title: Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity.
abstract: 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.
authors: Orekhovich Institute of Biomedical Chemistry of Russian Academy of Medical Sciences, Pogodinskaya str 10, Moscow 119121, Russia.
authors: Maria S
authors: MS
authors: Zharkova
authors: Boris N
authors: BN
authors: Sobolev
authors: Nina
authors: N
authors: Yu Oparina
authors: Alexander V
authors: AV
authors: Veselovsky
authors: Alexander I
authors: AI
authors: Archakov
mesh_terms: D020816:Amino Acid Motifs; D020134:Catalytic Domain; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D030562:Databases, Protein; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System