Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution
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Crystal structure of a maltogenic amylase provides insights into a catalytic versatilityAmylosucrase, a glucan-synthesizing enzyme from the alpha-amylase familySolution structure of the fibronectin type III domain from Bacillus circulans WL-12 chitinase A1The fully conserved Asp residue in conserved sequence region I of the alpha-amylase family is crucial for the catalytic site architecture and activityCrystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sitesCrystal structure and snapshots along the reaction pathway of a family 51 -L-arabinofuranosidaseStructural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding proteinStructural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidumStructural and Functional Analysis of a Glycoside Hydrolase Family 97 Enzyme from Bacteroides thetaiotaomicronDimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovoransMechanism of porcine pancreatic alpha-amylase. Inhibition of amylose and maltopentaose hydrolysis by alpha-, beta- and gamma-cyclodextrins.A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition.Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.Pullulan degrading enzymes of bacterial origin.A high molecular-mass Anoxybacillus sp. SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization.The Sus operon: a model system for starch uptake by the human gut Bacteroidetes.Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley alpha-amylase 1.A thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes.The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding.Molecular and biochemical analyses of the GH44 module of CbMan5B/Cel44A, a bifunctional enzyme from the hyperthermophilic bacterium Caldicellulosiruptor bescii.Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley alpha-amylase 1.Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.Structure and function of α-glucan debranching enzymes.Characteristics, protein engineering and applications of microbial thermostable pullulanases and pullulan hydrolases.The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans.Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffoldStructural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis
P2860
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P2860
Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@ast
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@en
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@nl
type
label
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@ast
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@en
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@nl
prefLabel
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@ast
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@en
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@nl
P2093
P356
P1476
Crystal structure of Thermoact ...... d pullulan at 2.6 A resolution
@en
P2093
P304
P356
10.1006/JMBI.1999.2647
P407
P577
1999-04-01T00:00:00Z