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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
1991-12-26
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pubmed:abstractText |
The active site of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) has been probed using site-directed mutagenesis and inhibitor binding techniques. Replacement of a specific glycyl with an alanyl or a prolyl with a seryl residue in a highly conserved region confers glyphosate tolerance to several bacterial and plant EPSPS enzymes, suggesting a high degree of structural conservation between these enzymes. The glycine to alanine substitution corresponding to Escherichia coli EPSPS G96A increases the Ki(app) (glyphosate) of petunia EPSPS 5000-fold while increasing the Km(app)(phosphoenolpyruvate) about 40-fold. Substitution of this glycine with serine, however, abolishes EPSPS activity but results in the elicitation of a novel EPSP hydrolase activity whereby EPSP is converted to shikimate 3-phosphate and pyruvate. This highly conserved region is critical for the interaction of the phosphate moiety of phosphoenolpyruvate with EPSPS.
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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 |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22364-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1939260-3-Phosphoshikimate 1-Carboxyvinyltransferase,
pubmed-meshheading:1939260-Alkyl and Aryl Transferases,
pubmed-meshheading:1939260-Amino Acid Sequence,
pubmed-meshheading:1939260-Bacteria,
pubmed-meshheading:1939260-Binding Sites,
pubmed-meshheading:1939260-Biological Evolution,
pubmed-meshheading:1939260-Escherichia coli,
pubmed-meshheading:1939260-Kinetics,
pubmed-meshheading:1939260-Molecular Sequence Data,
pubmed-meshheading:1939260-Mutagenesis, Site-Directed,
pubmed-meshheading:1939260-Plants,
pubmed-meshheading:1939260-Plasmids,
pubmed-meshheading:1939260-Saccharomyces cerevisiae,
pubmed-meshheading:1939260-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1939260-Species Specificity,
pubmed-meshheading:1939260-Transferases
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pubmed:year |
1991
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pubmed:articleTitle |
Site-directed mutagenesis of a conserved region of the 5-enolpyruvylshikimate-3-phosphate synthase active site.
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pubmed:affiliation |
Monsanto Agricultural Company, New Products Division, Chesterfield, Missouri.
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pubmed:publicationType |
Journal Article,
Comparative Study
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