4.5 Review

Sterol 14 alpha-demethylase cytochrome P450 (CYP51), a P450 in all biological kingdoms

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1770, Issue 3, Pages 467-477

Publisher

ELSEVIER
DOI: 10.1016/j.bbagen.2006.07.018

Keywords

sterol 14 alpha-demethylase (CYP51); sterol biosynthesis; substrate preferences; catalytic activity; inhibition

Funding

  1. NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [P30ES000267] Funding Source: NIH RePORTER
  2. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM067871] Funding Source: NIH RePORTER
  3. NIEHS NIH HHS [P30 ES000267, ES00267-32] Funding Source: Medline
  4. NIGMS NIH HHS [R01 GM067871, GM067871] Funding Source: Medline

Ask authors/readers for more resources

The CYP51 family is an intriguing Subject for fundamental P450 structure/function studies and is also an important clinical drug target. This review updates information on the variety of the CYP51 family members, including their physiological roles, natural substrates and substrate preferences, and catalytic properties in vitro. We present experimental support for the notion that specific conserved regions in the P450 sequences represent a CYP51 signature. Two possible roles of CYP51 in P450 evolution are discussed and the major approaches for CYP51 inhibition are summarized. (c) 2006 Elsevier B.V. All rights reserved.

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