PMID: 2508630Sep 1, 1989Paper

Kinetic analysis of the interaction of alkyl glycosides with two human beta-glucosidases

The Biochemical Journal
V GopalanM Claeyssens

Abstract

This paper addresses the similarities and differences in the topology of the catalytic centres of human liver cytosolic beta-glucosidase and placental lysosomal glucocerebrosidase, and utilizes well-documented reversible active-site-directed inhibitors. This comparative kinetic study was performed mainly to decipher the chemical and structural nature of the active site of the cytosolic beta-glucosidase, whose physiological function is unknown. Specifically, analysis of the effects of a family of alkyl beta-glucosides consistently displayed 100-250-fold lower inhibition constants with the cytosolic broad-specificity beta-glucosidase compared with the placental glucocerebrosidase; for example, with octyl beta-D-glucoside the Ki values were 10 microM and 1490 microM for the cytosolic and lysosomal beta-glucosidases respectively. Furthermore the higher affinity of the cytosolic beta-glucosidase than glucocerebrosidase for the amphipathic alkyl beta-D-glucosides was validated by the greater increase in the free energy of binding with increasing alkyl chain length [delta delta G0 (K,)/CH2: lysosomal enzyme, 2.01 kJ/mol (480 cal/mol); cytosolic enzyme, 3.05 kJ/mol (730 cal/mol)]. The implications of the presence of highly non-polar do...Continue Reading

Citations

Aug 24, 2010·Blood Cells, Molecules & Diseases·Nick DekkerJohannes M F G Aerts
Jun 14, 2017·Critical Reviews in Food Science and Nutrition·Bincy BabyRanjit Vijayan
Jun 1, 1991·Journal of Neurosurgery·T ShiraishiM Takagi
Jun 17, 2011·Biochemistry·Mahendra S SandbhorChristopher W Cairo

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