CATH Classification

Domain Context

CATH Clusters

Superfamily CO dehydrogenase flavoprotein, C-terminal domain
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 4TVY
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Computational design of a red fluorophore ligase for site-specific protein labeling in living cells.
Liu, D.S., Nivon, L.G., Richter, F., Goldman, P.J., Deerinck, T.J., Yao, J.Z., Richardson, D., Phipps, W.S., Ye, A.Z., Ellisman, M.H., Drennan, C.L., Baker, D., Ting, A.Y.
Proc.Natl.Acad.Sci.USA