CATH Classification

Domain Context

CATH Clusters

Superfamily 2.40.50.100
Functional Family Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Enzyme Information

2.3.1.12
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P11961
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
-!- 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 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.

UniProtKB Entries (1)

P11961
ODP2_GEOSE
Geobacillus stearothermophilus
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

PDB Structure

PDB 1LAC
External Links
Method SOLUTION NMR
Organism
Primary Citation
Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.
Dardel, F., Davis, A.L., Laue, E.D., Perham, R.N.
J.Mol.Biol.