CATH Domain 3crkC00

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.50	OB fold (Dihydrolipoamide Acetyltransferase, E2P)
	2.40.50.100	RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain

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)

P10515	ODP2_HUMAN Homo sapiens Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Q64536	PDK2_RAT Rattus norvegicus [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial

PDB Structure

PDB	3CRK
External Links	PDBSum Proteopedia
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. Green, T., Grigorian, A., Klyuyeva, A., Tuganova, A., Luo, M., Popov, K.M. J.Biol.Chem.

Network disruptions