|
rdf:type |
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|
lifeskim:mentions |
umls-concept:C0001898,
umls-concept:C0015127,
umls-concept:C0017890,
umls-concept:C0180860,
umls-concept:C0243144,
umls-concept:C0318255,
umls-concept:C0392747,
umls-concept:C0547047,
umls-concept:C0581406,
umls-concept:C0597484,
umls-concept:C0851827,
umls-concept:C1314792,
umls-concept:C1373200,
umls-concept:C1510827,
umls-concept:C1522664,
umls-concept:C1546465,
umls-concept:C1546637,
umls-concept:C1550638,
umls-concept:C1701901,
umls-concept:C1704240,
umls-concept:C1704449,
umls-concept:C1704684,
umls-concept:C1705175,
umls-concept:C1705176,
umls-concept:C1705177,
umls-concept:C1705178,
umls-concept:C1882348
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|
pubmed:issue |
3
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|
pubmed:dateCreated |
1999-7-22
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|
pubmed:abstractText |
KtrAB from Vibrio alginolyticus is a recently described new type of high affinity bacterial K+ uptake system. Its activity assayed in an Escherichia coli K+ uptake negative mutant depended on Na+ ions (Km of 40 microM). Subunit KtrB contains four putative P-loops. The selectivity filter from each P-loop contains a conserved glycine residue. Residue Gly-290 from the third P-loop selectivity filter in KtrB was exchanged for Ala, Ser or Asp. KtrB variants Ser-290 and Asp-290 were without activity. In contrast, KtrB variant Ala-290 was still active. This variant transported K+ with a two orders of magnitude decrease in apparent affinity for both K+ and Na+ with little effect on Vmax.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
450
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
217-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10359077-Alanine,
pubmed-meshheading:10359077-Amino Acid Sequence,
pubmed-meshheading:10359077-Amino Acid Substitution,
pubmed-meshheading:10359077-Bacterial Proteins,
pubmed-meshheading:10359077-Carrier Proteins,
pubmed-meshheading:10359077-Cation Transport Proteins,
pubmed-meshheading:10359077-Glycine,
pubmed-meshheading:10359077-Membrane Proteins,
pubmed-meshheading:10359077-Molecular Sequence Data,
pubmed-meshheading:10359077-Mutagenesis,
pubmed-meshheading:10359077-Potassium,
pubmed-meshheading:10359077-Sodium,
pubmed-meshheading:10359077-Vibrio
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pubmed:year |
1999
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pubmed:articleTitle |
Change to alanine of one out of four selectivity filter glycines in KtrB causes a two orders of magnitude decrease in the affinities for both K+ and Na+ of the Na+ dependent K+ uptake system KtrAB from Vibrio alginolyticus.
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pubmed:affiliation |
Abteilung Mikrobiologie, Universität Osnabrück, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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