CATH Classification

Domain Context

CATH Clusters

Superfamily Bira Bifunctional Protein; Domain 2
Functional Family Lipoate-protein ligase A

Enzyme Information

6.3.1.20
Lipoate--protein ligase.
based on mapping to UniProt P32099
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl- carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate.
-!- This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid. -!- The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- Lipoylation is essential for the function of these enzymes. -!- The enzyme can also use octanoate instead of lipoate. -!- Formerly EC 2.7.7.63.

UniProtKB Entries (1)

P32099
LPLA_ECOLI
Escherichia coli K-12
Lipoate-protein ligase A

PDB Structure

PDB 1X2H
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of lipoate-protein ligase A from Escherichia coli: Determination of the lipoic acid-binding site
Fujiwara, K., Toma, S., Okamura-Ikeda, K., Motokawa, Y., Nakagawa, A., Taniguchi, H.
J.Biol.Chem.