Regulation of nitrogen fixation in Azotobacter vinelandii OP and in an apparently partially constitutive mutant.
Methylamine and 2-methylalanine appeared to act as co-repressors of nitrogenase in Azotobacter vinelandii OP. They inhibited the growth of this organism on molecular nitrogen but not on nitrate, ammonia, or Casamino Acids; they prevented the formation of nitrogenase by cells transferred from repression to induction conditions; and they did not inhibit the activity of nitrogenase in vitro. A mutant of strain OP, selected on the basis of its relative resistance to methylalanine, appeared partially constitutive because nitrogenase in this strain was less sensitive to repressors than was the enzyme in the wild-type strain.
D000409:Alanine / Q000494:pharmacology; D000588:Amines / Q000494:pharmacology; D000641:Ammonia / Q000494:pharmacology; D001395:Azotobacter / Q000187:drug effects / Q000378:metabolism*; D004794:Enzyme Repression; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism; D009154:Mutation; D009586:Nitrogen Fixation; D010088:Oxidoreductases / Q000378:metabolism
D000588:Amines; D000641:Ammonia; D010088:Oxidoreductases; D005954:Glucosephosphate Dehydrogenase; D000409:Alanine