Nicotinamide Adenine Dinucleotide Kinase from Azotobacter vinelandii
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چکیده
منابع مشابه
Reduced nicotinamide-adenine dinucleotide-nitrite reductase from Azotobacter chroococcum.
1. The assimilatory nitrite reductase of the N(2)-fixing bacterium Azotobacter chroococcum was prepared in a soluble form from cells grown aerobically with nitrate as the nitrogen source, and some of its properties have been studied. 2. The enzyme is a FAD-dependent metalloprotein (mol.wt. about 67000), which stoicheiometrically catalyses the direct reduction of nitrite to NH(3) with NADH as th...
متن کاملRestoration by ubiquinone of Azotobacter vinelandii reduced nicotinamide adenine dinucleotide oxidase activity.
Extraction with pentane virtually abolished reduced nicotinamide adenine dinucleotide oxidase activity in small particles from Azotobacter vinelandii, but activity was largely restored by added ubiquinone.
متن کاملInhibition of rat liver nicotinamide adenine dinucleotide kinase by reduced nicotinamide adenine dinucleotide phosphate.
Rat liver NAD kinase (ATP : NAD 2’-phosphotransferase, EC 2.7.1.23) was purified about 70-fold. The MichaelisMenten constants (Km) for NAD and ATP were 8 x 10e4 M and 2 x low3 M, respectively. NAD kinase activity was markedly inhibited by NADH and also NADPH. The Ki of NADH was approximately 1 X 10q4 M, and that of NADPH was approximately 5 X 10M5 M. Both inhibitions were competitive with NAD, ...
متن کاملSubstituted Nicotinamide Analogues of Nicotinamide Adenine Dinucleotide.
A number of nicotinamide adenine dinucleotide analogues have been prepared in which the purine, pyridine, and ribose moieties have been modified (2-12). These analogues have proven to be valuable in studies dealing with the site of binding of the pyridine coenzyme to dehydrogenases, in elucidating the mechanism of dehydrogenases and the configuration of the pyridme coenzymes, and as indicators ...
متن کاملSubstituted Nicotinamide Analogues of Nicotinamide Adenine Dinucleotide*
A number of nicotinamide adenine dinucleotide analogues have been prepared in which the purine, pyridine, and ribose moieties have been modified (2-12). These analogues have proven to be valuable in studies dealing with the site of binding of the pyridine coenzyme to dehydrogenases, in elucidating the mechanism of dehydrogenases and the configuration of the pyridme coenzymes, and as indicators ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1967
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96161-2