Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces
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Substrate Deconstruction and the Nonadditivity of Enzyme RecognitionEnzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseReflections on the catalytic power of a TIM-barrel.α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction.Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.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.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferEnzyme activation through the utilization of intrinsic dianion binding energy.Structure-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.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.Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)† †Electronic supplementary information (ESI) available: Further experimental and computational data. See DOI: 10.1039/c5sc03666f.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
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Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 06 March 2014
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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
Enzyme architecture: remarkabl ...... te and the substrate in pieces
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Enzyme architecture: remarkabl ...... e and the substrate in pieces.
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type
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Enzyme architecture: remarkabl ...... te and the substrate in pieces
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Enzyme architecture: remarkabl ...... e and the substrate in pieces.
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prefLabel
Enzyme architecture: remarkabl ...... te and the substrate in pieces
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Enzyme architecture: remarkabl ...... e and the substrate in pieces.
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P2860
P356
P1476
Enzyme architecture: remarkabl ...... te and the substrate in pieces
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P2093
Tina L Amyes
P2860
P304
P356
10.1021/JA501103B
P407
P577
2014-03-06T00:00:00Z