A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase (NAD+) by phosphite dianion.
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Binding 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.Activation of R235A mutant orotidine 5'-monophosphate decarboxylase by the guanidinium cation: effective molarity of the cationic side chain of Arg-235Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach.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.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 DecarboxylaseRole 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 TransferDissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.Structural 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.Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organismsEnzyme architecture: the activating oxydianion binding domain for orotidine 5'-monophophate decarboxylase.Pyridoxal 5'-phosphate: electrophilic catalyst extraordinaire.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.The PLP cofactor: lessons from studies on model reactions.A paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Specificity in transition state binding: the Pauling model revisited.Enzyme activation through the utilization of intrinsic dianion binding energy.The role of phosphate in a multistep enzymatic reaction: reactions of the substrate and intermediate in piecesStructure-Reactivity Effects on Intrinsic Primary Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase.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: 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.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
A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase (NAD+) by phosphite dianion.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on April 2008
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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
A substrate in pieces: alloste ...... e (NAD+) by phosphite dianion.
@en
A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase
@nl
type
label
A substrate in pieces: alloste ...... e (NAD+) by phosphite dianion.
@en
A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase
@nl
prefLabel
A substrate in pieces: alloste ...... e (NAD+) by phosphite dianion.
@en
A substrate in pieces: allosteric activation of glycerol 3-phosphate dehydrogenase
@nl
P2860
P356
P1433
P1476
A substrate in pieces: alloste ...... e (NAD+) by phosphite dianion.
@en
P2093
Tina L Amyes
Wing-Yin Tsang
P2860
P304
P356
10.1021/BI8001743
P407
P577
2008-04-01T00:00:00Z