rdf:type |
|
lifeskim:mentions |
umls-concept:C0017797,
umls-concept:C0019601,
umls-concept:C0028158,
umls-concept:C0033809,
umls-concept:C0035820,
umls-concept:C0041945,
umls-concept:C0061461,
umls-concept:C0220781,
umls-concept:C0220905,
umls-concept:C0851285,
umls-concept:C1883254,
umls-concept:C2587213
|
pubmed:issue |
4
|
pubmed:dateCreated |
1981-6-25
|
pubmed:abstractText |
In Pseudomonas aeruginosa the formation of urease, histidase and some other enzymes involved in nitrogen assimilation is repressed by ammonia in the growth medium. The key metabolite in this process appears to be glutamine or a product derived from it, since ammonia and glutamate did not repress urease and histidase synthesis in a mutant lacking glutamine synthetase activity when growth was limited for glutamine. The synthesis of these enzymes was repressed in cells growing in the presence of excess glutamine. High levels of glutamine were also required for the derepression of NADP-dependent glutamate dehydrogenase formation in the glutamine synthetase-negative mutant.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0302-8933
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
128
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
398-402
|
pubmed:dateRevised |
2000-12-18
|
pubmed:meshHeading |
pubmed-meshheading:6111986-Ammonia,
pubmed-meshheading:6111986-Glutamate Dehydrogenase,
pubmed-meshheading:6111986-Glutamate-Ammonia Ligase,
pubmed-meshheading:6111986-Glutamates,
pubmed-meshheading:6111986-Glutamine,
pubmed-meshheading:6111986-Histidine Ammonia-Lyase,
pubmed-meshheading:6111986-Mutation,
pubmed-meshheading:6111986-Nitrates,
pubmed-meshheading:6111986-Nitrogen,
pubmed-meshheading:6111986-Pseudomonas aeruginosa,
pubmed-meshheading:6111986-Urease
|
pubmed:year |
1981
|
pubmed:articleTitle |
Nitrogen control in Pseudomonas aeruginosa: a role for glutamine in the regulations of the synthesis of nadp-dependent glutamate dehydrogenase, urease and histidase.
|
pubmed:publicationType |
Journal Article
|