A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
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Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5′-Phosphate Group Activates the EnzymeEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomerasePrecision is essential for efficient catalysis in an evolved Kemp eliminaseProbing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeReversibility and two state behaviour in the thermal unfolding of oligomeric TIM barrel proteinsReflections on the catalytic power of a TIM-barrel.Structural effects of protein aging: terminal marking by deamidation in human triosephosphate isomerase.Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.Enzyme architecture: optimization of transition state stabilization from a cation-phosphodianion pair.Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5'-Monophosphate DecarboxylaseMechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampCADEE: Computer-Aided Directed Evolution of Enzymes.Inhibition of enzyme activity of Rhipicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodies.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Catalysis by orotidine 5'-monophosphate decarboxylase: effect of 5-fluoro and 4'-substituents on the decarboxylation of two-part substrates.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferMagnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomeraseA mutational analysis of the active site loop residues in cis-3-Chloroacrylic acid dehalogenase.Structure-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.Role of a guanidinium cation-phosphodianion pair in stabilizing the vinyl carbanion intermediate of orotidine 5'-phosphate decarboxylase-catalyzed reactions.Enzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesSpecificity in transition state binding: the Pauling model revisited.The upside of downsizing: asymmetric trifunctional organocatalysts as small enzyme mimics for cooperative enhancement of both rate and enantioselectivity with regulation.Enzyme architecture: on the importance of being in a protein cage.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.The role of phosphate in a multistep enzymatic reaction: reactions of the substrate and intermediate in piecesIsolation and Analysis of Cell Wall Proteome in Elsholtzia splendens Roots Using ITRAQ with LC-ESI-MS/MS.Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer.Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomerase.Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate DehydrogenaseEnzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase
P2860
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P2860
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@en
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@nl
type
label
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@en
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@nl
prefLabel
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@en
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@nl
P2860
P356
P1433
P1476
A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.
@en
P2860
P304
P356
10.1021/BI300195B
P407
P577
2012-03-20T00:00:00Z