Publication date
August 2003
DOI Publisher
Cell Press. Published by Elsevier Ltd.Abstract
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the X-ray structure of the enzyme/tetrasaccharide complex
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the X-ray structure of the enzyme/tetrasaccharide complex
[[abstract]]GA (glucoamylase) hydrolyses starch and polysaccharides to beta-D-glucose. RoGA (Rhizopu...
The role in activity of outer regions in the substrate binding cleft in α-amylases is illustrated by...
AbstractA novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family...
AbstractThough the three-dimensional structures of barley α-amylase isozymes AMY1 and AMY2 are very ...
Some polysaccharide processing enzymes possess secondary carbohydrate binding sites situated on the ...
α-Amylases occur widely in plants, animals, and microorganisms. They often act in synergy with other...
Germinating barley seeds contain multiple forms of α-amylase, which are subject to both differential...
AbstractCertain starch hydrolases possess secondary carbohydrate binding sites outside of the active...
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the...
AbstractBackground: Carbohydrate-binding domains are usually small and physically separate from the ...
Most glucoamylases (α-1,4-d-glucan glucohydrolase, EC 3.2.1.3) have structures consisting of both a ...
Starch is a major energy source for all domains of life. Recent advances in structures of starch-deg...
In the first paper of this series, the tools necessary to evaluate the consequences of glucopyranose...
AbstractSubsite affinity maps of long substrate binding clefts in barley α-amylases, obtained using ...
The gene for a membrane-bound, halophilic, and thermostable α-amylase, AmyB, from Halothermothrix or...
[[abstract]]GA (glucoamylase) hydrolyses starch and polysaccharides to beta-D-glucose. RoGA (Rhizopu...
The role in activity of outer regions in the substrate binding cleft in α-amylases is illustrated by...
AbstractA novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family...
AbstractThough the three-dimensional structures of barley α-amylase isozymes AMY1 and AMY2 are very ...
Some polysaccharide processing enzymes possess secondary carbohydrate binding sites situated on the ...
α-Amylases occur widely in plants, animals, and microorganisms. They often act in synergy with other...
Germinating barley seeds contain multiple forms of α-amylase, which are subject to both differential...
AbstractCertain starch hydrolases possess secondary carbohydrate binding sites outside of the active...
AbstractA novel polysaccharide binding site is identified in domain C of barley α-amylase 1 from the...
AbstractBackground: Carbohydrate-binding domains are usually small and physically separate from the ...
Most glucoamylases (α-1,4-d-glucan glucohydrolase, EC 3.2.1.3) have structures consisting of both a ...
Starch is a major energy source for all domains of life. Recent advances in structures of starch-deg...
In the first paper of this series, the tools necessary to evaluate the consequences of glucopyranose...
AbstractSubsite affinity maps of long substrate binding clefts in barley α-amylases, obtained using ...
The gene for a membrane-bound, halophilic, and thermostable α-amylase, AmyB, from Halothermothrix or...
[[abstract]]GA (glucoamylase) hydrolyses starch and polysaccharides to beta-D-glucose. RoGA (Rhizopu...
The role in activity of outer regions in the substrate binding cleft in α-amylases is illustrated by...
AbstractA novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family...
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