]> BibSonomy publications for /author/Guo/analog http://www.bibsonomy.org/burst/author/Guo/analog BibSonomy BuRST Feed for /author/Guo/analog 2008-12-02T08:29:00+01:00 Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism http://www.bibsonomy.org/bibtex/2c7a914666032fb6aaf45995be7152c3c/hlwoodcock hlwoodcock 2006-06-16T05:03:46+02:00 ab-initio analog antibody bacillus-subtilis bibtex-import catalysis claisen crystal-structures dynamics electrostatic enzyme prephenate rearrangement state
Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism
H. Guo and Q. Cui and W. N. Lipscomb and M. Karplus Proc. Natl. Acad. Sci. USA 98 9032--9037 (2001)
to ab-initio analog antibody bacillus-subtilis bibtex-import catalysis claisen crystal-structures dynamics electrostatic enzyme prephenate rearrangement state by hlwoodcock on 2006-06-16 05:03:46 ]]> Proc. Natl. Acad. Sci. USA169032--9037Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism982001ab-initio analog antibody bacillus-subtilis bibtex-import catalysis claisen crystal-structures dynamics electrostatic enzyme prephenate rearrangement state 2006-06-16 05:03:46.0Chorismate mutase acts at the first branch-point of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. The results of molecular dynamics simulations of the substrate in solution and in the active site of chorismate mutase are reported. Two nonreactive conformers of chorismate are found to be more stable than the reactive pseudodiaxial chair conformer in solution. It is shown by QM/MM molecular dynamics simulations, which take into account the motions of the enzyme, that when these inactive conformers are bound to the active site, they are rapidly converted to the reactive chair conformer. This result suggests that one contribution of the enzyme is to bind the more prevalent nonreactive conformers and transform them into the active form in a step before the chemical reaction. The motion of the reactive chair conformer in the active site calculated by using the QM/MM potential generates transient structures that are closer to the transition state than is the stable CHAIR conformer.