Some Details of the Reaction Mechanism of Glucoamylase from Aspergillus Niger- Kinetic and Structural Studies on Trp52Phe and Trp317Phe Mutants
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1997.00638.x/fullpdf
Reference47 articles.
1. Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution.
2. Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.
3. Refined Crystal Structures of Glucoamylase from Aspergillus awamori var. X100
4. Crystallographic Complexes of Glucoamylase with Maltooligosaccharide Analogs: Relationship of Stereochemical Distortions at the Nonreducing End to the Catalytic Mechanism,
5. Thermodynamics of Inhibitor Binding to Mutant Forms of Glucoamylase from Aspergillus niger Determined by Isothermal Titration Calorimetry
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