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• W1995688538 abstract "• A novel aroA gene was identified from deep-sea bacteria, Alcanivorax sp . L27. • AroA A .sp exhibited activity between pH 5.5 and pH 8.0 and low temperatures. • The K M for PEP and IC50 [glyphosate] of AroA A .sp were investigated. • Site-directed mutagenesis was performed to increase the activity of AroA A .sp . • The specific activities of the wild-type and mutant AroA A .sp were determined. The 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) is a key enzyme in the aromatic amino acid biosynthetic pathway in microorganisms and plants, which catalyzes the formation of 5-enolpyruvylshikimate-3-phosphate (EPSP) from shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP). In this study, a novel AroA-encoding gene was identified from the deep sea bacterium Alcanivorax sp. L27 through screening the genomic library and termed as AroA A .sp . A phylogenetic analysis revealed that AroA A .sp (1317 bp and 438 amino acids) is a class II AroA. This enzyme exhibited considerable activity between pH 5.5 and pH 8.0 and notable activity at low temperatures. The K M for PEP and IC 50 [glyphosate] values (the concentration of glyphosate that inhibited enzyme activity by 50%) of AroA A .sp were 78 μM and 1.5 mM, respectively. Furthermore, site-directed mutagenesis revealed that the G100A mutant had a 30-fold increase in the IC 50 [glyphosate] value; while the L105P mutant showed only 20% catalytic activity compared to wild-type AroA A .sp . The specific activity of the wild-type AroA A .sp , the G100A mutant and the L105P mutant were 7.78 U/mg, 7.26 U/mg and 1.76 U/mg, respectively. This is the first report showing that the G100A mutant of AroA displays considerably improved glyphosate resistance and demonstrates that Leu105 is essential for the enzyme's activity." @default.
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• W1995688538 date "2014-09-01" @default.
• W1995688538 modified "2023-09-27" @default.
• W1995688538 title "Characterization and site-directed mutagenesis of a novel class II 5-enopyruvylshikimate-3-phosphate (EPSP) synthase from the deep-sea bacterium Alcanivorax sp. L27" @default.
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• W1995688538 doi "https://doi.org/10.1016/j.enzmictec.2014.02.010" @default.
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