Journal
JOURNAL OF BIOTECHNOLOGY
Volume 144, Issue 4, Pages 330-336Publisher
ELSEVIER
DOI: 10.1016/j.jbiotec.2009.09.014
Keywords
Class II; 5-enolpyruvylshikimate-3-phosphate synthase; RPMXR motif; Enzymatic activity; Glyphosate resistance; Pseudomonas stutzeri A1501
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Funding
- National Basic Research Program of China [2007CB109203]
- National High-Tech Program of China [2007AA021304]
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The shikimate pathway enzyme 5-enolpyruvyishikimate-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, Prol 28, 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. (C) 2009 Elsevier B.V. All rights reserved.
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