Binding of maltose to Rhizopus niveus glucoamylase in the pH range where the catalytic carboxyl groups are ionized
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry
Reference16 articles.
1. Kinetic Studies on Gluc-amylase
2. a D. French and M. Ohnishi, in preparation
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1. Kinetics of Some Selected Enzyme-Catalysed Reactions in Organic Solvents;Enzymatic Transformation;2012-11-19
2. Competitive substrate inhibition of amyloglucosidase fromRhizopussp. by vanillin and curcumin;Biocatalysis and Biotransformation;2006-01
3. Catalytic mechanism of enzymic glycosyl transfer;Chemical Reviews;1990-11-01
4. A pH-induced change in state around active-site tryptophan residues of Rhizopus niveus glucoamylase, detected by stopped-flow studies of chemical modification with N-bromosuccinimide;Carbohydrate Research;1990-03
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