Interaction of catalytic-site mutants of Bacillus subtilis α-amylase with substrate and acarbose
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference19 articles.
1. Site-directed mutagenesis of active site residues in Bacillus subtilis α-amylase
2. Structure and Possible Catalytic Residues of Taka-Amylase A
3. Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity.
4. The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA
5. NH2-terminal processing of Bacillus subtilis alpha-amylase.
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2. Liver alpha-amylase gene expression as an early obesity biomarker;Pharmacological Reports;2017-04
3. Cloning, molecular characterization and heterologous expression of AMY1, an α-amylase gene from Cryptococcus flavus;FEMS Microbiology Letters;2008-03
4. Crystal Structure of Bacillus subtilis α-Amylase in Complex with Acarbose;Journal of Bacteriology;2003-12
5. A Novel Approach to Anellated Carbasugar Derivatives, Using Intramolecular 1,3-Dipolar Cycloaddition Reactions of Sugar-Derived Nitrones;European Journal of Organic Chemistry;2001-02
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