Why is quinidine an inhibitor of cytochrome P450 2D6? The role of key active-site residues in quinidine binding. (Q46703082)

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6 January 2020

title

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

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Mark John Ingraham Paine

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Jean-Didier Maréchal

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Mike Sutcliffe

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C Roland Wolf

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Carol A Kemp

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Lesley A McLaughlin

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author name string

Jack U Flanagan

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Clive J Ward

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language of work or name

English

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publication date

14 September 2005

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Journal of Biological Chemistry

6 January 2020

published in

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volume

280

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issue

46

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page(s)

38617-38624

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Polymorphic hydroxylation of Debrisoquine in man.

6 January 2020

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Inhibition of cytochrome P450 2D6: structure-activity studies using a series of quinidine and quinine analogues

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Impact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.

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Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis

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Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6.

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Determinants of the substrate specificity of human cytochrome P-450 CYP2D6: design and construction of a mutant with testosterone hydroxylase activity

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Phe120 contributes to the regiospecificity of cytochrome P450 2D6: mutation leads to the formation of a novel dextromethorphan metabolite.

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Comparative protein modelling by satisfaction of spatial restraints

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High-resolution crystal structure of cytochrome P450cam

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Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution

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Structure of cytochrome P450eryF involved in erythromycin biosynthesis

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Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's

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Influence of phenylalanine 120 on cytochrome P450 2D6 catalytic selectivity and regiospecificity: crucial role in 7-methoxy-4-(aminomethyl)-coumarin metabolism

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The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid

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NMR studies of substrate binding to cytochrome P450 BM3: comparisons to cytochrome P450 cam.

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Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation

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21 January 2018

Identifiers

DOI

10.1074/JBC.M505974200

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6 January 2020

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