CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.180 | Quinone Oxidoreductase; Chain A, domain 1 |
|
3.90.180.10 | Medium-chain alcohol dehydrogenases, catalytic domain |
Domain Context
CATH Clusters
| Superfamily | Medium-chain alcohol dehydrogenases, catalytic domain |
| Functional Family |
Enzyme Information
| 2.3.1.161 |
Lovastatin nonaketide synthase.
based on mapping to UniProt Q9Y7D0
9 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO(2) + 11 NADP(+) + S-adenosyl-L-homocysteine + 6 H(2)O.
-!- This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. -!- The PKS catalyzes many of the chain building reactions of EC 2.3.1.85, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
|
UniProtKB Entries (1)
| Q9Y7D0 |
LOVC_ASPTE
Aspergillus terreus
Lovastatin nonaketide synthase, enoyl reductase component
|
PDB Structure
| PDB | 3B6Z |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure and biochemical studies of the trans-acting polyketide enoyl reductase LovC from lovastatin biosynthesis.
Proc.Natl.Acad.Sci.USA
|
