the methylotrophic thermo tolerant actinomycete strain 381, was isolated from a compost sample, assimilated methanol during growth. methanol dehydrogenase could not be detected in cell extracts using dye-linked assays in the absence of nad+. dichlorophenol-indophenol-linked methanol oxidation was detected in broken cell suspensions in the presence of nad+ and the absence of cyanide. taxonomic s...

some kinetic properties of nad+- and nadp+- dependent glucose 6-phosphatedehydrogenase (g6pd) purified from streptomyces aureofaciens were studied. both nadh andnadph inhibited the enzyme competitively and noncompetitively, with respect to the correspondingcoenzymes and glucose 6-phosphate, respectively. atp inhibited the nad+ - linked reaction but not thatof the nadp+- linked activity. the inh...

Nicotinamide-adenine dinucleotide (NAD+) synthetases catalyze the last step in NAD+ metabolism in the de novo, import, and salvage pathways that originate from tryptophan (or aspartic acid), nicotinic acid, and nicotinamide, respectively, and converge on nicotinic acid mononucleotide. NAD+ synthetase converts nicotinic acid adenine dinucleotide to NAD+ via an adenylylated intermediate. All of t...

each region through immunofluorescence, cross-linking Pacific Hall 0347 and chromatin immunoprecipitation, and biochemical 9500 Gilman Drive purification. SIR2 is not itself essential for viability, but La Jolla, California 92093 sir2⌬ null mutants have a number of phenotypes. In addition to transcriptional silencing defects, sir2⌬ strains have increased rates of recombination within Pundits an...

An indication of the ability of NAD-independent variants of Haemophilus paragallinarum to evade the immune system has been obtained from data obtained from several experiments. Firstly, it was noted that there was a difference in the serovar distribution between the NAD-dependent isolates in the 1990s and the NAD-independent isolates, as there was a significant decrease in the incidence of sero...

The Bacillus methanolicus methanol dehydrogenase (MDH) is a decameric nicotinoprotein alcohol dehydrogenase (family III) with one Zn(2+) ion, one or two Mg(2+) ions, and a tightly bound cofactor NAD(H) per subunit. The Mg(2+) ions are essential for binding of cofactor NAD(H) in MDH. A B. methanolicus activator protein strongly stimulates the relatively low coenzyme NAD(+)-dependent MDH activity...