Nov 1, 1993

Chemical modification of beta-glucosidase from Trichoderma reesei QM 9414

Journal of Biochemistry
I de la MataC Acebal

Abstract

The inhibition of beta-glucosidase from Trichoderma reesei QM 9414 by several specific reagents was studied. Diethylpyrocarbonate (DEP) nearly abolished the enzyme activity at concentrations above 10 mM. The presence of substrate or analogs protected the enzyme against inactivation. The reaction followed pseudo-first order kinetics with a second-order rate constant of 0.02 mM-1.min-1. The pH-dependence of the inactivation showed the involvement of a group with a pK of 5.2. Difference spectra at 242 nm and the reversal of the inactivation in the presence of 1 M hydroxylamine indicated the modification of histidine residues. Statistical analysis of residual fractional activity versus the number of modified histidine residues indicated that one histidine residue is essential for catalysis. p-Hydroxymercuribenzoate completely inhibited the enzyme at concentrations of the reagent above 2 mM. Substrate or analogs protected the enzyme against inactivation. The reaction followed pseudo-first order kinetics with a second-order rate constant of 0.002 mM-1.min-1. Treatment of the modified enzyme with 5,5'-dithio-bis(2-nitrobenzoic acid) (DTNB) showed that one cysteine residue was essential for activity. At pH 5.0 2-ethoxy-1-ethoxy-carbony...Continue Reading

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Mentioned in this Paper

4-hydroxymercuribenzoate
BC 681
Beta-Glucosidase
Histidine
Pseudo brand of pseudoephedrine
Quinolines
Analog
Dithionitrobenzoic Acid
Trichoderma reesei
Sodium p-hydroxymercury benzoate

About this Paper

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