|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 126.96.36.199
1.2.1.-: pyruvate + coenzyme A + NAD+ → acetyl-CoA + CO2 + NADH
In Pathway: pyruvate decarboxylation to acetyl CoA
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: dihydrolipoyllysine-residue acetyltransferase
Enzyme Commission Synonyms: acetyl-CoA:dihydrolipoamide S-acetyltransferase, dihydrolipoamide S-acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyltransferase, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, thioltransacetylase A, transacetylase X, enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase, acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase
Enzyme Commission Summary:
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 188.8.131.52, pyruvate dehydrogenase (acetyl-transferring) and EC 184.108.40.206, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 220.127.116.11, and the only observed direction catalyzed by EC 18.104.22.168 is that where the acetyl group is passed to coenzyme A.
Gunsalus54: Gunsalus IC (1954). "Group transfer and acyl-generating functions of lipoic acid derivatives." In: McElroy, W.D. and Glass, B. (Eds), A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, pp. 545-580.
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