The starch-binding domain from glucoamylase disrupts the structure of starch.
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The structural basis for the ligand specificity of family 2 carbohydrate-binding modulesMolecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManAHow nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificityCrystal Structure of Circular Permuted RoCBM21 (CP90): Dimerisation and Proximity of Binding SitesAssociation of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinusCrystal structures of starch binding domain from Rhizopus oryzae glucoamylase in complex with isomaltooligosaccharide: insights into polysaccharide binding mechanism of CBM21 familyTwo unique ligand-binding clamps of Rhizopus oryzae starch binding domain for helical structure disruption of amyloseCarbohydrate-binding modules: fine-tuning polysaccharide recognitionA starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch.A CBM20 low-affinity starch-binding domain from glucan, water dikinase.Enzymatic degradation of granular potato starch by Microbacterium aurum strain B8.A.A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.Carbohydrate-binding module 74 is a novel starch-binding domain associated with large and multidomain α-amylase enzymes.An Integrated Bioinformatics Analysis Reveals Divergent Evolutionary Pattern of Oil Biosynthesis in High- and Low-Oil PlantsCrystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13.Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules.Carbohydrate binding modules: biochemical properties and novel applications.Efficient hydrolysis of raw starch and ethanol fermentation: a novel raw starch-digesting glucoamylase from Penicillium oxalicum.The carbohydrate-binding module family 20--diversity, structure, and function.Microbial glucoamylases: characteristics and applications.Recombinant bacterial amylopullulanases: developments and perspectives.Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis.The biochemistry and structural biology of plant cell wall deconstruction.Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase.The starch-binding capacity of the noncatalytic SBD2 region and the interaction between the N- and C-terminal domains are involved in the modulation of the activity of starch synthase III from Arabidopsis thaliana.Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles.Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.Starch-binding domain affects catalysis in two Lactobacillus alpha-amylasesNovel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium.High throughput screening of starch structures using carbohydrate microarrays.Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification.Glucoamylase starch-binding domain of Aspergillus niger B1: molecular cloning and functional characterization.Potato starch synthases: Functions and relationships.Conservation and divergence of Starch Synthase III genes of monocots and dicots.Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars.Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution.The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation.Halotolerant, acid-alkali stable, chelator resistant and raw starch digesting α-amylase from a marine bacterium Bacillus subtilis S8-18.The starch-binding domain family CBM41-An in silico analysis of evolutionary relationships.Interactions of flavonoids with α-amylase and starch slowing down its digestion.
P2860
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P2860
The starch-binding domain from glucoamylase disrupts the structure of starch.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
The starch-binding domain from glucoamylase disrupts the structure of starch.
@en
The starch-binding domain from glucoamylase disrupts the structure of starch.
@nl
type
label
The starch-binding domain from glucoamylase disrupts the structure of starch.
@en
The starch-binding domain from glucoamylase disrupts the structure of starch.
@nl
prefLabel
The starch-binding domain from glucoamylase disrupts the structure of starch.
@en
The starch-binding domain from glucoamylase disrupts the structure of starch.
@nl
P2093
P2860
P1433
P1476
The starch-binding domain from glucoamylase disrupts the structure of starch.
@en
P2093
Gilbert HJ
Simpson PJ
Southall SM
Williamson G
Williamson MP
P2860
P356
10.1016/S0014-5793(99)00263-X
P407
P577
1999-03-01T00:00:00Z