Specificity in transition state binding: the Pauling model revisited.
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Enzymatic rate enhancements: a review and perspectiveSubstrate Distortion Contributes to the Catalysis of Orotidine 5′-Monophosphate DecarboxylaseStructural snapshots along the reaction pathway ofYersinia pestisRipA, a putative butyryl-CoA transferaseEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseSub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediateStructures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion holeReflections on the catalytic power of a TIM-barrel.The evolution of enzyme function in the isomerases.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.Quantum delocalization of protons in the hydrogen-bond network of an enzyme active site.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 DecarboxylaseFunctional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native ActivityRole 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 TransferFunctional Dissection of the Bipartite Active Site of the Class I Coenzyme A (CoA)-Transferase Succinyl-CoA:Acetate CoA-Transferase.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.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 piecesDesign of inhibitors of ODCase.Enzyme architecture: on the importance of being in a protein cage.Enzyme activation through the utilization of intrinsic dianion binding energy.Electric Fields and Enzyme Catalysis.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 piecesStructure-Reactivity Effects on Intrinsic Primary Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase.Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer.Coding of Class I and II Aminoacyl-tRNA Synthetases.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.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
Specificity in transition state binding: the Pauling model revisited.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
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name
Specificity in transition state binding: the Pauling model revisited.
@en
type
label
Specificity in transition state binding: the Pauling model revisited.
@en
prefLabel
Specificity in transition state binding: the Pauling model revisited.
@en
P2860
P356
P1433
P1476
Specificity in transition state binding: the Pauling model revisited.
@en
P2093
Tina L Amyes
P2860
P304
P356
10.1021/BI301491R
P407
P577
2013-02-04T00:00:00Z