Corticosterone 18-monooxygenase

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corticosterone 18-monooxygenase

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In enzymology, a corticosterone 18-monooxygenase (EC 1.14.15.5) is an enzyme that catalyzes the chemical reaction

corticosterone + reduced adrenal ferredoxin + O₂

\rightleftharpoons

18-hydroxycorticosterone + oxidized adrenal ferredoxin + H₂O^[1]

The 3 substrates of this enzyme are corticosterone, reduced adrenal ferredoxin, and O₂, whereas its 3 products are 18-hydroxycorticosterone, oxidized adrenal ferredoxin, and H₂O.^[2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor.^[3]^[4] 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. This enzyme participates in c21-steroid hormone metabolism.^[5]

References

^ "ENZYME - 1.14.15.5 corticosterone 18-monooxygenase". enzyme.expasy.org. Archived from the original on 2022-08-20. Retrieved 2022-08-20.
^ "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.
^ McDonald A (2019). "The Enzyme List Class 1 — Oxidoreductases" (PDF). Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. 1 (1). Ireland: 759. Archived (PDF) from the original on 2022-03-05. Retrieved 2022-08-20 – via Trinity College Dublin.
^ 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.
^ 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.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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