Ahmed, Sabbir (2004) The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme complex 17[alpha]-hydroxylase and 17,20-lyase. Biochemical and Biophysical Research Communications, 316(3), pp. 595-598. ISSN (print) 0006-291XFull text not available from this archive.
A novel molecular modelling technique, namely the substrate-heme complex (SHC) approach, is used to derive a representation of the overall active site of the enzyme complex 17alpha-hydroxylase (17alpha-OHase) and 17,20-lyase (lyase), a cytochrome P-450 dependent enzyme involved in the oxidative hydroxylation of the C(17) and cleavage of the C(17)-C(20) bond of the progestins (e.g., progesterone or pregnenolone). Using the derived model, we have rationalised the inhibitory activity of a number of steroidal and non-steroidal inhibitors, including miconazole and ketoconazole (the latter being a former potential treatment of hormone-dependent prostate cancer).
|Faculty, School or Research Centre:||Faculty of Science (until 2011) > School of Pharmacy and Chemistry|
|Depositing User:||Automatic Import Agent|
|Date Deposited:||08 Mar 2010 08:56|
|Last Modified:||07 Apr 2011 14:56|
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