CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

1.8.1.4
Dihydrolipoyl dehydrogenase.
based on mapping to UniProt P09622
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)

P09622
DLDH_HUMAN
Homo sapiens
Dihydrolipoyl dehydrogenase, mitochondrial

PDB Structure

PDB 2F5Z
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural Insight into Interactions between Dihydrolipoamide Dehydrogenase (E3) and E3 Binding Protein of Human Pyruvate Dehydrogenase Complex.
Brautigam, C.A., Wynn, R.M., Chuang, J.L., Machius, M., Tomchick, D.R., Chuang, D.T.
Structure