CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.390.30
Functional Family Dihydrolipoyl dehydrogenase

Enzyme Information

1.8.1.4
Dihydrolipoyl dehydrogenase.
based on mapping to UniProt P18925
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)

P18925
DLDH_AZOVI
Azotobacter vinelandii
Dihydrolipoyl dehydrogenase

PDB Structure

PDB 3LAD
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.
Mattevi, A., Schierbeek, A.J., Hol, W.G.
J.Mol.Biol.