CATH Domain 2q8iB00

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 (1)

Q15120

PDK3_HUMAN

Homo sapiens

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial

PDB Structure

PDB	2Q8I
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Distinct Structural Mechanisms for Inhibition of Pyruvate Dehydrogenase Kinase Isoforms by AZD7545, Dichloroacetate, and Radicicol. Kato, M., Li, J., Chuang, J.L., Chuang, D.T. Structure