Regulatory control and function of alanine dehydrogenase from a thermophilic bacillus.
L-alanine dehydrogenase, (L-alanine:NAD+ oxidoreductase (deaminating), EC 1.4.1.1) synthesis in a thermophilic bacillus was found to be subjected to regulatory control. Addition of L- and D-alanine and L-serine to cultures growing in the presence of either succinate or pyruvate, induced an accelerated synthesis of the alanine dehydrogenase enzyme. Synthesis of the enzyme was dependent on the presence of inducer during growth and was arrested by addition of glucose. Catabolite repression by glucose was abolished by limiting the ammonium concentration during growth. The apparent Km values of the substrates involved in alanine dehydrogenase activity are as follows (M): NH4+, 4-10(-2); pyruvate, 5-10(-4); NADH, 6-10(-5); L-alanine, 3.1-10(-3) and NAD, 2-10(-4). Alanine dehydrogenase activity was measurable at temperatures below the minimal growth temperature (at 25 degrees C) and the highest activity was found at 65 degrees C; heat denaturation occurred at 80 degrees C.
D000409:Alanine; D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000596:Amino Acids / Q000494:pharmacology; D000641:Ammonia / Q000494:pharmacology; D001407:Bacillus / Q000201:enzymology*; D002455:Cell Division; D004355:Drug Stability; D004790:Enzyme Induction / Q000187:drug effects; D004794:Enzyme Repression; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics
D000596:Amino Acids; D000641:Ammonia; D000594:Amino Acid Oxidoreductases; D000409:Alanine