Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1814, Issue 1, Pages 88-93Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2010.06.006
Keywords
Cytochrome P450; Sterol 14 alpha-demethylase; CYP51; Crystal structure
Categories
Funding
- National Institute of Health [GM067871]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM067871] Funding Source: NIH RePORTER
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Sterol 14 alpha-demethylases (14DM) comprise the CYP51 cytochrome P450 genome family. The 14DM reaction is essential for the biosynthesis of sterols which are necessary for production of cellular membranes. This is the most widely distributed P450, being present in all biological kingdoms. From one kingdom to another the primary amino acid sequence identity usually ranges between 30 and 20%. In this minireview we describe the conservation of specific amino acids and the various CYP51 orthologs and indicate the roles that they may play in the structure/function of this monooxygenase. The prediction of the roles of different amino acids in 14DM is based on high resolution tertiary structures of these enzymes which set the stage for detailed understanding of the 14 alpha-demethylase reaction and its selective, phyla-specific inhibition which is crucial for the design of potent inhibitors for treatment of infection by pathogenic microbes. (C) 2010 Elsevier By. All rights reserved.
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