Published February 16, 2007 | Version v1
Journal article

Adrenodoxin supports reactions catalyzed by microsomal steroidogenic cytochrome P450s

  • 1. Institute of Bioorganic Chemistry, Academy of Sciences of Belarus, Kuprevicha st., 5/2, Minsk 220141 (Belarus)

Description

The interaction of adrenodoxin (Adx) and NADPH cytochrome P450 reductase (CPR) with human microsomal steroidogenic cytochrome P450s was studied. It is found that Adx, mitochondrial electron transfer protein, is able to support reactions catalyzed by human microsomal P450s: full length CYP17, truncated CYP17, and truncated CYP21. CPR, but not Adx, supports activity of truncated CYP19. Truncated and the full length CYP17s show distinct preference for electron donor proteins. Truncated CYP17 has higher activity with Adx compared to CPR. The alteration in preference to electron donor does not change product profile for truncated enzymes. The electrostatic contacts play a major role in the interaction of truncated CYP17 with either CPR or Adx. Similarly electrostatic contacts are predominant in the interaction of full length CYP17 with Adx. We speculate that Adx might serve as an alternative electron donor for CYP17 at the conditions of CPR deficiency in human

Additional details

Identifiers

DOI
10.1016/j.bbrc.2006.12.047;
PII
S0006-291X(06)02713-6;

Publishing Information

Journal Title
Biochemical and Biophysical Research Communications
Journal Volume
353
Journal Issue
3
Journal Page Range
p. 598-604
ISSN
0006-291X
CODEN
BBRCA9

INIS

Country of Publication
United States
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
39008503
Subject category
S60: APPLIED LIFE SCIENCES;
Descriptors DEI
BINDING ENERGY; BIOSYNTHESIS; ELECTRON TRANSFER; ELECTRONS; FIRST AID; HYDROXYLASES; MITOCHONDRIA; STEROIDS
Descriptors DEC
CELL CONSTITUENTS; ELEMENTARY PARTICLES; ENERGY; ENZYMES; FERMIONS; LEPTONS; MEDICINE; ORGANIC COMPOUNDS; OXIDOREDUCTASES; PROTEINS; SYNTHESIS; THERAPY

Optional Information

Copyright
Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.