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Article

Why is quinidine an inhibitor of cytochrome P450 2D6? The role of key active-site residues in quinidine binding.

The Journal of biological chemistry - 18 Nov 2005

McLaughlin Lesley A, Paine Mark J I, Kemp Carol A, Maréchal Jean-Didier, Flanagan Jack U, Ward Clive J, Sutcliffe Michael J, Roberts Gordon C K, Wolf C Roland

Abstract excerpt

We have previously shown that Phe(120), Glu(216), and Asp(301) in the active site of cytochrome P450 2D6 (CYP2D6) play a key role in substrate recognition by this important drug-metabolizing enzyme (Paine, M. J., McLaughlin, L. A., Flanagan, J. U., Kemp, C. A., Sutcliffe, M. J., Roberts, G. C., and Wolf, C. R. (2003) J. Biol. Chem. 278, 4021-4027 and Flanagan, J. U., Maréchal, J.-D., Ward, R., Kemp, C. A.,...

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PMID: 16162505
DOI: 10.1074/jbc.M505974200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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