Correlation of human cytochrome P4502C substrate specificities with primary structure: warfarin as a probe

The regio- and stereoselectivity of warfarin metabolism have been used to assess structure-function relationships of human P4502C subfamily members. Metabolism was investigated using a yeast cDNA expression system in which full length cDNAs for P4502C8, -2C9 (alleles Arg144 Tyr358 Ile359 Gly417 and...

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Veröffentlicht in:	Molecular pharmacology 1993-02, Vol.43 (2), p.234-239
Hauptverfasser:	KAMINSKY, L. S, DE MORAIS, S. M. F, FALETTO, M. B, DUNBAR, D. A, GOLDSTEIN, J. A
Format:	Artikel
Sprache:	eng
Schlagworte:	Alleles Base Sequence Biological and medical sciences Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism General pharmacology Humans Hydroxylation Medical sciences Molecular Sequence Data Mutagenesis, Site-Directed Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions Pharmacology. Drug treatments Recombinant Proteins - metabolism Stereoisomerism Structure-Activity Relationship Substrate Specificity Warfarin - metabolism
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