CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.390.30
Functional Family Dihydrolipoyl dehydrogenase

Enzyme Information
Dihydrolipoyl dehydrogenase.
based on mapping to UniProt P0A9P0
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)

Escherichia coli K-12
Dihydrolipoyl dehydrogenase

PDB Structure

External Links
Primary Citation
Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches.
Chandrasekhar, K., Wang, J., Arjunan, P., Sax, M., Park, Y.H., Nemeria, N.S., Kumaran, S., Song, J., Jordan, F., Furey, W.