Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity.
J Mol Recognit
; 26(2): 86-91, 2013 Feb.
Article
em En
| MEDLINE
| ID: mdl-23334916
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 (CYP1Ð, CYP2Ð, CYP2С, CYP2D, CYP2E and CYP3Ð) 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.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Sistema Enzimático do Citocromo P-450
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Limite:
Humans
Idioma:
En
Revista:
J Mol Recognit
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Federação Russa