Studeis on subsites in the active sites of β-linked disaccharides-hydrolyzing enzymes on the basis of detail examination of their substrate specificities

April 01, 2015

◆Grant-in-Aid for Scientific Research (JSPS) "Scientific Research (C)"

◆Leader : KANZAKI Hiroshi

◆FY2015 - FY2017

β-N-Acetylhexosaminidase (HexNAcase) and β-glucosidase (β-Glcase) catalyze the hydrolysis of chitobiose and cellobiose obtained from chitin and cellobiose, respecticely. We isolated a novel HexNAcase inihibtor, TMG-chitotriomycin (1), and found that GH20 HexNAcases were divided into 1-sensitve and 1-insensitive enzymes. We also revealed that GH3 β-Glcases were divided into several groups depend on the basis of their substrate specificities. This study aims at examining detail properties of these enzymes useful for their application.