On the stability of tetrahedral intermediates within the active sites of serine and cysteine proteases.
An empirical method used for the calculation of the equilibrium constants for the formation of tetrahedral intermediates in solutions is extended for the prediction of the stability of these intermediates within the active sites of several serine proteases and papain. It is concluded that there is very little chance of observing the accumulation of such an intermediate in the course of the hydrolysis of an amide or peptide by these enzymes.
D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D006868:Hydrolysis; D007700:Kinetics; D008956:Models, Chemical; D012697:Serine Endopeptidases
D010450:Endopeptidases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases