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Titolo:
MOLECULAR MODELING OF CYTOCHROME P4502D6 (CYP2D6) BASED ON AN ALIGNMENT WITH CYP102 - STRUCTURAL STUDIES ON SPECIFIC CYP2D6 SUBSTRATE METABOLISM
Autore:
LEWIS DFV; EDDERSHAW PJ; GOLDFARB PS; TARBIT MH;
Indirizzi:
UNIV SURREY,SCH BIOL SCI,MOL TOXICOL GRP GUILDFORD GU2 5XH SURREY ENGLAND GLAXO GRP RES LTD,RES & DEV WARE SG12 0DP HERTS ENGLAND
Titolo Testata:
Xenobiotica
fascicolo: 4, volume: 27, anno: 1997,
pagine: 319 - 339
SICI:
0049-8254(1997)27:4<319:MMOCP(>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIVER-MICROSOMES; AMINO-ACID; GENETIC-POLYMORPHISM; SPARTEINE METABOLISM; DEBRISOQUINE; OXIDATION; 2D6; INHIBITION; ALLELE; HYDROXYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
66
Recensione:
Indirizzi per estratti:
Citazione:
D.F.V. Lewis et al., "MOLECULAR MODELING OF CYTOCHROME P4502D6 (CYP2D6) BASED ON AN ALIGNMENT WITH CYP102 - STRUCTURAL STUDIES ON SPECIFIC CYP2D6 SUBSTRATE METABOLISM", Xenobiotica, 27(4), 1997, pp. 319-339

Abstract

1. A molecular model of CYP2D6 has been constructed from the bacterial form CYP102 via a homology alignment between the CYP2D subfamily andCYP102 protein sequences. 2. A number of typical CYP2D6 substrates are shown to fit the putative active site of the enzyme, as can the specific inhibitor quinidine. 3. Some of the allelic variants in CYP2D6, which give rise to genetic polymorphisms in 2D6-mediated metabolism, can be rationalized in terms of their position within the active site region. 4. The results of site-directed mutagenesis experiments are consistent with the CYP2D6 model generated from the CYP102 crystal structure. 5. The possibility of an alternative orientation within the activesire may explain the CYP2D6-mediated metabolism of relatively large sized substrates.

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Documento generato il 07/04/20 alle ore 23:15:57