1. A single residue mutation of 5-enoylpyruvylshikimate-3-phosphate synthase in Pseudomonas stutzeri enhances resistance to the herbicide glyphosate
- Author
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Ming Chen, Yiding Wang, Liang Li, Dan Jin, Min Lin, Wei Zhang, Jin Wang, Aimin Liang, Yongliang Yan, Wei Lu, Shuzhen Ping, and Jiying Sha
- Subjects
Mutant ,Glycine ,Bioengineering ,Biology ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Serine ,medicine ,Asparagine ,Escherichia coli ,Phylogeny ,Pseudomonas stutzeri ,Herbicides ,Aroa ,Wild type ,General Medicine ,biology.organism_classification ,Complementation ,Kinetics ,Amino Acid Substitution ,Biochemistry ,Genes, Bacterial ,Mutation ,Mutant Proteins ,3-Phosphoshikimate 1-Carboxyvinyltransferase ,Herbicide Resistance ,Biotechnology - Abstract
A novel class II 5-enoylpyruvylshikimate-3-phosphate synthase (EPSPS) was identified from Pseudomonas stutzeri A1501 by complementation of an Escherichia coli auxotrophic aroA mutant. The single amino acid substitution of serine (Ser) for asparagine (Asn)-130 of the A1501 EPSPS enhanced resistance to 200 mM glyphosate. The mutated EPSPS had a 2.5-fold increase for IC(50) [glyphosate] value, a 2-fold increase for K (i) [glyphosate] value, but a K (m) [PEP] value similar to that of wild type. The effect of the single residue mutation on glyphosate resistance was also analyzed using a computer-based three-dimensional model.
- Published
- 2008
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