CATH Classification

Domain Context

CATH Clusters

Superfamily FAD/NAD(P)-binding domain
Functional Family Dihydrolipoyl dehydrogenase

Enzyme Information

1.8.1.4
Dihydrolipoyl dehydrogenase.
based on mapping to UniProt P9WHH9
Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
-!- A component of the multienzyme 2-oxo-acid dehydrogenase complexes. -!- In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups. -!- It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes. -!- Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine. -!- It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. -!- Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase. -!- The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein. -!- Formerly EC 1.6.4.3.

UniProtKB Entries (1)

P9WHH9
DLDH_MYCTU
Mycobacterium tuberculosis H37Rv
Dihydrolipoyl dehydrogenase

PDB Structure

PDB 4M52
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Lipoamide channel-binding sulfonamides selectively inhibit mycobacterial lipoamide dehydrogenase.
Bryk, R., Arango, N., Maksymiuk, C., Balakrishnan, A., Wu, Y.T., Wong, C.H., Masquelin, T., Hipskind, P., Lima, C.D., Nathan, C.
Biochemistry