On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
about
Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzymeSearching sequence space by definably random mutagenesis: improving the catalytic potency of an enzymeCrystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzymeCrystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexaneOptimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selectionIncreasing the Conformational Entropy of the Ω-Loop Lid Domain in Phosphoenolpyruvate Carboxykinase Impairs Catalysis and Decreases Catalytic Fidelity,Hereditary fructose intoleranceThe crystal structure of human muscle aldolase at 3.0 A resolution.Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli.Protein crystallography and infectious diseases.Enzymatic catalysis of proton transfer at carbon: activation of triosephosphate isomerase by phosphite dianion.Characterization of the gene for the microbody (glycosomal) triosephosphate isomerase of Trypanosoma bruceiTriosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy.Structural origins of efficient proton abstraction from carbon by a catalytic antibodyGating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme.Stabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.Control of oligomeric enzyme thermostability by protein engineering.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change.Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase.Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clampThe catalytic domain of endoglucanase A from Clostridium cellulolyticum: effects of arginine 79 and histidine 122 mutations on catalysis.Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues.Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Chicken triosephosphate isomerase complements an Escherichia coli deficiency.Premature translation termination mediates triosephosphate isomerase mRNA degradation.Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate IsomeraseHydron transfer catalyzed by triosephosphate isomerase. Products of the direct and phosphite-activated isomerization of [1-(13)C]-glycolaldehyde in D(2)O.Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana.Towards the engineering of in vitro systemsActive site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme.Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.The upside of downsizing: asymmetric trifunctional organocatalysts as small enzyme mimics for cooperative enhancement of both rate and enantioselectivity with regulation.Structural Basis for the Interconversion of Maltodextrins by MalQ, the Amylomaltase of Escherichia coli.Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase.Common elements on the surface of glycolytic enzymes from Trypanosoma brucei may serve as topogenic signals for import into glycosomes.Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities.iTRAQ-based proteomic profiling of a Microbacterium sp. strain during benzo(a)pyrene removal under anaerobic conditions.
P2860
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P2860
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
description
1981 nî lūn-bûn
@nan
1981 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
name
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@ast
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@en
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@nl
type
label
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@ast
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@en
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@nl
prefLabel
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@ast
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@en
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@nl
P2093
P356
P1476
On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase
@en
P2093
P304
P356
10.1098/RSTB.1981.0069
P407
P577
1981-06-26T00:00:00Z