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Inhibition by N'-nitrosonornicotine of the catalytic activity of glutamate dehydrogenase in alpha-ketoglutarate amination.

作者信息

Mao You-An, Zhong Ke-Jun, Wei Wan-Zhi, Wei Xin-Liang, Lu Hong-Bing

机构信息

Postdoctorate Working Station, Changde Cigarette Factory, Changde 415000, China.

出版信息

J Enzyme Inhib Med Chem. 2005 Feb;20(1):89-94. doi: 10.1080/14756360410001733702.

DOI:10.1080/14756360410001733702
PMID:15895690
Abstract

The effect of N'-nitrosonornicotine (NNN), one of the tobacco-specific nitrosamines, on the catalytic activity of glutamate dehydrogenase (GLDH) in the alpha-ketoglutarate amination, using reduced nicotinamide adenine dinucleotide as coenzyme, was studied by a chronoamperometric method. The maximum reaction rate of the enzyme-catalyzed reaction and the Michaelis-Menten constant, or the apparent Michaelis-Menten constant, were determined in the absence and presence of NNN. NNN remarkably inhibited the bio-catalysis activity of GLDH, and was a reversible competitive inhibitior with K(i), estimated as 199 micromol l(-1) at 25 degrees C and pH 8.0.

摘要

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