The mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic interactions with TS are much weaker than with chorismate. Interactions and the mechanism of catalysis of chorismate --> prephenate by the EcCM enzyme are discussed.
Hur
Sun
S
Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, USA.
Bruice
Thomas C
TC
D001665:Binding Sites; D002151:Calorimetry; D002384:Catalysis; D002826:Chorismate Mutase / Q000737:chemistry / Q000378:metabolism*; D003509:Cyclohexanecarboxylic Acids / Q000737:chemistry / Q000378:metabolism*; D053138:Cyclohexenes; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D013816:Thermodynamics
D003509:Cyclohexanecarboxylic Acids; D053138:Cyclohexenes; D002826:Chorismate Mutase; C005550:prephenic acid