Relationship of l-alanine and l-glutamate dehydrogenases of Bacillus thuringienses

Borris, David P.; Aronson, John N.

doi:10.1016/0005-2744(69)90366-0

Cited by 14 publications

(2 citation statements)

References 11 publications

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“…Only one species of Bacillus (thuringiensis) was reported to contain NAD-dependent GDH activity and this organism apparently lacks an NADP-dependent enzyme (4). These investigators (4) suggested that the NAD-specific GDH activity is associated with a protein tetramer which is interconvertible with a trimer which then exhibits NAD-specific L-alanine dehydrogenase activity. McCormick and Halvorson (23) were unable to detect GDH activity in extracts of B. cereus T, and highly purified NAD-specific L-alanine dehydrogenase from this organism was not found to exhibit GDH activity.…”

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confidence: 99%

Purification, Properties, and Regulation of Glutamic Dehydrogenase ofBacillus licheniformis

Phibbs

Bernlohr

1971

J Bacteriol

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Cell-free extracts of Bacillus licheniformis and B. cereus were found to contain high specific activities of nicotinamide adenine dinucleotide phosphate (NADP)-dependent- l -glutamate dehydrogenase [EC 1.4.1.4; l -glutamate: NADP oxidoreductase (deaminating)]. Maximum specific activities were found in extracts of cells during the late exponential phase of growth when ammonium ion served as the sole source of nitrogen. Extremely low specific activities were detected throughout the growth cycle when l -glutamate or Casamino Acids served as the source of carbon and nitrogen. The enzyme was purified 55-fold from crude extracts of B. licheniformis , and apparent kinetic constants were determined. Sigmoidal saturation kinetics were not observed, and various adenylates had no effect on the enzyme. Repression of enzyme synthesis during growth on l -glutamate or Casamino Acids was partially overcome by additions of glucose or pyruvate, and this apparent derepression was totally abolished by inhibitors of ribonucleic acid and protein synthesis. Similarly, additions of l -glutamate or Casamino Acids to cells growing on glucose-ammonium ion resulted in strong repression of enzyme synthesis. It is suggested that the enzyme serves an anabolic role in metabolism. Nicotinamide adenine dinucleotide-dependent glutamate dehydrogenase activity was not detected in five species of Bacillus , irrespective of nutritional conditions or of the physiological age of cells.

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confidence: 99%

Purification, Properties, and Regulation of Glutamic Dehydrogenase ofBacillus licheniformis

Phibbs

Bernlohr

1971

J Bacteriol

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“…The transfer of nitrogen from glutamate to other metabolites is catalyzed mainly by glutamate oxaloacetate transaminase and, to a lesser extent, by glutamate pyruvate transaminase and glutamate dehydrogenase. The pathways for ammonia assimilation are catabolized by alanine dehydrogenase and glutamate dehydrogenase (26,30). Although glutamate synthase and glutamine synthetase have been found in Bacillus megaterium (31,32), Bacillus licheniformis (33), and Bacillus subtilis (34), as far as the authors are aware, no report about the presence of this system in BT has been made.…”

Section: Nitrogen Metabolismmentioning

confidence: 99%

Bacillus thuringiensis growth and toxicity

Avignone–Rossa¹,

Mignone²

1995

Mol Biotechnol

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A further characterization of alanine dehydrogenase from Streptomyces aureofaciens

Vančurová

Vančura

Volc

et al. 1989

J. Basic Microbiol.

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Homogeneous alanine dehydrogenase isolated from Streptomyces aureofaciens, a producer of tetracycline, was characterized from the point of its molecular and catalytic properties. Using analytical ultracentrifugation the molecular weight of alanine dehydrogenase was found to be 198,000. The enzyme could use as cofactors apart from NAD+ also 1,N6-etheno-NAD+, 3-acetylpyridine-NAD+, deamino-NAD+ and nicotinamide guanine dinucleotide. The enzyme activity in the direction of oxidative deamination was not affected by the addition of nonsubstrate amino acids, however, it was sensitive to inhibitors of SH-groups. Reductive amination of pyruvate was inhibited by L-alanine, L-serine and D-alanine. The inhibition by L-alanine and L-serine was uncompetitive with respect to NADH and noncompetitive with regard to pyruvate and ammonium ions.

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Relationship of l-alanine and l-glutamate dehydrogenases of Bacillus thuringienses

Cited by 14 publications

References 11 publications

Purification, Properties, and Regulation of Glutamic Dehydrogenase ofBacillus licheniformis

Purification, Properties, and Regulation of Glutamic Dehydrogenase ofBacillus licheniformis

Bacillus thuringiensis growth and toxicity

A further characterization of alanine dehydrogenase from Streptomyces aureofaciens

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