Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase (Q44891391)

7 December 2017

Conformational effects in enzyme catalysis: QM/MM free energy calculation of the 'NAC' contribution in chorismate mutase (English)

1 reference

7 December 2017

Adrian J Mulholland

2

0 references

author name string

Kara E Ranaghan

series ordinal

1

1 reference

PubMed ID

15136856

7 December 2017

language of work or name

English

0 references

publication date

27 April 2004

1 reference

7 December 2017

Chemical Communications

1 reference

7 December 2017

10

1 reference

7 December 2017

1238-1239

1 reference

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

7 December 2017

1 reference

Transition state stabilization and substrate strain in enzyme catalysis: ab initio QM/MM modelling of the chorismate mutase reaction.

21 January 2018

1 reference

Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor

21 January 2018

1 reference

Apparent NAC effect in chorismate mutase reflects electrostatic transition state stabilization

21 January 2018

1 reference

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

21 January 2018

1 reference

Preorganization and reorganization as related factors in enzyme catalysis: the chorismate mutase case

21 January 2018

1 reference

Contributions of conformational compression and preferential transition state stabilization to the rate enhancement by chorismate mutase.

21 January 2018

1 reference

Comparison of Formation of Reactive Conformers (NACs) for the Claisen Rearrangement of Chorismate to Prephenate in Water and in the E. coli Mutase: The Efficiency of the Enzyme Catalysis

21 January 2018

1 reference

Enzymes do what is expected (chalcone isomerase versus chorismate mutase).

21 January 2018

1 reference

Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants).

21 January 2018

1 reference

How much do enzymes really gain by restraining their reacting fragments?

21 January 2018

1 reference

A combined quantum mechanical and molecular mechanical potential for molecular dynamics simulations

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

Understanding the Role of Active‐Site Residues in Chorismate Mutase Catalysis from Molecular‐Dynamics Simulations

21 January 2018

1 reference

21 January 2018

Identifiers

DOI

10.1039/B402388A

1 reference

7 December 2017

1 reference

PubMed ID

15136856