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J Steroid Biochem Mol Biol. 2016 Jul;161:54-72. doi: 10.1016/j.jsbmb.2016.02.021. Epub 2016 Feb 24.

Androgen-metabolizing enzymes: A structural perspective.

Author information

1
Département de Biochimie, de Microbiologie et de Bio-informatique, PROTEO, Université Laval, Québec City, QC G1V 0A6, Canada; Institut de Biologie Intégrative et des Systèmes (IBIS), Université Laval, Pavillon Charles-Eugène-Marchand, Québec City, QC G1V 0A6, Canada.
2
Département de Biochimie, de Microbiologie et de Bio-informatique, PROTEO, Université Laval, Québec City, QC G1V 0A6, Canada; Institut de Biologie Intégrative et des Systèmes (IBIS), Université Laval, Pavillon Charles-Eugène-Marchand, Québec City, QC G1V 0A6, Canada. Electronic address: rong.shi@bcm.ulaval.ca.

Abstract

Androgen-metabolizing enzymes convert cholesterol, a relatively inert molecule, into some of the most potent chemical messengers in vertebrates. This conversion involves thermodynamically challenging reactions catalyzed by P450 enzymes and redox reactions catalyzed by Aldo-Keto Reductases (AKRs). This review covers the structures of these enzymes with a focus on active site interactions and proposed mechanisms. Due to their role in a number of diseases, particularly in cancer, androgen-metabolizing enzymes have been targets of drug design. Hence we will also highlight how existing knowledge of structure is being used to this end.

KEYWORDS:

AKRs; Androgen; Aromatase; Inhibitors; P450s; PDB; Structure

PMID:
26924584
DOI:
10.1016/j.jsbmb.2016.02.021
[Indexed for MEDLINE]

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