EC 2.3.1.12 - Dihydrolipoyllysine-residue acetyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.12

Names

Accepted name:
dihydrolipoyllysine-residue acetyltransferase
Other names:
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

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004742
CAS Registry Number: 9032-29-5
UniProtKB/Swiss-Prot: (55) [show] [UniProt]

References

  1. Brady, R.O. and Stadtman, E.R.
    Enzymatic thioltransacetylation.
    J. Biol. Chem. 211: 621-629 (1954). [PMID: 13221570]
  2. Gunsalus, I.C.
    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, 1954, 545-480
  3. Gunsalus, I.C., Barton, L.S. and Gruber, W.
    Biosynthesis and structure of lipoic acid derivatives.
    J. Am. Chem. Soc. 78: 1763-1766 (1956).
  4. Perham, R.N.
    Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
    Annu. Rev. Biochem. 69: 961-1004 (2000). [PMID: 10966480]

[EC 2.3.1.12 created 1961, modified 2003]