Document Detail


Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity.
MedLine Citation:
PMID:  23334916     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Cytochromes P450 comprise a large superfamily and several of their isoforms play a crucial role in metabolism of xenobiotics, including drugs. Although these enzymes demonstrate broad and cross-substrate specificity, different cytochrome P450 subfamilies exhibit certain selectivity for some types of substrates. Analysis of amino acid residues of the active sites of six cytochrome subfamilies (CYP1А, CYP2А, CYP2С, CYP2D, CYP2E and CYP3А) enables to define subfamily-specific patterns that consist of four residues. These residues are located on the periphery of the active sites of these cytochromes. We suggest that they can form a primary binding site at the entrance to the active site, defining cytochrome substrate recognition. Copyright © 2013 John Wiley & Sons, Ltd.
Authors:
Maria S Zharkova; Boris N Sobolev; Nina Yu Oparina; Alexander V Veselovsky; Alexander I Archakov
Related Documents :
24487036 - Quantitative proteomics of sesuvium portulacastrum leaves revealed ions transportation ...
8955376 - Analysis of the reaction mechanism of the non-specific endonuclease of serratia marcesc...
24338896 - Structures of reduced and ligand-bound nitric oxide reductase provide insights into fun...
23090406 - Structural characterization of a modification subunit of a putative type i restriction ...
9054576 - On the mechanism of the inhibition of transducin function by farnesylcysteine analogs.
22320426 - Crystal structure of the enzyme capf of staphylococcus aureus reveals a unique architec...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular recognition : JMR     Volume:  26     ISSN:  1099-1352     ISO Abbreviation:  J. Mol. Recognit.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9004580     Medline TA:  J Mol Recognit     Country:  England    
Other Details:
Languages:  eng     Pagination:  86-91     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 John Wiley & Sons, Ltd.
Affiliation:
Orekhovich Institute of Biomedical Chemistry of Russian Academy of Medical Sciences, Pogodinskaya str., 10, Moscow, 119121, Russia.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Mapping of heparin/heparan sulfate binding sites on ?v?3 integrin by molecular docking.
Next Document:  Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.