Steroid 18-hydroxylation
Last modified: Tue Jul 6 11:12:42 BST 2004
Steroid |
|
 |
NADPH |
18-Hydroxysteroid |
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Steroid carbon nomenclature
Pathways:
Reaction: steroid hydroxylation at C18
Enzyme: P450c18 (steroid 18-hydroxylase), CYP11B1
EC 1.14.15.4
Enzyme: P450c18 (steroid 18-hydroxylase), CYP11B2
EC 1.14.15.5
Enzyme: P450c18 (steroid 18-hydroxylase), CYP11B3
EC 1.14.15.4
References
- Ruckpaul, K. and Rein, H., Eds. (1990)
Frontiers in Biotransformation, vol. 3:
Molecular Mechanisms of Adrenal Steroidogenesis and Aspects of Regulation
and Application.
Taylor & Francis, London.
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Domalik, L.J., Chaplin, D.D., Kirkman, M.S., Wu, R.C., Liu, W.W., Howard, T.A.,
Seldin, M.F. and Parker, K.L. (1991)
Different isozymes of mouse 11ß-hydroxylase produce mineralocorticoids and
glucocorticoids.
Mol. Endocrinol. 5, 1853-1861.
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Nomura, M., Morohashi, K., Kirita, S., Nonaka, Y., Okamoto, M., Nawata, H. and
Omura, T. (1993)
Three forms of rat CYP11B genes: 11ß-hydroxylase gene, aldosterone
synthase gene, and a novel gene.
J. Biochem. (Tokyo) 113, 144-152.
-
Mellon, S.H., Bair, S.R. and Monis, H. (1995)
P450c11B3 mRNA, transcribed from a third P450c11 gene, is expressed in a
tissue-specific, developmentally, and hormonally regulated fashion in the
rodent adrenal and encodes a protein with both 11-hydroxylase and
18-hydroxylase activities.
J. Biol. Chem. 270, 1643-1649.
-
Nonaka, Y., Takemori, H., Halder, S.K., Sun, T., Ohta, M., Hatano, O.,
Takakusu, A. and Okamoto, M. (1995)
Frog cytochrome P-450 (11ß, aldo), a single enzyme involved in the final
steps of glucocorticoid and mineralocorticoid biosynthesis.
Eur. J. Biochem. 229, 249-256.
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Okamoto, M., Nonaka, Y., Ohta, M., Takemori, H., Halder, S.K., Wang, Z.N.,
Sun, T., Hatano, O., Takakusu, A. and Murakami, T. (1995)
Cytochrome P450(11ß): structure-function relationship of the enzyme
and its involvement in blood pressure regulation.
J. Steroid. Biochem. Mol. Biol. 53, 89-94.
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