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'''2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''BCKDHA'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCKDHA branched chain keto acid dehydrogenase E1, alpha polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=593| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_BCKDHA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dtw.
| PDB = {{PDB2|1dtw}}, {{PDB2|1ols}}, {{PDB2|1olu}}, {{PDB2|1olx}}, {{PDB2|1u5b}}, {{PDB2|1v11}}, {{PDB2|1v16}}, {{PDB2|1v1m}}, {{PDB2|1v1r}}, {{PDB2|1wci}}, {{PDB2|1x7w}}, {{PDB2|1x7x}}, {{PDB2|1x7y}}, {{PDB2|1x7z}}, {{PDB2|1x80}}, {{PDB2|2beu}}, {{PDB2|2bev}}, {{PDB2|2bew}}, {{PDB2|2bfb}}, {{PDB2|2bfc}}, {{PDB2|2bfd}}, {{PDB2|2bfe}}, {{PDB2|2bff}}, {{PDB2|2j9f}}
| Name = Branched chain keto acid dehydrogenase E1, alpha polypeptide
| HGNCid = 986
| Symbol = BCKDHA
| AltSymbols =; FLJ45695; MSU; MSUD1
| OMIM = 608348
| ECnumber = 
| Homologene = 569
| MGIid = 107701
| Function = {{GNF_GO|id=GO:0003826 |text = alpha-ketoacid dehydrogenase activity}} {{GNF_GO|id=GO:0003863 |text = 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016624 |text = oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor}} {{GNF_GO|id=GO:0016831 |text = carboxy-lyase activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005947 |text = mitochondrial alpha-ketoglutarate dehydrogenase complex}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009083 |text = branched chain family amino acid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 593
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_000700
    | Hs_RefseqmRNA = NM_000709
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 12039
    | Mm_Ensembl = ENSMUSG00000060376
    | Mm_RefseqmRNA = NM_007533
    | Mm_RefseqProtein = NP_031559
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 25338707
    | Mm_GenLoc_end = 25367507
    | Mm_Uniprot = Q3U3J1
  }}
}}
'''Branched chain keto acid dehydrogenase E1, alpha polypeptide''', also known as '''BCKDHA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCKDHA branched chain keto acid dehydrogenase E1, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=593| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = The second major step in the catabolism of the branched-chain amino acids, isoleucine, leucine, and valine, is catalyzed by the branched-chain alpha-keto acid dehydrogenase complex (BCKD; EC 1.2.4.4), an inner-mitochondrial enzyme complex that consists of 3 catalytic components: a heterotetrameric (alpha2, beta2) branched-chain alpha-keto acid decarboxylase (E1), a homo-24-meric dihydrolipoyl transacylase (E2; MIM 248610), and a homodimeric dihydrolipoamide dehydrogenase (E3; MIM 238331). The reaction is irreversible and constitutes the first committed step in BCAA oxidation. The complex also contains 2 regulatory enzymes, a kinase and a phosphorylase. The BCKDHA gene encodes the alpha subunit of E1, and the BCKDHB gene (MIM 248611) encodes the beta subunit of E1.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: BCKDHA branched chain keto acid dehydrogenase E1, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=593| accessdate = }}</ref>
| summary_text = The second major step in the catabolism of the branched-chain amino acids, isoleucine, leucine, and valine, is catalyzed by the branched-chain alpha-keto acid dehydrogenase complex (BCKD; EC 1.2.4.4), an inner-mitochondrial enzyme complex that consists of 3 catalytic components: a heterotetrameric (alpha2, beta2) branched-chain alpha-keto acid decarboxylase (E1), a homo-24-meric dihydrolipoyl transacylase (E2; MIM 248610), and a homodimeric dihydrolipoamide dehydrogenase (E3; MIM 238331). The reaction is irreversible and constitutes the first committed step in BCAA oxidation. The complex also contains 2 regulatory enzymes, a kinase and a phosphorylase. The BCKDHA gene encodes the alpha subunit of E1, and the BCKDHB gene (MIM 248611) encodes the beta subunit of E1.[supplied by OMIM]<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|BCKDHA}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Mitsubuchi H, Matsuda I, Nobukuni Y, ''et al.'' |title=Gene analysis of Mennonite maple syrup urine disease kindred using primer-specified restriction map modification. |journal=J. Inherit. Metab. Dis. |volume=15 |issue= 2 |pages= 181-7 |year= 1992 |pmid= 1356170 |doi=  }}
