PMID:19799945: Difference between revisions
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!align=left |Citation | |||
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'''Li, L, Lu, W, Han, Y, Ping, S, Zhang, W, Chen, M, Zhao, Z, Yan, Y, Jiang, Y and Lin, M''' (2009) A novel RPMXR motif among class II 5-enolpyruvylshikimate-3-phosphate synthases is required for enzymatic activity and glyphosate resistance. ''J. Biotechnol.'' '''144''':330-6 | |||
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!align=left |Abstract | |||
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The shikimate pathway enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an attractive target for drugs and herbicides. Here we identified a novel RPMXR motif that is strictly conserved among class II EPSP synthases. Site-directed mutational analysis of this motif showed that substitutions of the four strictly conserved amino acid residues, Arg127, Pro128, Met129, and Arg131, resulted in complete loss of enzymatic activity, whereas changes in the non-conserved Asn130 residue strongly influenced glyphosate resistance (all numbering according to Pseudomonas stutzeri A1501 EPSP synthase). These experimental results, combined with 3D structure modeling of the location and interaction of the RPMXR motif with phosphoenolpyruvate (PEP) and shikimate-3-phosphate (S3P), demonstrate that the novel motif is required for enzymatic activity and glyphosate resistance of class II EPSP synthases. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19799945 PubMed] | |||
Online version:[http://dx.doi.org/10.1016/j.jbiotec.2009.09.014 10.1016/j.jbiotec.2009.09.014] | |||
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!align=left |Keywords | |||
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3-Phosphoshikimate 1-Carboxyvinyltransferase/antagonists & inhibitors; 3-Phosphoshikimate 1-Carboxyvinyltransferase/chemistry; 3-Phosphoshikimate 1-Carboxyvinyltransferase/metabolism; Amino Acid Motifs; Amino Acid Sequence; Conserved Sequence; Drug Resistance, Bacterial; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Glycine/analogs & derivatives; Glycine/pharmacology; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate/metabolism; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism; Structure-Activity Relationship | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
<protect><annotationlinks/></protect> | |||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
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==See also== | |||
==References== | |||
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Latest revision as of 04:35, 15 September 2013
| Citation |
Li, L, Lu, W, Han, Y, Ping, S, Zhang, W, Chen, M, Zhao, Z, Yan, Y, Jiang, Y and Lin, M (2009) A novel RPMXR motif among class II 5-enolpyruvylshikimate-3-phosphate synthases is required for enzymatic activity and glyphosate resistance. J. Biotechnol. 144:330-6 |
|---|---|
| Abstract |
The shikimate pathway enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase is an attractive target for drugs and herbicides. Here we identified a novel RPMXR motif that is strictly conserved among class II EPSP synthases. Site-directed mutational analysis of this motif showed that substitutions of the four strictly conserved amino acid residues, Arg127, Pro128, Met129, and Arg131, resulted in complete loss of enzymatic activity, whereas changes in the non-conserved Asn130 residue strongly influenced glyphosate resistance (all numbering according to Pseudomonas stutzeri A1501 EPSP synthase). These experimental results, combined with 3D structure modeling of the location and interaction of the RPMXR motif with phosphoenolpyruvate (PEP) and shikimate-3-phosphate (S3P), demonstrate that the novel motif is required for enzymatic activity and glyphosate resistance of class II EPSP synthases. |
| Links |
PubMed Online version:10.1016/j.jbiotec.2009.09.014 |
| Keywords |
3-Phosphoshikimate 1-Carboxyvinyltransferase/antagonists & inhibitors; 3-Phosphoshikimate 1-Carboxyvinyltransferase/chemistry; 3-Phosphoshikimate 1-Carboxyvinyltransferase/metabolism; Amino Acid Motifs; Amino Acid Sequence; Conserved Sequence; Drug Resistance, Bacterial; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Glycine/analogs & derivatives; Glycine/pharmacology; Models, Molecular; Mutagenesis, Site-Directed; Phosphoenolpyruvate/metabolism; Shikimic Acid/analogs & derivatives; Shikimic Acid/metabolism; Structure-Activity Relationship |
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