Abstract
The kinetic mechanism of a semipurified tRNA (uracil-5-)-methyltransferase (EC 2.1.1.35) preparation obtained from Escherichia coli has been 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 transfer RNA to separate and independent binding sites on the enzyme. Values have been determined for the Michaelis and product inhibitor constants.
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