*{{cite journal  | vauthors=Mitsubuchi H, Matsuda I, Nobukuni Y |title=Gene analysis of Mennonite maple syrup urine disease kindred using primer-specified restriction map modification |journal=J. Inherit. Metab. Dis. |volume=15 |issue= 2 |pages= 181–7 |year= 1992 |pmid= 1356170 |doi=10.1007/BF01799628 |display-authors=etal}}
*{{cite journal  | author=McKean MC, Winkeler KA, Danner DJ |title=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. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 1 |pages= 109-12 |year= 1992 |pmid= 1420356 |doi=  }}
*{{cite journal  | vauthors=McKean MC, Winkeler KA, Danner DJ |title=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 |journal=Biochim. Biophys. Acta |volume=1171 |issue= 1 |pages= 109–12 |year= 1992 |pmid= 1420356 |doi=  10.1016/0167-4781(92)90149-t}}
*{{cite journal  | author=Dariush N, Fisher CW, Cox RP, Chuang DT |title=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. |journal=FEBS Lett. |volume=291 |issue= 2 |pages= 376-7 |year= 1991 |pmid= 1682165 |doi= }}
*{{cite journal  | vauthors=Dariush N, Fisher CW, Cox RP, Chuang DT |title=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 |journal=FEBS Lett. |volume=291 |issue= 2 |pages= 376–7 |year= 1991 |pmid= 1682165 |doi=10.1016/0014-5793(91)81324-2  }}
*{{cite journal  | author=Eisenstein RS, Hoganson G, Miller RH, Harper AE |title=Altered phosphorylation state of branched-chain 2-oxo acid dehydrogenase in a branched-chain acyltransferase deficient human fibroblast cell line. |journal=J. Inherit. Metab. Dis. |volume=14 |issue= 1 |pages= 37-44 |year= 1991 |pmid= 1861457 |doi=  }}
*{{cite journal  | vauthors=Eisenstein RS, Hoganson G, Miller RH, Harper AE |title=Altered phosphorylation state of branched-chain 2-oxo acid dehydrogenase in a branched-chain acyltransferase deficient human fibroblast cell line |journal=J. Inherit. Metab. Dis. |volume=14 |issue= 1 |pages= 37–44 |year= 1991 |pmid= 1861457 |doi=10.1007/BF01804386 }}
*{{cite journal  | author=Fisher CR, Fisher CW, Chuang DT, Cox RP |title=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. |journal=Am. J. Hum. Genet. |volume=49 |issue= 2 |pages= 429-34 |year= 1991 |pmid= 1867199 |doi=  }}
*{{cite journal  | vauthors=Fisher CR, Fisher CW, Chuang DT, Cox RP |title=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 |journal=Am. J. Hum. Genet. |volume=49 |issue= 2 |pages= 429–34 |year= 1991 |pmid= 1867199 |doi= | pmc=1683290 }}
*{{cite journal  | author=Fisher CR, Chuang JL, Cox RP, ''et al.'' |title=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. |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 1034-7 |year= 1991 |pmid= 1885764 |doi=  }}
*{{cite journal  | vauthors=Fisher CR, Chuang JL, Cox RP |title=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 |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 1034–7 |year= 1991 |pmid= 1885764 |doi=10.1172/JCI115363 | pmc=295513  |display-authors=etal}}
*{{cite journal  | author=Zneimer SM, Lau KS, Eddy RL, ''et al.'' |title=Regional assignment of two genes of the human branched-chain alpha-keto acid dehydrogenase complex: the E1 beta gene (BCKDHB) to chromosome 6p21-22 and the E2 gene (DBT) to chromosome 1p31. |journal=Genomics |volume=10 |issue= 3 |pages= 740-7 |year= 1991 |pmid= 1889817 |doi=  }}
*{{cite journal  | vauthors=Zneimer SM, Lau KS, Eddy RL |title=Regional assignment of two genes of the human branched-chain alpha-keto acid dehydrogenase complex: the E1 beta gene (BCKDHB) to chromosome 6p21-22 and the E2 gene (DBT) to chromosome 1p31 |journal=Genomics |volume=10 |issue= 3 |pages= 740–7 |year= 1991 |pmid= 1889817 |doi=10.1016/0888-7543(91)90458-Q |display-authors=etal}}
