Abstract
By use of a new technique for the assay of products resulting from hydrolyses catalyzed by urease, the following substituted ureas and esters of carbamic acid have been found to be substrates for urease: methyl-, ethyl-, formyl-, and allylurea, and methyl and ethyl carbamates. The rate–pH profiles have been determined for urea and these substrates, under conditions of enzyme saturation and in the absence of buffer. Variations of rate with substrate concentration have been studied at the optimum pH in each case; approximate Michaelis–Menten kinetics was observed in all cases, but with substrate inhibition for the substituted ureas, not for the carbamates. All of the reactions were inhibited by the NH4+ ions formed.
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