CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family |
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.
J.Mol.Biol.
|