*{{cite journal  | author=Zhang B, Zhao Y, Harris RA, Crabb DW |title=Molecular defects in the E1 alpha subunit of the branched-chain alpha-ketoacid dehydrogenase complex that cause maple syrup urine disease. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 39-47 |year= 1991 |pmid= 1943689 |doi=  }}
*{{cite journal  | vauthors=Zhang B, Zhao Y, Harris RA, Crabb DW |title=Molecular defects in the E1 alpha subunit of the branched-chain alpha-ketoacid dehydrogenase complex that cause maple syrup urine disease |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 39–47 |year= 1991 |pmid= 1943689 |doi=  }}
*{{cite journal  | author=Dariush N, Fisher CW, Cox RP, Chuang DT |title=Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. |journal=FEBS Lett. |volume=284 |issue= 1 |pages= 34-8 |year= 1991 |pmid= 2060625 |doi=  }}
*{{cite journal  | vauthors=Dariush N, Fisher CW, Cox RP, Chuang DT |title=Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex |journal=FEBS Lett. |volume=284 |issue= 1 |pages= 34–8 |year= 1991 |pmid= 2060625 |doi=10.1016/0014-5793(91)80755-R }}
*{{cite journal  | author=Matsuda I, Nobukuni Y, Mitsubuchi H, ''et al.'' |title=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. |journal=Biochem. Biophys. Res. Commun. |volume=172 |issue= 2 |pages= 646-51 |year= 1990 |pmid= 2241958 |doi=  }}
*{{cite journal  | vauthors=Matsuda I, Nobukuni Y, Mitsubuchi H |title=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 |journal=Biochem. Biophys. Res. Commun. |volume=172 |issue= 2 |pages= 646–51 |year= 1990 |pmid= 2241958 |doi=10.1016/0006-291X(90)90723-Z |display-authors=etal}}
*{{cite journal  | author=Zhang B, Edenberg HJ, Crabb DW, Harris RA |title=Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease. |journal=J. Clin. Invest. |volume=83 |issue= 4 |pages= 1425-9 |year= 1989 |pmid= 2703538 |doi=  }}
*{{cite journal  | vauthors=Zhang B, Edenberg HJ, Crabb DW, Harris RA |title=Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease |journal=J. Clin. Invest. |volume=83 |issue= 4 |pages= 1425–9 |year= 1989 |pmid= 2703538 |doi=10.1172/JCI114033  | pmc=303839 }}
*{{cite journal  | author=Fekete G, Plattner R, Crabb DW, ''et al.'' |title=Localization of the human gene for the El alpha subunit of branched chain keto acid dehydrogenase (BCKDHA) to chromosome 19q13.1----q13.2. |journal=Cytogenet. Cell Genet. |volume=50 |issue= 4 |pages= 236-7 |year= 1989 |pmid= 2805821 |doi=  }}
*{{cite journal  | vauthors=Fekete G, Plattner R, Crabb DW |title=Localization of the human gene for the El alpha subunit of branched chain keto acid dehydrogenase (BCKDHA) to chromosome 19q13.1----q13.2 |journal=Cytogenet. Cell Genet. |volume=50 |issue= 4 |pages= 236–7 |year= 1989 |pmid= 2805821 |doi=10.1159/000132768 |display-authors=etal}}
*{{cite journal  | author=Fisher CW, Chuang JL, Griffin TA, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=264 |issue= 6 |pages= 3448-53 |year= 1989 |pmid= 2914958 |doi=  }}
*{{cite journal  | vauthors=Fisher CW, Chuang JL, Griffin TA |title=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 |journal=J. Biol. Chem. |volume=264 |issue= 6 |pages= 3448–53 |year= 1989 |pmid= 2914958 |doi=  |display-authors=etal}}
*{{cite journal  | author=Zhang B, Crabb DW, Harris RA |title=Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase. |journal=Gene |volume=69 |issue= 1 |pages= 159-64 |year= 1989 |pmid= 3224821 |doi=  }}
*{{cite journal  | vauthors=Zhang B, Crabb DW, Harris RA |title=Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase |journal=Gene |volume=69 |issue= 1 |pages= 159–64 |year= 1989 |pmid= 3224821 |doi=10.1016/0378-1119(88)90390-3 }}
