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The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activityMulti-site substrate binding and interplay in barley alpha-amylase 1Starch Catabolism by a Prominent Human Gut Symbiont Is Directed by the Recognition of Amylose HelicesStructure of the Arabidopsis Glucan Phosphatase LIKE SEX FOUR2 Reveals a Unique Mechanism for Starch DephosphorylationMutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activityStructure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activityRaw starch-degrading α-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme.α-Amylase is a potential growth inhibitor of Porphyromonas gingivalis, a periodontal pathogenic bacterium.Using Carbohydrate Interaction Assays to Reveal Novel Binding Sites in Carbohydrate Active Enzymes.Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13.Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.Unique carbohydrate binding platforms employed by the glucan phosphatases.Structural mechanisms of plant glucan phosphatases in starch metabolismProbing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial bindingThe carbohydrate-binding module family 20--diversity, structure, and function.Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases.Engineering yeasts for raw starch conversion.α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model.The Sus operon: a model system for starch uptake by the human gut Bacteroidetes.Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrateMapping of barley alpha-amylases and outer subsite mutants reveals dynamic high-affinity subsites and barriers in the long substrate binding cleft.Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids.The Importance of Surface-Binding Site towards Starch-Adsorptivity Level in α-Amylase: A Review on Structural Point of View.Roles of multiple surface sites, long substrate binding clefts, and carbohydrate binding modules in the action of amylolytic enzymes on polysaccharide substrates
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Oligosaccharide binding to barley alpha-amylase 1.
@en
type
label
Oligosaccharide binding to barley alpha-amylase 1.
@en
prefLabel
Oligosaccharide binding to barley alpha-amylase 1.
@en
P2093
P2860
P356
P1476
Oligosaccharide binding to barley alpha-amylase 1
@en
P2093
Birte Svensson
Haruhide Mori
Richard Haser
P2860
P304
32968-32978
P356
10.1074/JBC.M505515200
P407
P577
2005-07-19T00:00:00Z