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Characterization of a glyphosate‐insensitive 5‐enolpyruvylshikimic acid‐3‐phosphate synthase
Author(s) -
Sost Dietrich,
Schulz Arno,
Amrhein Nikolaus
Publication year - 1984
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 - 10.1016/0014-5793(84)81054-6
Subject(s) - biochemistry , enzyme , glycine , carbamoyl phosphate synthetase , chemistry , shikimate pathway , atp synthase , phosphate , biology , microbiology and biotechnology , amino acid
A glyphosate ( N ‐[phosphonomethyl]glycine)‐insensitive 5‐enolpyruvylshikimic acid‐3‐phosphate (EPSP) synthase has been purified from a strain of Klebsiella pneumoniae which is resistant to this herbicide [(1984) Arch. Microbiol. 137, 121‐123] and its properties compared with those of the glyphosate‐sensitive EPSP synthase of the parent strain. The apparent K m values of the insensitive enzyme for phospho enol pyruvate (PEP) and shikimate 3‐phosphate (S‐3‐P) were increased 15.6‐ and 4.3‐fold, respectively, as compared to those of the sensitive enzyme, and significant differences were found for the optimal pH and temperature, as well as the isoelectric points of the two enzymes. While PEP protected both enzymes against inactivation by N ‐ethylmaleimide, 3‐bromopyruvate, and phenylglyoxal, glyphosate protected only the sensitive enzyme.