*{{cite journal  | author=Hu CW, Lau KS, Griffin TA, ''et al.'' |title=Isolation and sequencing of a cDNA encoding the decarboxylase (E1)alpha precursor of bovine branched-chain alpha-keto acid dehydrogenase complex. Expression of E1 alpha mRNA and subunit in maple-syrup-urine-disease and 3T3-L1 cells. |journal=J. Biol. Chem. |volume=263 |issue= 18 |pages= 9007-14 |year= 1988 |pmid= 3379058 |doi=  }}
*{{cite journal  | vauthors=Hu CW, Lau KS, Griffin TA |title=Isolation and sequencing of a cDNA encoding the decarboxylase (E1)alpha precursor of bovine branched-chain alpha-keto acid dehydrogenase complex. Expression of E1 alpha mRNA and subunit in maple-syrup-urine-disease and 3T3-L1 cells |journal=J. Biol. Chem. |volume=263 |issue= 18 |pages= 9007–14 |year= 1988 |pmid= 3379058 |doi=  |display-authors=etal}}
*{{cite journal  | author=Chuang JL, Davie JR, Chinsky JM, ''et al.'' |title=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. |journal=J. Clin. Invest. |volume=95 |issue= 3 |pages= 954-63 |year= 1995 |pmid= 7883996 |doi=  }}
*{{cite journal  | vauthors=Chuang JL, Davie JR, Chinsky JM |title=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 |journal=J. Clin. Invest. |volume=95 |issue= 3 |pages= 954–63 |year= 1995 |pmid= 7883996 |doi=10.1172/JCI117804  | pmc=441427 |display-authors=etal}}
*{{cite journal  | author=Wynn RM, Kochi H, Cox RP, Chuang DT |title=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. |journal=Biochim. Biophys. Acta |volume=1201 |issue= 1 |pages= 125-8 |year= 1994 |pmid= 7918575 |doi=  }}
*{{cite journal  | vauthors=Wynn RM, Kochi H, Cox RP, Chuang DT |title=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 |journal=Biochim. Biophys. Acta |volume=1201 |issue= 1 |pages= 125–8 |year= 1994 |pmid= 7918575 |doi=  10.1016/0304-4165(94)90161-9}}
*{{cite journal  | author=Chuang JL, Fisher CR, Cox RP, Chuang DT |title=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. |journal=Am. J. Hum. Genet. |volume=55 |issue= 2 |pages= 297-304 |year= 1994 |pmid= 8037208 |doi=  }}
*{{cite journal  | vauthors=Chuang JL, Fisher CR, Cox RP, Chuang DT |title=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 |journal=Am. J. Hum. Genet. |volume=55 |issue= 2 |pages= 297–304 |year= 1994 |pmid= 8037208 |doi= | pmc=1918348 }}
*{{cite journal  | author=Nobukuni Y, Mitsubuchi H, Hayashida Y, ''et al.'' |title=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. |journal=Biochim. Biophys. Acta |volume=1225 |issue= 1 |pages= 64-70 |year= 1993 |pmid= 8161368 |doi=  }}
*{{cite journal  | vauthors=Nobukuni Y, Mitsubuchi H, Hayashida Y |title=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 |journal=Biochim. Biophys. Acta |volume=1225 |issue= 1 |pages= 64–70 |year= 1993 |pmid= 8161368 |doi=  10.1016/0925-4439(93)90123-i|display-authors=etal}}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
}}
}}
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Revision as of 01:54, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial is an enzyme that in humans is encoded by the BCKDHA gene.[1]

The second major step in the catabolism of the branched-chain amino acids, isoleucine, leucine, and valine, is catalyzed by the branched-chain alpha-keto acid dehydrogenase complex (BCKD; EC 1.2.4.4), an inner-mitochondrial enzyme complex that consists of 3 catalytic components: a heterotetrameric (alpha2, beta2) branched-chain alpha-keto acid decarboxylase (E1), a homo-24-meric dihydrolipoyl transacylase (E2; MIM 248610), and a homodimeric dihydrolipoamide dehydrogenase (E3; MIM 238331). The reaction is irreversible and constitutes the first committed step in BCAA oxidation. The complex also contains 2 regulatory enzymes, a kinase and a phosphorylase. The BCKDHA gene encodes the alpha subunit of E1, and the BCKDHB gene (MIM 248611) encodes the beta subunit of E1.[supplied by OMIM][1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: BCKDHA branched chain keto acid dehydrogenase E1, alpha polypeptide".

External links

Further reading


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