ExplorEnz: EC 2.3.1.12

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2.3.1.12

Accepted name:

dihydrolipoyllysine-residue acetyltransferase

Reaction:

acetyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(S-acetyldihydrolipoyl)lysine

For diagram of oxo-acid-dehydrogenase complexes, click here

Glossary:

dihydrolipoyl group

Other name(s):

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

Systematic name:

acetyl-CoA:enzyme N⁶-(dihydrolipoyl)lysine S-acetyltransferase

Comments:

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 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-29-5

References:

1.	Brady, R.O. and Stadtman, E.R. Enzymatic thioltransacetylation. J. Biol. Chem. 211 (1954) 621–629. [PMID: 13221570]
2.	Gunsalus, I.C. Group transfer and acyl-generating functions of lipoic acid derivatives. In: McElroy, W.D. and Glass, B. (Ed.), A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, pp. 545–580.
3.	Gunsalus, I.C., Barton, L.S. and Gruber, W. Biosynthesis and structure of lipoic acid derivatives. J. Am. Chem. Soc. 78 (1956) 1763–1766.
4.	Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [DOI] [PMID: 10966480]

[EC 2.3.1.12 created 1961, modified 2003]