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 (2)
Q64536 |
PDK2_RAT
Rattus norvegicus
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial
|
P10515 |
ODP2_HUMAN
Homo sapiens
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
|
PDB Structure
PDB | 3CRK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2.
J.Biol.Chem.
|