Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
about
A database of macromolecular motionsCooperativity in monomeric enzymes with single ligand-binding sitesModeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificityThe importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysisOptimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolutionIncreasing the Conformational Entropy of the Ω-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity,Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stabilityRevisiting 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 FunctionInvestigation of Catalytic Loop Structure, Dynamics, and Function Relationship of Yersinia Protein Tyrosine Phosphatase by Temperature-Jump Relaxation Spectroscopy and X-ray Structural DeterminationStructural and functional perturbation of Giardia lamblia triosephosphate isomerase by modification of a non-catalytic, non-conserved regionProbing the flexibility of large conformational changes in protein structures through local perturbationsEnzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Slow proton transfer from the hydrogen-labelled carboxylic acid side chain (Glu-165) of triosephosphate isomerase to imidazole buffer in D2O.Prediction of protein motions from amino acid sequence and its application to protein-protein interactionThe loop opening/closing motion of the enzyme triosephosphate isomeraseSite-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampCADEE: Computer-Aided Directed Evolution of Enzymes.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Purification and kinetic characterization of the mitogen-activated protein kinase phosphatase rVH6.Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomeraseStructure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseStructural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Focused functional dynamics of supramolecules by use of a mixed-resolution elastic network model.Hydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organismsExtension of the tryptophan chi2,1 dihedral angle-W3 band frequency relationship to a full rotation: correlations and caveats.Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana.Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in piecesEnzyme activation through the utilization of intrinsic dianion binding energy.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.The flexibility of a distant loop modulates active site motion and product release in ribonuclease A.Negative Epistasis and Evolvability in TEM-1 β-Lactamase--The Thin Line between an Enzyme's Conformational Freedom and Disorder.Loop motions of triosephosphate isomerase observed with elastic networks.Inhibition of plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine. Electrospray ionization mass spectrometric analysis of differential cysteine reactivities.Altered dynamics upon oligomerization corresponds to key functional sites.
P2860
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P2860
Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Segmental movement: definition ...... by triosephosphate isomerase.
@en
Segmental movement: definition ...... by triosephosphate isomerase.
@nl
type
label
Segmental movement: definition ...... by triosephosphate isomerase.
@en
Segmental movement: definition ...... by triosephosphate isomerase.
@nl
prefLabel
Segmental movement: definition ...... by triosephosphate isomerase.
@en
Segmental movement: definition ...... by triosephosphate isomerase.
@nl
P356
P1433
P1476
Segmental movement: definition ...... by triosephosphate isomerase.
@en
P2093
Knowles JR
Sampson NS
P304
P356
10.1021/BI00151A014
P407
P577
1992-09-01T00:00:00Z