The active site of β-glucosidase from Botryodiplodia theobromae. Effects of pH and dioxan on enzyme-catalysed reactions
- 1 December 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 167 (3) , 831-833
- https://doi.org/10.1042/bj1670831
Abstract
1. The hydrolysis of o-nitrophenyl beta-D-glucopyranoside by the high-molecular-weight beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) of Botryodiplodia theobromae Pat in the absence or presence of added dioxan was found to be dependent on the ionization of two groups, which appeared to be a carboxyl group and an imidazole group. 2. Dioxan increased the Michaelis constant, Km, but decreased the maximum velocity, V.This publication has 10 references indexed in Scilit:
- Kinetic analysis of the mechanism of action of β-glucosidase from Botryodiplodia theobromae Pat.Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
- The subunit structure of β-glucosidase from Botryodiplodia theobromae PatBiochemical Journal, 1975
- Kinetic properties of β-glucosidase from Botryodiplodia theobromae pat.Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
- The purification and properties of extracellular β-glucosidase from Botryodiplodia theobromae Pat.Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
- Inhibition, transgalactosylation and mechanism of action of sweet almond α-galactosidaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- Peptides Derived from Tryptic Digestion of Egg White LysozymeJournal of Biological Chemistry, 1963
- The active site and mechanism of action of bovine pancreatic ribonuclease. 5. The charge types at the active centreBiochemical Journal, 1962
- The mechanism of ficin-catalysed reactionsBiochemical Journal, 1959
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934