Enzymes with Unfavorable Binding Inhibition

The simplest case of a reactor is a cuvette, such as that in a photometer. From the Michaelis-Menten equation and the equation for the batch reactor [Eqs. (5.11) and (5.12)], respectively, as well as the definition for the degree of conversion % for the simple reaction S — P, x = 1 - [S]/[S0] = [P]/[S0], the integrated equation (5.15) for an enzyme reaction following a Michaelis-Menten law in a batch reactor is obtained. 

The same form of equation results from the equation for the PFR [Eq. (5.13)]. For a CSTR with the mass balance given by Eq. (5.14), the integrated rate equation (5.16) results from a procedure similar to that for the batch reactor. 

Cases 2 and 3 will be discussed below in connection with inhibition. 

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The amino acid with the next highest i cleavage probability is Gin with 0.14. Two of the leucyl residues are terminal and will not interact well with pepsin (see Table VI). The third (Leu-6) has a prolyl residue it 2> unfavorable interaction. The fourth leucine residue (Leu-12) is part of a sequence (Fig.5) where each of the 7 subsites has an amino acid residue which is either favorable or neutral except one. There is a Lys at P3, and we propose that this region of the peptide inhibits pepsin because the peptide either binds nonproductively or induces a conformational change in the enzyme. 

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