Enzyme architecture: on the importance of being in a protein cage.
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Enzyme Architecture: The Effect of Replacement and Deletion Mutations of Loop 6 on Catalysis by Triosephosphate IsomeraseProbing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeRv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosisReflections on the catalytic power of a TIM-barrel.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.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.Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride TransferStructure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseActive Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.AQUA-DUCT a ligands tracking tool.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.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.Difference FTIR Studies of Substrate Distribution in Triosephosphate Isomerase.Evidence of a sequestered imine intermediate during reduction of nitrile to amine by the nitrile reductase QueF from Escherichia coli.Substituent Effects on Carbon Acidity in Aqueous Solution and at Enzyme Active Sites.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.Mixed-valence copper(I,II) complexes with 4-(1H-pyrazol-1-yl)-6-R-pyrimidines: from ionic structures to coordination polymers.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.Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomerase.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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P2860
Enzyme architecture: on the importance of being in a protein cage.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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Enzyme architecture: on the importance of being in a protein cage.
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Enzyme architecture: on the importance of being in a protein cage.
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prefLabel
Enzyme architecture: on the importance of being in a protein cage.
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P2860
P1476
Enzyme architecture: on the importance of being in a protein cage.
@en
P2093
Bogdana Goryanova
Tina L Amyes
P2860
P356
10.1016/J.CBPA.2014.03.001
P577
2014-03-31T00:00:00Z