(Q24645366)

5

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Gerhard H Braus

object named as

G Braus

4

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author name string

J Ma

1

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X Zheng

2

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G Schnappauf

3

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W N Lipscomb

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

6

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language of work or name

English

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publication date

8 December 1998

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published in

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volume

95

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issue

25

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page(s)

14640-5

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cites work

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

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

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Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state

7 April 2017

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

7 April 2017

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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

7 April 2017

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

7 April 2017

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

7 April 2017

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pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model

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Classical electrostatics in biology and chemistry

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Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms

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On the mechanism of the chorismate mutase reaction

27 September 2017

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Calorimetric investigation of inhibitor binding to rabbit muscle aldolase

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Transition-state stabilization and enzymic catalysis. Kinetic and molecular orbital studies of the rearrangement of chorismate to prephenate.

30 May 2018

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Binding Energy and Catalysis: The Implications for Transition-State Analogs and Catalytic Antibodies.

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Investigation of the enzymatic mechanism of the yeast chorismate mutase by docking a transition state analog

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94

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Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution

21 January 2018

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Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme

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Simulation of activation free energies in molecular systems

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Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics program

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Secondary tritium isotope effects as probes of the enzymic and nonenzymic conversion of chorismate to prephenate

21 January 2018

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Monofunctional chorismate mutase from Bacillus subtilis: kinetic and 13C NMR studies on the interactions of the enzyme with its ligands

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