In:
Canadian Journal of Physiology and Pharmacology, Canadian Science Publishing, Vol. 68, No. 6 ( 1990-06-01), p. 754-761
Abstract:
We characterized the genes of the male-specific mouse steroid 16α-hydroxylase (C-P-450 16α ) and the female-specific mouse steroid 15α-hydroxylase (P-450 15α ) within two distinct gene families. In spite of the high structural identities within each family, the expression of the hydroxylase genes is uniquely regulated. Moreover, the other family members encode the P-450s which are structurally very similar to the hydroxylases but are not able to catalyze steroid hydroxylase activities. For example, only a single amino acid substitution creates steroid 15α-hydroxylase activity in another family-member P-450coh, which catalyzes coumarin 7-hydroxylase but little steroid hydroxylase activity. It appears, therefore, that the mouse P-450 gene families evolved through gene duplication and selective mutation to create new P-450s structurally as well as to establish novel regulatory elements for the gene expressions.Key words: cytochrome P-450, steroid hydroxylase, site-directed mutagenesis, evolution, gene regulation.
Type of Medium:
Online Resource
ISSN:
0008-4212
,
1205-7541
Language:
English
Publisher:
Canadian Science Publishing
Publication Date:
1990
detail.hit.zdb_id:
2004356-9
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