Abstract
The kinetic mechanism of a semipurified tRNA (uracil-5-)-methyltransferase (EC 2.1.1.35) preparation obtained from E. coli was studied at pH 9.0 in the presence and absence of products. The initial velocity and product inhibition patterns are consistent with a random order of addition of adenosylmethionine and tRNA to separate and independent binding sites on the enzyme. Values were determined for the Km and product inhibitor constants.