Steroid 11beta-monooxygenase

From Wikipedia, the free encyclopedia

In enzymology, a steroid 11beta-monooxygenase (EC 1.14.15.4) is an enzyme that catalyzes the chemical reaction

a steroid + reduced adrenal ferredoxin + O₂ $\rightleftharpoons$ an 11beta-hydroxysteroid + oxidized adrenal ferredoxin + H₂O

The 3 substrates of this enzyme are steroid, reduced adrenal ferredoxin, and O₂, whereas its 3 products are 11beta-hydroxysteroid, oxidized adrenal ferredoxin, and H₂O.

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 o one atom of oxygen into the other donor. The systematic name of this enzyme class is steroid,reduced-adrenal-ferredoxin:oxygen oxidoreductase (11beta-hydroxylating). Other names in common use include steroid 11beta-hydroxylase, steroid 11beta/18-hydroxylase, and oxygenase, steroid 11beta -mono-. This enzyme participates in c21-steroid hormone metabolism and androgen and estrogen metabolism. It employs one cofactor, heme.

[edit] References

IUBMB entry for 1.14.15.4
BRENDA references for 1.14.15.4 (Recommended.)
PubMed references for 1.14.15.4
PubMed Central references for 1.14.15.4
Google Scholar references for 1.14.15.4
GRANT JK, BROWNIE AC (1955). "The role of fumarate and TPN in steroid enzymic 11beta-hydroxylation". Biochim. Biophys. Acta. 18: 433–4. doi:10.1016/0006-3002(55)90111-6. PMID 13276417.
HAYANO M, DORFMAN RI (1954). "On the mechanism of the C11 beta-hydroxylation of steroids". J. Biol. Chem. 211: 227–35. PMID 13211659.
TOMKINS GM, MICHAEL PJ, CURRAN JF (1957). "Studies on the nature of steroid 11-beta hydroxylation". Biochim. Biophys. Acta. 23: 655–6. doi:10.1016/0006-3002(57)90396-7. PMID 13426185.
Yanagibashi K, Haniu M, Shively JE, Shen WH, Hall P (1986). "The synthesis of aldosterone by the adrenal cortex. Two zones (fasciculata and glomerulosa) possess one enzyme for 11 beta-, 18-hydroxylation, and aldehyde synthesis". J. Biol. Chem. 261: 3556–62. PMID 3485096.
Zuidweg MH (1968). "Hydroxylation of Reichstein's compound S with cell-free preparations from Curvularia lunata". Biochim. Biophys. Acta. 152: 144–58. PMID 4967077.