Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism

Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism

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http://www.wikidata.org/entity/Q27660254
High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active siteBinding Energy and Catalysis by d -Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of ( R )-GlyceraldehydeThe Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking InvestigationsReflections on the catalytic power of a TIM-barrel.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.ENOblock Does Not Inhibit the Activity of the Glycolytic Enzyme EnolaseThe activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomeraseStructure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseStructural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesA role for flexible loops in enzyme catalysis.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Enzyme architecture: on the importance of being in a protein cage.A survey of global radiation damage to 15 different protein crystal types at room temperature: a new decay model.
P2860

Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism

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http://www.wikidata.org/entity/Q27660254
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2010 nî lūn-bûn
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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
Atomic resolution crystallogra ...... on transfer reaction mechanism
@ast
Atomic resolution crystallogra ...... on transfer reaction mechanism
@en
Atomic resolution crystallogra ...... on transfer reaction mechanism
@nl
type
label
Atomic resolution crystallogra ...... on transfer reaction mechanism
@ast
Atomic resolution crystallogra ...... on transfer reaction mechanism
@en
Atomic resolution crystallogra ...... on transfer reaction mechanism
@nl
prefLabel
Atomic resolution crystallogra ...... on transfer reaction mechanism
@ast
Atomic resolution crystallogra ...... on transfer reaction mechanism
@en
Atomic resolution crystallogra ...... on transfer reaction mechanism
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P356
P1433
P1476
Atomic resolution crystallogra ...... on transfer reaction mechanism
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921