ACTIVITY OF NMN+, NICOTINAMIDE RIBOSE AND ANALOGS IN ALCOHOL OXIDATION PROMOTED BY HORSE-LIVER ALCOHOL-DEHYDROGENASE - IMPROVEMENT OF THIS ACTIVITY AND STRUCTURAL REQUIREMENTS OF THE PYRIDINE-NUCLEOTIDE PART OF THE NAD+ COENZYME

被引：26

作者：

SICSIC, S ^{[1
]}

DURAND, P ^{[1
]}

LANGRENE, S ^{[1
]}

LEGOFFIC, F ^{[1
]}

机构：

[1] CNRS, CTR ETUDES & RECH CHIM ORGAN APPL, BOITE POSTALE 28, F-94320 THIAIS, FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1986年 / 155卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1986.tb09505.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Kinetic constants of horse-liver alcohol-dehydrogenase-mediated oxidation of alcohol by nicotinamide mononucleotide and nicotinamide ribose were determined and the role of different adenine moieties complementing the reaction mixtures was investigated. Five nicotinamide ribose analogs were synthesized and their activities as NAD+ inhibitors and as cofactors in this dehydrogenase-mediated oxidation of alcohol were assayed. In the light of these results, structural requirements of the pyridine ribofuranosyl part of the NAD+ are discussed.

引用

页码：403 / 407

页数：5

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