CATH Classification

Domain Context

CATH Clusters

Superfamily Chloramphenicol acetyltransferase-like domain
Functional Family Acetyltransferase component of pyruvate dehydrogenase complex

Enzyme Information

2.3.1.12
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P10802
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)

P10802
ODP2_AZOVI
Azotobacter vinelandii
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

PDB Structure

PDB 1DPC
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p).
Hendle, J., Mattevi, A., Westphal, A.H., Spee, J., de Kok, A., Teplyakov, A., Hol, W.G.
Biochemistry