Transglycosylation activity of alpha-D-galactosidase from Trichoderma reesei. An investigation of the active site

Carbohydrate Research
E V EneyskayaK N Neustroev

Abstract

The transglycosylation reaction catalyzed by alpha-D-galactosidase from the mycelial fungus Trichoderma reesei was studied using p-nitrophenyl alpha-D-galactopyranoside (PNPG). An aliphatic alcohol or the substrate itself can be an acceptor of the galactose residue in this reaction. The transglycosylation products were identified as alkyl galactosides in the case of alcohols or as galactobioside and galactotrioside in the case of PNPG. The transglycosylation rates follow a first-order equation with respect to the alcohol concentrations except for methanol. Affinities of some substrates were estimated from their Ki values in the reaction of the enzyme with PNPG. Transglycosylation of the substrate suggests a model for the enzyme active center. It is proposed that the active center includes two galactose-binding sites and a hydrophobic site.

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Citations

Nov 24, 2001·Clinica Chimica Acta; International Journal of Clinical Chemistry·A N Savel'evK N Neustroev
Aug 13, 2003·Bioscience, Biotechnology, and Biochemistry·Thida SripuanHidehiko Kumagai
Apr 1, 2014·Applied Microbiology and Biotechnology·Veličković DušanDimitrijević Aleksandra
Dec 17, 2004·Organic & Biomolecular Chemistry·Elena V EneyskayaKirill N Neustroev
Jan 6, 2018·World Journal of Microbiology & Biotechnology·Barbora StratilováRenáta Vadkertiová
Jun 11, 2003·Biochemistry·David L ZechelStephen G Withers

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