A metaphosphate-dependent nicotinamide adenine dinucleotide kinase from Brevibacterium ammoniagenes.
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منابع مشابه
Inhibition 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 کاملThe stereospecificity of nicotinamide-adenine dinucleotide-dependent oxidoreductases from plants.
1. The stereospecificity of 20 enzymes from plants is reported. 2. The stereospecificity of all known forms of malate dehydrogenase in plants and animals has been shown to be A-specific. 3. The generalization that ;the stereospecificity of a particular reaction is independent of the source of the enzyme' is confirmed for a total of 12 plant enzymes. 4. A new generalization is proposed: ;When a ...
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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 ...
متن کاملRegulation of the nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenases of Saccharomyces cerevisiae.
Saccharomyces cerevisiae contains two distinct l-glutamate dehydrogenases. These enzymes are affected in a reciprocal fashion by growth on ammonia or dicarboxylic amino acids as the nitrogen source. The specific activity of the nicotinamide adenine dinucleotide phosphate (NADP) (anabolic) enzyme is highest in ammonia-grown cells and is reduced in cells grown on glutamate or aspartate. Conversel...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1980
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.44.1165