Mutants of Pseudomonas aeruginosa unable to inactivate allantoinase and NADP-dependent glutamate dehydrogenase.
Both allantoinase and NADP-GDH in Pseudomonas aeruginosa were inactivated when cells reached the stationary phase of growth. Mutants unable to inactivate these enzymes were isolated. Results with recombinants showed that the mutation is not located in the structural genes of these enzymes but in an independent gene involved in the inactivation.
D000481:Allantoin / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism*; D003227:Conjugation, Genetic; D003470:Culture Media; D004794:Enzyme Repression; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D014510:Urease / Q000378:metabolism
D003470:Culture Media; D000481:Allantoin; D005969:Glutamate Dehydrogenase; D000581:Amidohydrolases; D014510:Urease; C019659:allantoinase; D005974:Glutamate-Ammonia Ligase