Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.
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Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: “Remote” Residues That Stabilize the Active ConformationBinding Energy and Catalysis by d -Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of ( R )-GlyceraldehydeEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseReflections on the catalytic power of a TIM-barrel.Enzymatic Catalysis of Proton Transfer and Decarboxylation Reactions.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.Tracing compartmentalized NADPH metabolism in the cytosol and mitochondria of mammalian cellsRole of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.Bovine serum albumin-catalyzed deprotonation of [1-(13)C]glycolaldehyde: protein reactivity toward deprotonation of the alpha-hydroxy alpha-carbonyl carbon.Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate.The 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 ligand-driven conformational change.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 clampRole of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.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 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.Enzyme activation through the utilization of intrinsic dianion binding energy.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.Ground-state destabilization in orotate phosphoribosyltransferases by binding isotope effects.Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer.A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.Enzyme Architecture: Erection of Active Orotidine 5'-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes.Orotidine 5'-Monophosphate Decarboxylase: Probing the Limits of the Possible for Enzyme Catalysis.Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate Dehydrogenase
P2860
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P2860
Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Hydron transfer catalyzed by t ...... activated isomerization of [1-
@nl
Hydron transfer catalyzed by t ...... 13)C]-glycolaldehyde in D(2)O.
@en
type
label
Hydron transfer catalyzed by t ...... activated isomerization of [1-
@nl
Hydron transfer catalyzed by t ...... 13)C]-glycolaldehyde in D(2)O.
@en
prefLabel
Hydron transfer catalyzed by t ...... activated isomerization of [1-
@nl
Hydron transfer catalyzed by t ...... 13)C]-glycolaldehyde in D(2)O.
@en
P2860
P356
P1433
P1476
Hydron transfer catalyzed by t ...... 13)C]-glycolaldehyde in D(2)O.
@en
P2093
Maybelle K Go
Tina L Amyes
P2860
P304
P356
10.1021/BI900636C
P407
P577
2009-06-01T00:00:00Z