The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175 - Wikidata - wikimedia - TriplyDB

The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175

The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175

http://www.wikidata.org/entity/Q27639510

about

Catalytic mechanism of cellulose degradation by a cellobiohydrolase, CelS Structural and mechanistic fundamentals for designing of cellulases Filming biomolecular processes by high-speed atomic force microscopy "Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography.The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum Crystal Structure of Glycoside Hydrolase Family 55 -1,3-Glucanase from the Basidiomycete Phanerochaete chrysosporium Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea Structural insights into a unique cellulase fold and mechanism of cellulose hydrolysis Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea--a tweezer-like motion in the structure of CcCel6C Loop Motions Important to Product Expulsion in the Thermobifida fusca Glycoside Hydrolase Family 6 Cellobiohydrolase from Structural and Computational Studies Evidence That GH115 -Glucuronidase Activity, Which Is Required to Degrade Plant Biomass, Is Dependent on Conformational Flexibility Structure of the catalytic core module of the Chaetomium thermophilum family GH6 cellobiohydrolase Cel6A Rational design, synthesis, evaluation and enzyme-substrate structures of improved fluorogenic substrates for family 6 glycoside hydrolases Ultrastructure and composition of the Nannochloropsis gaditana cell wall Active site and laminarin binding in glycoside hydrolase family 55 Multiple functions of aromatic-carbohydrate interactions in a processive cellulase examined with molecular simulation Hypocrea jecorina CEL6A protein engineering.A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases.Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism Computational investigation of the pH dependence of loop flexibility and catalytic function in glycoside hydrolases.Insights into exo- and endoglucanase activities of family 6 glycoside hydrolases from Podospora anserina.Chemical tools to explore nutrient-driven O-GlcNAc cycling.Advances in understanding glycosyltransferases from a structural perspective.Genetic and functional characterization of an extracellular modular GH6 endo-β-1,4-glucanase from an earthworm symbiont, Cellulosimicrobium funkei HY-13.Identification of catalytic residues of Ca2+-independent 1,2-alpha-D-mannosidase from Aspergillus saitoi by site-directed mutagenesis.Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family.Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B.Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose.Structure-function analysis of the bacterial expansin EXLX1.Heterologous expression of cellobiohydrolase II (Cel6A) in maize endosperm.A mechanistic model for rational design of optimal cellulase mixtures.A mutation in an exoglucanase of Xanthomonas oryzae pv. oryzae, which confers an endo mode of activity, affects bacterial virulence, but not the induction of immune responses, in rice.Advantages of a Distant Cellulase Catalytic Base.Contribution of presenilin transmembrane domains 6 and 7 to a water-containing cavity in the gamma-secretase complex.A bacterial GH6 cellobiohydrolase with a novel modular structure.

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P2860

The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175

http://www.wikidata.org/entity/Q27639510

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2002 nî lūn-bûn

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2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2002 թվականի օգոստոսին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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Journal of the American Chemical Society

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The active site of cellobiohyd ...... f aspartic acids D221 and D175

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P2093

Andrea Vasella

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Dieter Becker

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Gerd Wohlfahrt

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Jin-Yu Zou

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Kathleen Piens

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Laura Ruohonen

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Marc Claeyssens

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Martin Weber

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Michael L Sinnott

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Michael Szardenings

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10015-24

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10.1021/JA012659Q

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34

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124

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Jerry Ståhlberg

Gerard Kleywegt

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2002-08-28T00:00:00Z

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12188666

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