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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-9-26
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pubmed:abstractText |
The guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg2+ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2-3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Tsmt were 5-10-fold less active in stimulating the activity of EF-Tumt. The double mutation completely abolished the activity of EF-Tsmt.
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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 |
Aug
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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 |
12
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pubmed:volume |
391
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
330-2
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
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pubmed:year |
1996
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pubmed:articleTitle |
Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange.
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pubmed:affiliation |
Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.
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pubmed:publicationType |
Journal Article
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