Journal article

KINETIC-STUDIES ON THE MECHANISM OF CHORISMATE MUTASE PREPHENATE DEHYDRATASE FROM ESCHERICHIA-COLI-K12

GS BALDWIN, BE DAVIDSON

BIOCHIMICA ET BIOPHYSICA ACTA | ELSEVIER SCIENCE BV | Published : 1983

Abstract

The effect of pH on chorismate mutase/prephenate dehydratase (chorismate pyruvate mutase/prephenate hydro-lyase (decarboxylating) EC 5.4.99.5/EC 4.2.1.51) from Escherichia coli K12 has been studied. While the maximum velocity of both activities is independent of pH, Km for chorismate or prephenate shows a complex pH dependence. Differences in mutase activity in acetate/phosphate/borate and citrate/phosphate/borate buffers were traced to inhibition by citrate. When a variety of analogues of citrate were tested as possible inhibitors of the enzyme, several were found to inhibit mutase and dehydratase activities to different extents, and by different mechanisms. Thus citrate competitively inhib..

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