KEGG   ENZYME: 1.2.1.104
Entry
EC 1.2.1.104                Enzyme                                 

Name
pyruvate dehydrogenase system;
pyruvate dehydrogenase complex;
PDH
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
Sysname
pyruvate:NAD+ 2-oxidoreductase (CoA-acetylating)
Reaction(IUBMB)
pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH [RN:R00209]
Reaction(KEGG)
R00209
Substrate
pyruvate [CPD:C00022];
CoA [CPD:C00010];
NAD+ [CPD:C00003]
Product
acetyl-CoA [CPD:C00024];
CO2 [CPD:C00011];
NADH [CPD:C00004]
Comment
The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain alpha-keto acid dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) (E1), EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase (E2), and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3). The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
History
EC 1.2.1.104 created 2020
Reference
1  [PMID:1103138]
  Authors
Reed LJ, Pettit FH, Eley MH, Hamilton L, Collins JH, Oliver RM.
  Title
Reconstitution of the Escherichia coli pyruvate dehydrogenase complex.
  Journal
Proc Natl Acad Sci U S A 72:3068-72 (1975)
DOI:10.1073/pnas.72.8.3068
Reference
2  [PMID:329143]
  Authors
Bates DL, Danson MJ, Hale G, Hooper EA, Perham RN.
  Title
Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
  Journal
Nature 268:313-6 (1977)
DOI:10.1038/268313a0
Reference
3  [PMID:7032507]
  Authors
Stanley CJ, Packman LC, Danson MJ, Henderson CE, Perham RN.
  Title
Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources.
  Journal
Biochem J 195:715-21 (1981)
DOI:10.1042/bj1950715
Reference
4  [PMID:3905803]
  Authors
Yang HC, Hainfeld JF, Wall JS, Frey PA.
  Title
Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli.
  Journal
J Biol Chem 260:16049-51 (1985)
Reference
5  [PMID:2227213]
  Authors
Patel MS, Roche TE.
  Title
Molecular biology and biochemistry of pyruvate dehydrogenase complexes.
  Journal
FASEB J 4:3224-33 (1990)
DOI:10.1096/fasebj.4.14.2227213
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.104
IUBMB Enzyme Nomenclature: 1.2.1.104
ExPASy - ENZYME nomenclature database: 1.2.1.104
BRENDA, the Enzyme Database: 1.2.1.104
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