Inhibition by N′-nitrosonornicotine of the catalytic activity of glutamate dehydrogenase in α-ketoglutarate amination
| Autor: | Hongbing Lu, Wanzhi Wei, Ke-Jun Zhong, Youan Mao, Xin-Liang Wei |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Nitrosamines
Reduced nicotinamide-adenine dinucleotide Binding Competitive Medicinal chemistry Catalysis Cofactor chemistry.chemical_compound Alpha ketoglutarate Glutamate Dehydrogenase Drug Discovery Animals Enzyme Inhibitors Amination Pharmacology biology Glutamate dehydrogenase Maximum reaction rate General Medicine NAD Liver Biochemistry chemistry N-Nitrosonornicotine biology.protein Ketoglutaric Acids Cattle |
| Zdroj: | Journal of Enzyme Inhibition and Medicinal Chemistry. 20:89-94 |
| ISSN: | 1475-6374 1475-6366 |
| DOI: | 10.1080/14756360410001733702 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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