Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mutants were isolated from Pseudomonas aeruginosa that were impaired in the utilization of a number of nitrogen sources. In contrast to the wild-type strain, these mutants appeared to be unable to derepress the formation of glutamine synthetase and urease under nitrogen-limited growth conditions, whereas NADP-dependent glutamate dehydrogenase became derepressed. This GlnR- phenotype appeared to be caused by a mutation located in the early region of the P. aeruginosa PAO chromosomal map, close to hisIV59. Partial suppression of the GlnR- phenotype due to a mutation located close to hisII4 was observed. These revertants were different from both the wild-type strain and the GlnR- mutant with respect to the regulation of the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase (GlnRc phenotype). Also the regulation of glutamine synthetase activity by adenylylation/deadenylylation was altered in the revertants. The results suggest the presence of a regulatory gene that plays a role in the regulation of enzyme formation in response to the availability of ammonia.
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PMID:Nitrogen control in Pseudomonas aeruginosa: mutants affected in the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase. 612 99

The formation of amidase was studied in mutants from Pseudomonas aeruginosa PAO lacking glutamine synthetase activity. It appeared that catabolite repression of amidase synthesis by succinate was partially relieved when cellular growth was limited by glutamine. Under these conditions, a correlation between amidase and urease formation was observed. The results suggest that amidase formation in strain PAO is subject to nitrogen control and that glutamine or some compound derived from it mediates the nitrogen repression of amidase.
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PMID:Regulation of amidase formation in mutants from Pseudomonas aeruginosa PAO lacking glutamine synthetase activity. 612 69