Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme.
The relationship between the active sites of the bifunctional enzyme chorismate mutase-prephenate dehydratase has been examined. Steady-state kinetic investigations of the reactions with chorismate or prephenate as substrate and studies of the overall conversion of chorismate to phenylpyruvate indicate that there are two distinct active sites. One site is responsible for the mutase activity and the other for the dehydratase activity. Studies of the overall reaction using radioactive chorismate show that prephenate, which is formed from chorismate, dissociates from the mutase site and equilibrates with the bulk medium before combining at the dehydratase site. No evidence was obtained for direct channeling of prephenate from one site to the other, or for any strong interaction between the sites.
D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology*; D006836:Hydro-Lyases / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D011302:Prephenate Dehydratase / Q000378:metabolism*
D006836:Hydro-Lyases; D011302:Prephenate Dehydratase