CATH Classification

Domain Context

CATH Clusters

Superfamily 2.40.50.100
Functional Family Acetyltransferase component of pyruvate dehydrogenase complex

Enzyme Information

2.3.1.12
Dihydrolipoyllysine-residue acetyltransferase.
based on mapping to UniProt P10515
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)

Q15120
PDK3_HUMAN
Homo sapiens
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial

PDB Structure

PDB 2PNR
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal Structure of an Asymmetric complex of Pyruvate Dehydrogenase Kinase 3 with Lipoyl domain 2 and its Biological Implications
Devedjiev, Y., Steussy, C.N., Vassylyev, D.G.
J.Mol.Biol.