KEGG ENZYME: 1.2.1.104

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

All links

Chemical substance (7)   
   KEGG COMPOUND (7)   
Chemical reaction (3)   
   KEGG REACTION (1)   
   KEGG RCLASS (2)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (3)   
   RefSeq(nuc) (1)   
   GenBank (1)   
   EMBL (1)   
All databases (16)   

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