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Article

Analysis of differential substrate selectivities of CYP2B6 and CYP2E1 by site-directed mutagenesis and molecular modeling.

The Journal of pharmacology and experimental therapeutics - 1 Jan 2003

Spatzenegger Margit, Liu Hong, Wang Qinmi, Debarber Andrea, Koop Dennis R, Halpert James R

Abstract excerpt

Human CYP2B6 and CYP2E1 were used to investigate the extent to which differential substrate selectivities between cytochrome P450 subfamilies reflect differences in active-site residues as opposed to distinct arrangement of the backbone of the enzymes. Reciprocal CYP2B6 and CYP2E1 mutants at active-site positions 103, 209, 294, 363, 367, and 477 (numbering according to CYP2B6) were characterized using the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytochrome P-450 CYP2B6

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Share to Oxidoreductases, N-Demethylating

Source

Identifiers

PMID: 12490624
DOI: 10.1124/jpet.102.043323

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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