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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1976-10-29
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pubmed:abstractText |
Nitrogenase biosynthesis in Klebsiella pneumoniae including mutant strains, which produce nitrogenase in the presence of NH+4 (Shanmugam, K.T., Chan, Irene, and Morandi, C. (1975) Biochim. Biophys. Acta 408, 101--111) is repressed by a mixture of L-amino acids. Biochemical analysis shows that glutamine synthetase activity in strains SK-24, SK-28, and SK-29 is also repressed by amino acids, with no detectable effect on glutamate dehydrogenase. Among the various amino acids, L-glutamine in combination with L-aspartate was found to repress nitrogenase biosynthesis completely. In the presence of high concentrations of glutamine (1 mg/ml) even NH+4 repressed nitrogenase biosynthesis in the strains SK-27, SK-37, SK-55 and SK-56. Under these conditions, increased glutamate dehydrogenase activity was also detected. Physiological studies show that nitrogenase derepressed strains are unable to utilize NH+4 as sole source of nitrogen for biosynthesis of glutamate for biosynthesis of glutamate, whereas back mutations leading to NH+4 utilization results in sensitivity to repression by NH+4. These findings suggest that amino acids play an important role as regulators of nitrogen fixation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate-Ammonia Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
437
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
322-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8101-Amino Acids,
pubmed-meshheading:8101-Aspartic Acid,
pubmed-meshheading:8101-Enzyme Repression,
pubmed-meshheading:8101-Glutamate Dehydrogenase,
pubmed-meshheading:8101-Glutamate-Ammonia Ligase,
pubmed-meshheading:8101-Glutamine,
pubmed-meshheading:8101-Klebsiella pneumoniae,
pubmed-meshheading:8101-Models, Biological,
pubmed-meshheading:8101-Mutation,
pubmed-meshheading:8101-Nitrogenase,
pubmed-meshheading:8101-Species Specificity
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pubmed:year |
1976
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pubmed:articleTitle |
Amino acids as repressors of nitrogenase biosynthesis in Klebsiella pneumoniae.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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