+ 2 reduced
ferredoxin + H+
Corticosterone 18-monooxygenase
| Corticosterone 18-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.15.5 | ||||||||
| CAS no. | 37256-75-0 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Corticosterone 18-monooxygenase (EC 1.14.15.5) is an enzyme that catalyzes the chemical reaction
Corticosterone is an oxidoreductase which uses molecular oxygen to insert a hydroxy group at position 18 of the steroid. It requires adrenal ferredoxin to transfer electrons to the cytochrome P450 active site.[1][2] The systematic name of this enzyme class is corticosterone,reduced-adrenal-ferredoxin:oxygen oxidoreductase (18-hydroxylating). Other names in common use include corticosterone 18-hydroxylase, and corticosterone methyl oxidase.[3] This enzyme is part of the pathway which converts corticosterone to aldosterone.[4]
References
- ↑ "PhytoMine: GOTerm GO:0047783 corticosterone 18-monooxygenase activity GO". phytozome-next.jgi.doe.gov. Archived from the original on 2022-08-20. Retrieved 2022-08-20.
- ↑ Pivonello R, Fleseriu M, Newell-Price J, Bertagna X, Findling J, Shimatsu A, et al. (September 2020). "Efficacy and safety of osilodrostat in patients with Cushing's disease (LINC 3): a multicentre phase III study with a double-blind, randomised withdrawal phase" (PDF). The Lancet. Diabetes & Endocrinology. 8 (9): 748–761. doi:10.1016/S2213-8587(20)30240-0. PMID 32730798. S2CID 220892722.
- ↑ Enzyme 1.14.15.5 at KEGG Pathway Database.
- ↑ Yanagibashi K, Shackleton CH, Hall PF (June 1988). "Conversion of 11-deoxycorticosterone and corticosterone to aldosterone by cytochrome P-450 11 beta-/18-hydroxylase from porcine adrenal". Journal of Steroid Biochemistry. 29 (6): 665–675. doi:10.1016/0022-4731(88)90167-7. PMID 3386233.