Kinetic investigation of the substrate specificity of the cyanogenic beta-D-glucosidase (linamarase) of white clover.

@article{Pcsi1989KineticIO,
  title={Kinetic investigation of the substrate specificity of the cyanogenic beta-D-glucosidase (linamarase) of white clover.},
  author={Istv{\'a}n P{\'o}csi and L{\'a}szl{\'o} Kiss and Monica A. Hughes and P{\'a}l N{\'a}n{\'a}si},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={272 2},
  pages={496-506}
}
Partially purified linamarase from Trifolium repens (genotype Lili acac) plants was kinetically characterized. Kinetic evidence was found to support the assumption that this cyanogenic beta-D-glucosidase has a broad substrate spectrum. p-Nitrophenyl-beta-D-xylopyranoside and p-nitrophenyl-alpha-L-arabinopyranoside substrates bound almost as tightly to the active center of the enzyme as the glucono(1----5)lactone transition-state analog inhibitor. Substrate specificity investigation also… CONTINUE READING