Structural basis of α-amylase activation by chloride - Wikidata - thesis-toulmin - TriplyDB

Structural basis of α-amylase activation by chloride

Structural basis of α-amylase activation by chloride

http://www.wikidata.org/entity/Q27639020

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Group B Streptococcus Pullulanase Crystal Structures in the Context of a Novel Strategy for Vaccine Development Structure and activity of the cold-active and anion-activated carboxyl esterase OLEI01171 from the oil-degrading marine bacterium Oleispira antarctica Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutations Raw starch-degrading α-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme.Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Characterization of Halomonas sp. strain H11 α-glucosidase activated by monovalent cations and its application for efficient synthesis of α-D-glucosylglycerol Psychrophilic enzymes: from folding to function and biotechnology.α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase.Oleanolic acid and ursolic acid as potential inhibitors of human salivary α-amylase: insights from in vitro assays and in silico simulations.Optimization of Amylase Production from B. amyloliquefaciens (MTCC 1270) Using Solid State Fermentation.Effect of neohesperidin dihydrochalcone on the activity and stability of alpha-amylase: a comparative study on bacterial, fungal, and mammalian enzymes.Entropy and free energy of a mobile protein loop in explicit water.Chloride Activated Halophilic α-Amylase from Marinobacter sp. EMB8: Production Optimization and Nanoimmobilization for Efficient Starch Hydrolysis Enhancement of the alcoholytic activity of alpha-amylase AmyA from Thermotoga maritima MSB8 (DSM 3109) by site-directed mutagenesis.Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources.Neohesperidin dihydrochalcone: presentation of a small molecule activator of mammalian alpha-amylase as an allosteric effector.Mechanism of salt-induced activity enhancement of a marine-derived laccase, Lac15.Functional annotation of the mesophilic-like character of mutants in a cold-adapted enzyme by self-organising map analysis of their molecular dynamics.

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P2860

Structural basis of α-amylase activation by chloride

http://www.wikidata.org/entity/Q27639020

description

2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Structural basis of α-amylase activation by chloride

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Protein Science

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Structural basis of α-amylase activation by chloride

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Charles Gerday

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Georges Feller

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Nushin Aghajari

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Richard Haser

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P2860

Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques

Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor

The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex

Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase

X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases

The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution

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1435-41

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scholarly article

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10.1110/PS.0202602

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6

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11

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