CATH Classification

Domain Context

CATH Clusters

Superfamily E3-binding domain
Functional Family Pyruvate dehydrogenase E2 component

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.
2.3.1.-
Transferring groups other than amino-acyl groups.
based on mapping to UniProt P11961

UniProtKB Entries (1)

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

PDB Structure

PDB 1EBD
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase.
Mande, S.S., Sarfaty, S., Allen, M.D., Perham, R.N., Hol, W.G.
Structure