Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism - Wikidata - wikimedia - TriplyDB

Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism

Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism

http://www.wikidata.org/entity/Q24556126

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Catalytic mechanism of cellulose degradation by a cellobiohydrolase, CelS Carbinolamine formation and dehydration in a DNA repair enzyme active site Correct and incorrect nucleotide incorporation pathways in DNA polymerase beta The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.Transition-state charge stabilization through multiple non-covalent interactions in the guanidinium-catalyzed enantioselective Claisen rearrangement The proficiency of a thermophilic chorismate mutase enzyme is solely through an entropic advantage in the enzyme reaction.Theoretical insights in enzyme catalysis.'In-line attack' conformational effect plays a modest role in an enzyme-catalyzed RNA cleavage: a free energy simulation study.How similar are enzyme active site geometries derived from quantum mechanical theozymes to crystal structures of enzyme-inhibitor complexes? Implications for enzyme design.Restricting the ψ Torsion Angle Has Stereoelectronic Consequences on a Scissile Bond: An Electronic Structure Analysis.Multi-resolution simulation of biomolecular systems: a review of methodological issues.Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin.Chemical accuracy in QM/MM calculations on enzyme-catalysed reactions.Interaction-dependent gene expression in Mla-specified response to barley powdery mildew.Exploration of swapping enzymatic function between two proteins: a simulation study of chorismate mutase and isochorismate pyruvate lyase.Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase.The catalytic power of enzymes: conformational selection or transition state stabilization?Improved constrained optimization method for reaction-path determination in the generalized hybrid orbital quantum mechanical/molecular mechanical calculations.QM/MM-Methoden für biomolekulare Systeme Biocontrol and Osmoprotection for Plants under Salinated Conditions

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Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism

http://www.wikidata.org/entity/Q24556126

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2001 nî lūn-bûn

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2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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Substrate conformational trans ...... ole in the catalytic mechanism

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Substrate conformational trans ...... ole in the catalytic mechanism

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Substrate conformational trans ...... ole in the catalytic mechanism

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Proceedings of the National Academy of Sciences of the United States of America

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Substrate conformational trans ...... ole in the catalytic mechanism

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P2860

Yeast chorismate mutase in the R state: simulations of the active site

A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions

The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction

Routes to catalysis: structure of a catalytic antibody and comparison with its natural counterpart

Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog

Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures

All-atom empirical potential for molecular modeling and dynamics studies of proteins

Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway.

Catalysis of concerted reactions by antibodies: the Claisen rearrangement.

On the mechanism of the chorismate mutase reaction.

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10.1073/PNAS.141230998

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