PMID: 2502070Aug 1, 1989Paper

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

Archives of Biochemistry and Biophysics
I PócsiP Nánási

Abstract

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 indicated that positions C-4 and C-6 on the pyranoside ring play an essential role in both substrate orientation and splitting. Recently very similar kinetic characteristics were reported on some mammalian cytosolic beta-D-glucosidases and a possible physiological interpretation of this coincidence is discussed. Inhibition studies with glucono(1----5)lactone revealed that the carbohydrate moiety of each substrate attached to the same binding site in the active center. Inhibition experiments with 1-thio substrate analogs demonstrated that the aglycon and the angular arrangement around the glycosidic linkage were the major determinants in the observed substrate specificity.

References

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Citations

May 24, 2003·Biochemical and Biophysical Research Communications·Jisnuson SvastiRakrudee Sarnthima
Jun 25, 1999·Bioscience, Biotechnology, and Biochemistry·M PetruccioliF Federici
Nov 18, 2005·Phytochemistry·Dumrongkiet ArthanJisnuson Svasti
Apr 1, 1999·Biotechnology and Bioengineering·M Cicek, A Esen
Jul 11, 2008·Biopolymers·Anthony D Hill, Peter J Reilly
May 13, 2008·Phytochemistry·Anne Vinther MorantSøren Bak

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