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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Oxygen-18 leaving group kinetic isotope effects (KIEs) have been measured for a set of glycosyl transfer reactions with p-nitrophenyl beta-D-glycosides as substrates. Acid-catalyzed hydrolysis and alkaline hydrolysis exhibit KIEs of K16/k18 = 1.0355 +/- 0.0015 and 1.0386 +/- 0.0032, respectively. Lysozyme and beta-glucosidase A show KIEs on Vmax/Km (V/K) of (V/KI)16/(V/K)18 = 1.0467 +/- 0.0015 and 1.0377 +/0 0.0061, respectively. The large magnitude of these KIEs requires that carbon-oxygen bond scission be far advanced in the transition states for these reactions; therefore in the transition states for the first irreversible steps in these reaction sequences, scission of the glycosidic bond must be essentially complete for the reactions catalyzed by lysozyme and beta-glucosidase A, which are thought to proceed via SN1 and SN2 mechanisms, respectively. Acid-catalyzed hydrolysis is shown to proceed through a transition state involving at least 80% C-O bond cleavage and only partially proton transfer to the leaving p-nitrophenyl oxygen atom.
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PMID:Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysis. 678 83

A beta-glucosidase with the molecular mass of 160,000 Da was purified to homogeneity from cell extract of a cellulolytic bacterium, Cellulomonas uda CS1-1. The kinetic parameters (Km and Vmax) of the enzyme were determined with pNP-cellooligosccharides (DP 1-5) and cellobiose. The molecular orbital theoretical studies on the cellulolytic reactivity between the pNP-cellooligosaccharides as substrate (S) molecules and the purified beta-glucosidase (E) were conducted by applying the frontier molecular orbital (FMO) interaction theory. The results of the FMO interaction between E and S molecules verified that the first stage of the reaction was induced by exocyclic cleavage, which occurred in an electrophilic reaction based on a strong charge-controlled reaction between the highest occupied molecular orbital (HOMO) energy of the S molecule and the lowest occupied molecular orbital (LUMO) energy of the hydronium ion (H3O+), more than endocyclic cleavage, whereas a nucleophilic substitution reaction was induced by an orbital-controlled reaction between the LUMO energy of the oxonium ion (SH+) protonated to the S molecule and the HOMO energy of the H2O2 molecule. A hypothetic reaction route was proposed with the experimental results in which the enzymatic acid-catalyst hydrolysis reaction of E and S molecules would be progressed via SN1 and SN2 reactions. In addition, the quantitative structure-activity relationships (QSARs) between these kinetic parameters showed that Km has a significant correlation with hydrophobicity (logP), and specific activity has with dipole moment, respectively.
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PMID:Molecular orbital theory on cellulolytic reactivity between pNP-cellooligosccharides and beta-glucosidase from Cellulomonas uda CS1-1. 1809 62