The purification and properties of a beta-N-acetylhexosaminidase from Trichomonas foetus.
A beta-N-acetylhexosaminidase was purified 800-fold from extracts of Trichomonas foetus by affinity chromatography on a column of N-(epsilon-aminohexanoyl)-2-acetamido-2-deoxy-beta-D-glucopyranosylamine bound to CNBr-activated Sepharose. The enzyme has a dual specificity for the p-nitrophenyl beta-D-glycosides of N-acetylglucosamine and N-acetyl-galactosamine. The parent sugars are both competitive inhibitors. The enzyme has a mol. wt. approx. 150000 and a pH optimum of 6.2. It is suggested that the same active site catalyses both activities and that no part is played by the 4-hydroxyl group in substrate binding, but it is involved in determining the catalytic rate.
D000116:Acetylgalactosamine / Q000031:analogs & derivatives / Q000378:metabolism; D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000378:metabolism; D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006596:Hexosaminidases / Q000302:isolation & purification*; D007700:Kinetics; D008970:Molecular Weight; D014244:Trichomonas / Q000201:enzymology*
D006596:Hexosaminidases; D000116:Acetylgalactosamine; D000117:Acetylglucosamine