Source:http://linkedlifedata.com/resource/pubmed/id/14715237
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-1-12
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pubmed:abstractText |
An analysis is made of the rate constants for the reactions involving the interactions of EF-Tu, EF-Ts, GDP, and GTP recently derived by Gromadski et al. [Biochemistry 41 (2002) 162]. Though their measured values appear to allow a reasonable rate of nucleotide exchange sufficient to support rates of protein synthesis in vivo, their data underestimate the thermodynamic barrier involved in nucleotide exchange and therefore cannot be considered definitive. A kinetic scheme consistent with the thermodynamic barrier can be achieved by modification of various rate constants, particularly of those involving the release of EF-Ts from EF-Tu.GTP.EF-Ts, but such constants are markedly different from what are experimentally observed. It thus remains impossible at present satisfactorily to model guanine nucleotide exchange on EF-Tu, catalysed by EF-Ts by a double displacement mechanism, with experimentally derived rate constants. Metabolic control analysis has been applied to determine the degree of flux control of the different steps in the pathway.
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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/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factor Tu,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/elongation factor Ts
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
314
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14715237-Computer Simulation,
pubmed-meshheading:14715237-Energy Metabolism,
pubmed-meshheading:14715237-Escherichia coli,
pubmed-meshheading:14715237-GTP-Binding Proteins,
pubmed-meshheading:14715237-Guanine Nucleotides,
pubmed-meshheading:14715237-Guanosine Diphosphate,
pubmed-meshheading:14715237-Guanosine Triphosphate,
pubmed-meshheading:14715237-Kinetics,
pubmed-meshheading:14715237-Models, Biological,
pubmed-meshheading:14715237-Peptide Elongation Factor Tu,
pubmed-meshheading:14715237-Peptide Elongation Factors,
pubmed-meshheading:14715237-Protein Binding
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pubmed:year |
2004
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pubmed:articleTitle |
Determination of the kinetics of guanine nucleotide exchange on EF-Tu and EF-Ts: continuing uncertainties.
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pubmed:affiliation |
School of Molecular and Cell Biology, University of the Witwatersrand, Johannesburg, South Africa. kmanches@gecko.biol.wits.ac.za
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pubmed:publicationType |
Journal Article,
Comparative Study,
Evaluation Studies,
Validation Studies
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