α-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1994.tb00167.x/fullpdf
Reference25 articles.
1. Purification and some properties of a novel .ALPHA.-amylase produced by a strain of Thermoactinomyces vulgaris.
2. Enzymatic properties and action patterns of Thermoactinomyces vulgaris .ALPHA.-amylase.
3. Hydrolysis of .ALPHA.-1,6-glucosidic linkages by an .ALPHA.-amylase from Thermoactinomyces vulgaris R-47.
4. Some properties of a highly thermostable α-amylase from a Thermoactinomyces sp.
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1. Structural studies of a Phe256Trp mutant of human salivary α-amylase: implications for the role of a conserved water molecule in enzyme activity;Archives of Biochemistry and Biophysics;2004-01
2. A rapid method to detect dried saliva stains swabbed from human skin using fluorescence spectroscopy;Forensic Science International;2000-12
3. Purification and characterization of the α-amylase of Bacillus flavothermus;Enzyme and Microbial Technology;1997-04
4. α-amylase family: Molecular biology and evolution;Progress in Biophysics and Molecular Biology;1997
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