CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information
Dihydrolipoyl dehydrogenase.
based on mapping to UniProt P09624
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 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 and EC 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, the T protein (EC, the L protein (EC and the lipoyl-bearing H protein. -!- Formerly EC

UniProtKB Entries (1)

Saccharomyces cerevisiae S288C
Dihydrolipoyl dehydrogenase, mitochondrial

PDB Structure

External Links
Primary Citation
Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
Toyoda, T., Suzuki, K., Sekiguchi, T., Reed, L.J., Takenaka, A.