The competitive inhibition of of the urease-catalyzed hydrolysis of urea by phosphate

The urease-catalyzed hydrolysis of urea has been found to be competitively inhibited by phosphate at pH 7.0 and 25°. The Michaelis constant of the urea-urease system has been found to be approximately 0.003 M urea and the comparable constant defining the phosphate-urease system 0.035 M phosphate

The hydrolysis of N-benzoyl-L-argininamide by crystalline trypsin

A reinvestigation of the kinetics of hydrolysis of N-benzoyl-n-argininamide by crystalline trypsin has led to the conclusion that the hydrolysis products enter into the over-all reaction as inhibitors