PMID: 3109376Jan 15, 1987

The mechanism of action of beta-glucosidase from Botryodiplodia theobromae Pat

The Biochemical Journal
G M Umezurike


The activity of the high-molecular-weight beta-glucosidase (beta-D-glucoside glucohydrolase, EC obtained from culture filtrates of Botryodiplodia theobromae Pat. was affected by added NaCl in such a way that an initial phase of stimulation was followed by a phase of rapid non-linear decrease in velocity and finally by a phase of slow linear decrease in velocity as the concentration of NaCl was increased. In the presence of 0.014 M-sodium acetate/acetic acid buffer (pH 5.0) there was a slight increase in enzymic activity in the presence of low concentrations of dioxan (up to about 10% dioxan) and a rapid decrease in enzymic activity at higher dioxan concentrations, but both effects were mitigated in the presence of 0.1 M buffer. The order of efficiency of added glucosyl acceptors in beta-glucosidase-catalysed reactions was found to be fructose greater than sucrose greater than glycerol greater than methanol. The enzyme was inactivated by the active-site-directed compound conduritol-B-epoxide; but this inactivation was concentration-dependent, was prevented by 10 mM-glucose, and involved an acidic group with pKa 4.3. A rate equation has been derived on the assumption of a mechanism of action involving a solvent-separate...Continue Reading


Aug 31, 2004·The Journal of Biological Chemistry·Stephanie N HicksElizabeth E Howell

Related Concepts

Conduritol C epoxide
Emulsion beta-D-Glucosidase
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