Urease of Klebsiella aerogenes: control of its synthesis by glutamine synthetase.
Urease was purified 24-fold from extracts of Klebsiella aerogenes. The enzyme has a molecular weight of 230,000 as determined by gel filtration, is highly substrate specific, and has a Km for urea of 0.7 mM. A mutant strain lacking urease was isolated; it failed to grow with urea as the sole source of nitrogen but did grow on media containing other nitrogen sources such as ammonia, histidine, or arginine. Urease was present at a high level when the cells were starved for nitrogen; its synthesis was repressed when the external ammonia concentration was high. Formation of urease did not require induction by urea and was not subject to catabolite repression. Its synthesis was controlled by glutamine synthetase. Mutants lacking glutamine synthetase failed to produce urease, and mutants forming glutamine synthetase at a high constitutive level also formed urease constitutively. Thus, the formation of urease is regulated like that of other enzymes of K. aerogenes capable of supplying the cell with ammonia or glutamate.
D004794:Enzyme Repression; D005796:Genes; D005974:Glutamate-Ammonia Ligase / Q000096:biosynthesis / Q000378:metabolism*; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis; D007700:Kinetics; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D008970:Molecular Weight; D009154:Mutation; D014508:Urea / Q000378:metabolism; D014510:Urease / Q000096:biosynthesis* / Q000302:isolation & purification
D014508:Urea; D014510:Urease; D006638:Histidine Ammonia-Lyase; D005974:Glutamate-Ammonia Ligase