Journal ArticleDOI
Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution.
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TLDR
The three-dimensional structure of Bacillus licheniformis alpha-amylase (BLA) has been determined by multiple isomorphous replacement in a crystal of space group P4(3)2(1)2 (a = b = 119.6 A, c = 85.4 A) as discussed by the authors.About:
This article is published in Journal of Molecular Biology.The article was published on 1995-03-03. It has received 325 citations till now. The article focuses on the topics: Multiple isomorphous replacement & Bacillus licheniformis.read more
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Journal ArticleDOI
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
TL;DR: The sequence- Specificity and structure-specificity relationships described may provide useful pointers for rational protein engineering.
Journal ArticleDOI
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins
TL;DR: A large-scale analysis of 1691 family GH13 sequences is performed by combining clustering, similarity search and phylogenetic methods to establish robust groups that show an improved correlation between sequence and enzymatic specificity.
Journal ArticleDOI
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
TL;DR: In this review, existing knowledge of insect α-amylases, plant α-AMylase inhibitors and their interaction is summarized and positive results recently obtained for transgenic plants and future prospects in the area are reviewed.
Journal ArticleDOI
Fold change in evolution of protein structures.
TL;DR: The existence of evolutionarily related proteins that possess different folds brings new challenges to the homology modeling techniques and the structure classification strategies and offers new opportunities for protein design in experimental studies.
Patent
.alpha.-amylase mutants
TL;DR: In this article, a variant of a parent Termamyl-like alpha-amylase has been shown to exhibit an alteration in at least one of the following properties relative to the parent alpha-AMylase: substrate specificity, substrate binding, substrate cleavage pattern, thermal stability, pH/activity profile, pH-stability profile, stability towards oxidation, Ca 2+ dependency and specific activity.