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Acid proteinase and the multiplicity of aspergillus awamori glucoamylase forms

K. N. Neustroev, +1 more
- 25 Dec 1990 - 
- Vol. 55, Iss: 5, pp 776-785
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This article is published in Biokhimiya.The article was published on 1990-12-25 and is currently open access. It has received 11 citations till now. The article focuses on the topics: Aspergillus awamori.

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Journal ArticleDOI

Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.

TL;DR: The three-dimensional structure of the pseudotetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var.
Journal ArticleDOI

Glucoamylase structural, functional, and evolutionary relationships

TL;DR: To correlate structural features with glucoamylase properties, a structure‐based multisequence alignment was constructed using information from catalytic and starch‐binding domain models, and protein parsimony analysis suggests an ancient bacterial origin for the glu coamylases gene.
Journal ArticleDOI

Refined structure for the complex of 1-deoxynojirimycin with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.

TL;DR: The three-dimensional structure of the complex of 1-deoxynojirimycin with glucoamylase II-(471) from Aspergillus awamori var.
Book ChapterDOI

Enzymes and Their Action on Starch

TL;DR: The application of modern biochemical and biophysical techniques of protein sequence analysis, chemical modification of specific amino acid groups, x-ray crystallography, recombinant DNA cloning and sequencing, and site-directed mutagenesis have given a much more complete understanding of how the enzyme protein structure provides specificity and performs catalysis.
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