CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.990 | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
|
1.20.990.10 | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
| Functional Family | Nitric oxide synthase |
Enzyme Information
| 1.14.13.39 |
Nitric-oxide synthase (NADPH).
based on mapping to UniProt P29476
2 L-arginine + 3 NADPH + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
-!- The enzyme consists of linked oxygenase and reductase domains. -!- The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. -!- Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. -!- The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. -!- Cf. EC 1.14.14.47.
|
UniProtKB Entries (1)
| P29476 |
NOS1_RAT
Rattus norvegicus
Nitric oxide synthase, brain
|
PDB Structure
| PDB | 1TLL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Pichia |
| Primary Citation |
Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase
J.Biol.Chem.
|
