Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.
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Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseConnecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial EnzymeReflections on the catalytic power of a TIM-barrel.The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.CADEE: Computer-Aided Directed Evolution of Enzymes.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferRole 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 piecesEnzyme architecture: on the importance of being in a protein cage.Enzyme activation through the utilization of intrinsic dianion binding energy.A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.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.First characterization of a microsporidial triosephosphate isomerase and the biochemical mechanisms of its inactivation to propose a new druggable target.Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase
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P2860
Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.
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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 16 August 2013
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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
Structural mutations that prob ...... of triosephosphate isomerase.
@en
Structural mutations that prob ...... of triosephosphate isomerase.
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type
label
Structural mutations that prob ...... of triosephosphate isomerase.
@en
Structural mutations that prob ...... of triosephosphate isomerase.
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prefLabel
Structural mutations that prob ...... of triosephosphate isomerase.
@en
Structural mutations that prob ...... of triosephosphate isomerase.
@nl
P2093
P2860
P356
P1433
P1476
Structural mutations that prob ...... of triosephosphate isomerase.
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P2093
J Patrick Loria
Rik K Wierenga
Tina L Amyes
P2860
P304
P356
10.1021/BI401019H
P407
P577
2013-08-16T00:00:00Z