Title : Mechanism of Cytochrome P450 17A1-Catalyzed Hydroxylase and Lyase Reactions.

Pub. Date : 2017 May 22

PMID : 28387522






3 Functional Relationships(s)
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1 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. 17-alpha-Hydroxypregnenolone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
2 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. 17-alpha-Hydroxypregnenolone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
3 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. 17-alpha-Hydroxypregnenolone cytochrome P450 family 17 subfamily A member 1 Homo sapiens