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Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity
Author(s) -
Zharkova Maria S.,
Sobolev Boris N.,
Yu. Opariina,
Veselovsky Alexander V.,
Archakov Alexander I.
Publication year - 2013
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2251
Subject(s) - subfamily , cytochrome p450 , biochemistry , cytochrome , substrate (aquarium) , active site , amino acid residue , gene isoform , substrate specificity , xenobiotic , enzyme , biology , isozyme , binding site , stereochemistry , chemistry , peptide sequence , gene , ecology
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.