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Point mutation of a conserved arginine (104) to lysine introduces hypersensitivity to inhibition by glyphosate in the 5‐enolpyruvylshikimate‐3‐phosphate synthase of Bacillus subtilis
Author(s) -
Selvapandiyan Angamuthu,
Majumder Kumud,
Fattah Farkad A.,
Ahmad Suhail,
Arora Naresh,
Bhatnagar Raj K.
Publication year - 1995
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(95)01124-w
Subject(s) - shikimate pathway , bacillus subtilis , biochemistry , mutant , arginine , lysine , chemistry , site directed mutagenesis , amino acid , mutagenesis , glutamine , tryptophan synthase , enzyme , biology , biosynthesis , tryptophan , bacteria , genetics , gene
The role of a conserved arginine (R104) in the putative phosphoenol pyruvate binding region of 5‐enolpyruvyl shikimate‐3‐phosphate synthase of Bacillus subtilis has been investigated. Employing site directed mutagenesis arginine was substituted by lysine or glutamine. Native and mutant proteins were expressed and purified to near homogeneity. Estimation of Michaelis and inhibitor constants of the native and mutant proteins exhibited altered substrate—inhibitor binding mode and constants. Mutation R104K hypersensitized the enzyme reaction to inhibition by glyphosate. The role of R104 in discriminating between glyphosate and phosphoenol pyruvate is discussed.