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A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation.

Abstract：

:A single nucleotide polymorphism (SNP) resulting in a substitution from Gln to His was found in exon 4 of the CYP2B6 gene in Japanese. The frequency of the variant allele was found to be 19.9%. The mutant- and the wild-type enzymes were expressed in Escherichia coli, and the effects of the single amino acid substitution on the catalytic activity were examined by investigating the kinetic profiles of 7-ethoxycoumarin O-deethylase activity. The wild-type enzyme showed typical Michaelis-Menten kinetics, while the mutant-type enzyme represented the sigmoidal kinetics with a higher V(max) value compared to that of the wild-type enzyme. Eadie-Hofstee plots further revealed an existence of allosteric effects for the reaction catalyzed by the variant. This is the first evidence demonstrating that only one amino acid substitution, Gln172His, caused by natural SNP enhances the catalytic activity of CYP by obtaining the character of homotropic cooperativity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ariyoshi N,Miyazaki M,Toide K,Sawamura Yi,Kamataki T

doi

10.1006/bbrc.2001.4524

subject

Has Abstract

pub_date

2001-03-01 00:00:00

pages

1256-60

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006291X01945243

journal_volume

281

pub_type

杂志文章

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