Effect of modifying histidine residues on the action of Bacillus amyloliquefaciens and barley-malt α-amylases
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry
Reference24 articles.
1. Selective inhibition of histidine-modified pancreatic α-amylase by proteinaceous inhibitor from Phaseolus vulgaris
2. New substrate specificity of modified porcine pancreatic α-amylase
3. Substrate-Selective Activation of Histidine-Modified Porcine Pancreatic α-Amylase by Chloride Ion
4. Kinetic Study on Chemical Modification of Taka-Amylase A. II. Ethoxycarbonylation of Histidine Residues
5. Structure and Possible Catalytic Residues of Taka-Amylase A
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1. Chemical Modification of Lysine Residues in Bacillus licheniformis α-Amylase: Conversion of an Endo- to an Exo-type Enzyme;BMB Reports;2004-11-30
2. Enzymic properties of a SDS-resistant Bacillus sp. TS-23 α-amylase produced by recombinant Escherichia coli;Process Biochemistry;2001-03
3. Amylose chain behavior in an interacting context II. Molecular modeling of a maltopentaose fragment in the barley ?-amylase catalytic site;Biopolymers;1999-01
4. Purification and characterization of the α-amylase of Bacillus flavothermus;Enzyme and Microbial Technology;1997-04
5. Structure and activity of some starch-metabolising enzymes;Enzymes for Carbohydrate Engineering;1996
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