. 4-methyl-2-oxo-Valeric acid
  16. Methyloxovalerate
  17. Methyloxovaleric acid
  18. a-Ketoisocaproate
  19. a-Ketoisocaproic acid
  20. a-Ketoisocapronate
  21. a-Ketoisocapronic acid
  22. a-Oxoisocaproate
  23. a-Oxoisocaproic acid
  24. alpha-keto-isocaproic acid
  25. alpha-ketoisocaproate
  26. ketoisocaproate
  27. oxoisocaproate
  28. alpha-Ketoisocaproic acid
  29. alpha-Ketoisocapronate
  30. alpha-Ketoisocapronic acid
  31. alpha-Oxoisocaproate
  32. alpha-Oxoisocaproic acid
  33. alpha-keto-isocaproate
  34. ketoisocaproic acid
  35. oxoisocaproic acid
Chemical IUPAC Name 4-methyl-2-oxopentanoic 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
  • Component of Pantothenate and CoA biosynthesis
  • Component of Valine, leucine and isoleucine biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 130.142
Monoisotopic Molecular Weight 130.062988
Isomeric SMILES CC(C)CC(=O)C(O)=O
Canonical SMILES CC(C)CC(=O)C(O)=O
KEGG Compound ID Not Available
BioCyc ID 2K-4CH3-PENTANOATE Link Image
BiGG ID 34334 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00695 Link Image
Metagene Link HMDB00695 Link Image
METLIN ID 5663 Link Image
PubChem Compound 70 Link Image
PubChem Substance 10342986 Link Image
ChEBI ID Not Available
CAS Registry Number 816-66-0
InChI Identifier InChI=1/C6H10O3/c1-4(2)3-5(7)6(8)9/h4H,3H2,1-2H3,(H,8,9)
Synthesis Reference Tabuchi, Takeshi; Abe, Matazo. Fermentative preparation of a-ketoisocaproic acid. Jpn. Tokkyo Koho (1970), 3 pp.
Melting Point (Experimental) 8-10 oC
Experimental Water Solubility 32 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 6.76 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.9 [Predicted by PubChem via XLOGP]; 0.82 [Predicted by ALOGPS] 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 1DXY 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 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
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Muscle
Neuron
Concentrations (Normal)
Biofluid Blood
Value 33.5 +/- 8.2 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 28.0 (0.0-58.0) 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 5.0 +/- 4.4 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 0.13 (0.02-0.45) 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 0.13 (0.03-0.34) 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) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Valine, Leucine and Isoleucine Degradation SMP00032 Link Image map00280 Link Image
General References
  1. Chow LS, Albright RC, Bigelow ML, Toffolo G, Cobelli C, Nair KS: Mechanism of insulin's anabolic effect on muscle: measurements of muscle protein synthesis and breakdown using aminoacyl-tRNA and other surrogate measures. Am J Physiol Endocrinol Metab. 2006 Oct;291(4):E729-36. Epub 2006 May 16. [PubMed Link Image]
  2. Wang Y, Holmes E, Nicholson JK, Cloarec O, Chollet J, Tanner M, Singer BH, Utzinger J: Metabonomic investigations in mice infected with Schistosoma mansoni: an approach for biomarker identification. Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12676-81. Epub 2004 Aug 16. [PubMed Link Image]
  3. Mitch WE, Walser M, Sapir DG: Nitrogen sparing induced by leucine compared with that induced by its keto analogue, alpha-ketoisocaproate, in fasting obese man. J Clin Invest. 1981 Feb;67(2):553-62. [PubMed Link Image]
  4. Sgaravatti AM, Rosa RB, Schuck PF, Ribeiro CA, Wannmacher CM, Wyse AT, Dutra-Filho CS, Wajner M: Inhibition of brain energy metabolism by the alpha-keto acids accumulating in maple syrup urine disease. Biochim Biophys Acta. 2003 Nov 20;1639(3):232-8. [PubMed Link Image]
  5. Yudkoff M, Daikhin Y, Nissim I, Horyn O, Luhovyy B, Lazarow A, Nissim I: Brain amino acid requirements and toxicity: the example of leucine. J Nutr. 2005 Jun;135(6 Suppl):1531S-8S. [PubMed Link Image]
  6. 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]
  7. Hachey DL, Patterson BW, Reeds PJ, Elsas LJ: Isotopic determination of organic keto acid pentafluorobenzyl esters in biological fluids by negative chemical ionization gas chromatography/mass spectrometry. Anal Chem. 1991 May 1;63(9):919-23. [PubMed Link Image]
Metabolic Enzymes
  1. 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
  2. Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 1 [top]
Enzyme 1 ID 5535
Enzyme 1 Name 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Enzyme 1 Synonyms
  1. Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
  2. BCKDE1A
  3. BCKDH E1-alpha
Enzyme 1 Gene Name BCKDHA
Enzyme 1 Protein Sequence >2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAE
FIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILY
ESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYG
NISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGA
ASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDG
NDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHP
ISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQL
RKQQESLARHLQTYGEHYPLDHFDK
Enzyme 1 Number of Residues 445
Enzyme 1 Molecular Weight 50470.6
Enzyme 1 Theoretical pI 8.41
Enzyme 1 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
  • metabolic process
Component
Enzyme 1 General Function Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
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 [RN:R01701]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 29391 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P12694 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ODBA_HUMAN Link Image
Enzyme 1 PDB ID 1U5B Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID Z14093 Link Image
Enzyme 1 GeneCard ID BCKDHA Link Image
Enzyme 1 GenAtlas ID BCKDHA Link Image
Enzyme 1 HGNC ID HGNC:986 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 19q13.1-q13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. 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. 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]
  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. FEBS Lett. 1991 Jun 17;284(1):34-8. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  10. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  11. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  12. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5536
Enzyme 2 Name Branched-chain-amino-acid aminotransferase, cytosolic
Enzyme 2 Synonyms
  1. BCAT(c)
  2. Protein ECA39
Enzyme 2 Gene Name BCAT1
Enzyme 2 Protein Sequence >Branched-chain-amino-acid aminotransferase, cytosolic
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
Enzyme 2 Number of Residues 386
Enzyme 2 Molecular Weight 42965.8
Enzyme 2 Theoretical pI 4.95
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
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 38176287 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P54687 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name BCAT1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID NM_005504.6 Link Image
Enzyme 2 GeneCard ID BCAT1 Link Image
Enzyme 2 GenAtlas ID BCAT1 Link Image
Enzyme 2 HGNC ID HGNC:976 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 12p12.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available