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Cooperativity in monomeric enzymes with single ligand-binding sitesAn ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.Identification of Amino Acids that Account for Long-Range Interactions in Two Triosephosphate Isomerases from Pathogenic TrypanosomesHigh resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: The conformational flexibility of the catalytic glutamate in its closed, liganded active siteRevisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residueThe Ω-Loop Lid Domain of Phosphoenolpyruvate Carboxykinase Is Essential for Catalytic FunctionBinding Energy and Catalysis by d -Xylose Isomerase: Kinetic, Product, and X-ray Crystallographic Analysis of Enzyme-Catalyzed Isomerization of ( R )-GlyceraldehydeThe 1.8 A Cholix Toxin Crystal Structure in Complex with NAD+ and Evidence for a New Kinetic ModelStructural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic HelixStructural snapshots along the reaction pathway ofYersinia pestisRipA, a putative butyryl-CoA transferaseStructural basis for the evolution of vancomycin resistance D,D-peptidasesEnzyme 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 enzymeStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceReflections on the catalytic power of a TIM-barrel.Flexible Proteins at the Origin of Life.Identification of catalytic residues using a novel feature that integrates the microenvironment and geometrical location properties of residues.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase.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.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.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 DecarboxylaseMechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampOrotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Functional dichotomy in the 16S rRNA (m1A1408) methyltransferase family and control of catalytic activity via a novel tryptophan mediated loop reorganizationCatalysis by orotidine 5'-monophosphate decarboxylase: effect of 5-fluoro and 4'-substituents on the decarboxylation of two-part substrates.Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomeraseFunctional Dissection of the Bipartite Active Site of the Class I Coenzyme A (CoA)-Transferase Succinyl-CoA:Acetate CoA-Transferase.A mutational analysis of the active site loop residues in cis-3-Chloroacrylic acid dehalogenase.Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseGates of enzymes.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 pieces
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 October 2010
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A role for flexible loops in enzyme catalysis.
@en
A role for flexible loops in enzyme catalysis.
@nl
type
label
A role for flexible loops in enzyme catalysis.
@en
A role for flexible loops in enzyme catalysis.
@nl
prefLabel
A role for flexible loops in enzyme catalysis.
@en
A role for flexible loops in enzyme catalysis.
@nl
P2860
P1476
A role for flexible loops in enzyme catalysis.
@en
P2093
M Merced Malabanan
Tina L Amyes
P2860
P304
P356
10.1016/J.SBI.2010.09.005
P577
2010-10-13T00:00:00Z