Regular ArticleNonsubstrate Recognition Site Residues Are Involved in Testosterone Hydroxylation by Cytochrome P450 CYP 2C11
References (21)
J. Biol. Chem.
(1992)- et al.
Arch. Biochem. Biophys.
(1993) - et al.
Arch. Biochem. Biophys.
(1996) - et al.
J. Biol. Chem.
(1964) - et al.
Biochem. Biophys. Acta
(1992) - et al.
Arch. Biochem. Biophys.
(1987) J. Steroid Biochem. Mol. Biol.
(1992)- et al.
J. Mol. Biol.
(1982) - et al.
J. Biol. Chem.
(1993) - et al.
J. Biol. Chem.
(1993)
There are more references available in the full text version of this article.
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Functional characterization of the G162R and D216H genetic variants of human CYP17A1
2018, Journal of Steroid Biochemistry and Molecular BiologyCitation Excerpt :This reasoning is further supported by Ng and Henikoff, who reported most methods predict that 25–30% of nonsynonymous variants in a gene’s coding region will have a negative effect on protein function [25]. Although most amino acid substitutions that alter enzyme activity are located in or near the active site, variants situated on the periphery of P450s affecting either enzyme activity or stability have been described [26,27]. Here we show that CYP17A1 variants alter activity via different mechanisms: D216H increases the ratio of 17OHP4 to 16OHP4 products, and G162R enhances ubiquitination and proteasomal degradation.
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