Rudee SuraritHirokazu MatsuiSeiya ChibaJisnuson SvastiChantragan SrisomsapMahidol UniversityHokkaido UniversityChulabhorn Research Institute2018-07-042018-07-041996-01-01Bioscience, Biotechnology and Biochemistry. Vol.60, No.8 (1996), 1265-126813476947091684512-s2.0-0029804739https://repository.li.mahidol.ac.th/handle/20.500.14594/17570Studies have been done on the inhibition and inactivation of the β-glucosidase and β-fucosidase enzyme from Thai Rosewood (Dalbergia cochinchinesis Pierre). The enzyme was inhibited by Tris with similar Kiof 11.7 mm and 14.3 mm for the hydrolysis of p/nitrophenyl β-d-glucoside (PNPG) and p/nitrophenyl β-d-fucoside (PNPF), respectively. Conduritol B epoxide inhibited both β-glucosidase and β/fucosidase activities to similar extents, with a pseudo-first-order rate constant (Kobs) of inactivation of 5.56 × 10−3s−1, and binding stoichiometry of 0.9 mol per subunit. Partially inactivated enzyme showed similar kinetics with PNPG and PNPF as substrates. Moreover, Tris at 300 mm protected both β-glucosidase and β-fucosidase activities from inactivation by 6mm CBE. The data support the idea that the Dalbergia cochinchinensis Pierre enzyme has a common active site for the hydrolysis of PNPG and PNPF. © 1996, Taylor & Francis Group, LLC. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemistryImmunology and MicrobiologyArticleSCOPUS10.1271/bbb.60.1265