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Understanding the Role of Active‐Site Residues in Chorismate Mutase Catalysis from Molecular‐Dynamics Simulations
Author(s) -
Guo Hong,
Cui Qiang,
Lipscomb William N.,
Karplus Martin
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200219878
Subject(s) - chorismate mutase , active site , residue (chemistry) , chemistry , mutase , molecular dynamics , stereochemistry , enzyme , biochemistry , computational chemistry , biosynthesis
The removal of a key residue (Arg 90) from the chorismate mutase enzyme destroys the balance of the interactions in the active site required for stabilizing the conformation of the transition state in the Claisen rearrangement of chorismate to prephenate (see picture).