| Literature DB >> 21157 |
Abstract
Glutamine synthetase could be repressed several hundredfold rather than 6- to 10-fold as previously reported. Ammonia was not the primary repression signal for glutamine synthetase. Repression appeared to be mediated by a high level of glutamine and probably by a high ratio of glutamine to alpha-ketoglutarate. Mutations in glnA (the structural gene for glutamine synthetase) were seen to fall into three phenotypic groups: glutamine auxotrophs that produced no detectable glnA product; glutamine auxotrophs that produced a glnA product lacking enzymatic activity (and hence repressibility by ammonia) but were repressible under appropriate conditions; and glutamine synthetase regulatory mutants, whose glnA product was enzymatically active and not repressible under any conditions.Entities:
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Year: 1977 PMID: 21157 PMCID: PMC221831 DOI: 10.1128/jb.132.1.100-105.1977
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490