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5‐Enolpyruvylshikimate‐3‐phosphate synthase from Staphylococcus aureus is insensitive to glyphosate
Author(s) -
Priestman Melanie A.,
Funke Todd,
Singh Inder M.,
Crupper Scott S.,
Schönbrunn Ernst
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.057
Subject(s) - shikimate pathway , staphylococcus aureus , phosphoenolpyruvate carboxykinase , enzyme , chemistry , glyphosate , atp synthase , biochemistry , bacteria , microbiology and biotechnology , biology , genetics
The enzyme 5‐enolpyruvylshikimate‐3‐phosphate synthase (EPSPS) catalyzes the penultimate step of the shikimate pathway, and is the target of the broad‐spectrum herbicide glyphosate. Kinetic analysis of the cloned EPSPS from Staphylococcus aureus revealed that this enzyme exerts a high tolerance to glyphosate, while maintaining a high affinity for its substrate phosphoenolpyruvate. Enzymatic activity is markedly influenced by monovalent cations such as potassium or ammonium, which is due to an increase in catalytic turnover. However, insensitivity to glyphosate appears to be independent from the presence of cations. Therefore, we propose that the Staphylococcus aureus EPSPS should be classified as a class II EPSPS. This research illustrates a critical mechanism of glyphosate resistance naturally occurring in certain pathogenic bacteria.