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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1990-3-28
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pubmed:abstractText |
Two transport systems for L-arginine were evident in Anabaena sp. strain PCC 7120: a high-affinity one (Km, 1.7 microM) that accumulated arginine within the cells through an energy-requiring process and another one that exhibited low affinity for L-arginine (Km, 0.75 mM) and was unable to accumulate the substrate. Both systems were inhibited by L-canavanine, L-lysine, and L-ornithine. Two systems were also evident for L-lysine uptake (Km, 1.9 and 110 microM, respectively). After selection for resistance to canavanine or hydroxylysine, independent mutants were isolated which were impaired in the high-affinity uptake of arginine and lysine. A common permease appears, therefore, to be involved in the high-affinity transport of these basic amino acids. Both the high- and the low-affinity systems can contribute to the growth of Anabaena sp. on L-arginine. However, arginine did not effectively repress either nitrogenase or nitrate reductase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
265
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3931-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2105956-Amino Acids, Diamino,
pubmed-meshheading:2105956-Arginine,
pubmed-meshheading:2105956-Biological Transport,
pubmed-meshheading:2105956-Cyanobacteria,
pubmed-meshheading:2105956-Dicyclohexylcarbodiimide,
pubmed-meshheading:2105956-Kinetics,
pubmed-meshheading:2105956-Mutation,
pubmed-meshheading:2105956-Nitrogen Fixation
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pubmed:year |
1990
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pubmed:articleTitle |
Transport of basic amino acids by the dinitrogen-fixing cyanobacterium Anabaena PCC 7120.
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pubmed:affiliation |
Instituto de Bioquímica Vegetal y Fotosintesis, Universidad de Sevilla, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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