Kinetic analysis of the mechanism of action of beta-glucosidase from Botryodiplodia theobromae Pat.
1. The kinetic mechanism of beta-glucosidase (beta-D-glucoside glucohydrolase, EC 3.2.1.21) of Botryodiplodia theobromae Pat. has been studied in the presence of competing glucosyl acceptors. 2. Glycerol, fructose, sucrose, cellobiose and to a much lesser extent, maltose can act as glucosyl acceptors, apart from water. 3. Evidence confirming and supporting the kinetic mechanism previously postulated (Umezurike, G.M. (1971) Biochim. Biophys. Acta. 250, 182-191) is presented. 4. A theoretical kinetic analysis of the behaviour of the enzyme in the presence of two alternative glucosyl acceptors in addition to water is found to be consistent with experimental observation, suggesting a system in which both donor and acceptors bind to the enzyme in a random fashion to form ternary complexes. 5. The results are discussed in terms of the mechanism of group-transfer reactions.
D050260:Carbohydrate Metabolism; D002845:Chromatography; D004305:Dose-Response Relationship, Drug; D005959:Glucosidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005990:Glycerol / Q000378:metabolism; D007700:Kinetics; D008320:Maltose / Q000378:metabolism / Q000494:pharmacology; D003904:Mitosporic Fungi / Q000201:enzymology*; D008954:Models, Biological; D009844:Oligosaccharides / Q000378:metabolism; D013329:Structure-Activity Relationship
D009844:Oligosaccharides; D008320:Maltose; D005959:Glucosidases; D005990:Glycerol