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By P. D. Boyer

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The most interesting of the water molecules which have three ligands is that which is bound to one carboxyl oxygen of Glu 108. Because the other two ligands to this water molecule are backbone carbonyl oxygen atoms, this must be a trapped H30+ion which neutralizes the 36 J . A. HARTSUCK AND W. N . LIPSCOMB buried charge of Glu 108. We caution that the suggestion that this molecule exists as H,O+ rather than H,O depends upon the chemical identification of residue 108 as Glu and not Gln. Finally, one water molecule makes only two hydrogen bonds with a backbone carbonyl oxygen and with another water.

B . Distribution I1. Purification of the Enzyme and Zymogen; Assay . I11. Physical-Chemical Properties of Carboxypeptidaae B . A . Physical Properties . . . . B . Chemical Composition . . . . C . End Groups and Amino Acid Sequences . . D. Early Considerations of Homology between Bovine Carboxypeptidases A and B . . . IV . Physical-Chemical Properties and Activation of Procarboxypeptidase B . . . . . V . Enzymic Properties of Carboxypeptidase B . . A . Specificity . . . . . B .

Koshland, Proc. Natl. Acad. Sci. S. 44, 98 (1958). D. E. Koshland, Cold Spring Harbor S y n p . Quant. Bbl. 28, 473 (1963). 1. CARBOXYPEPTIDASE A 43 10. Use of the CPA Model to Interpret the Enzyme Substrate Specificity If we assume that in the productive binding mode substrates are bound to CPA with the C-terminal side chain in the pocket, with the terminal carboxyl group salt linked to Arg 145,with the carbonyl group of the scissile peptide bond bound to zinc; and with the OH of Tyr 248 near enough to donate a proton to the NH of the susceptible peptide bond, then it is possible to build models of substrates other than Gly-Tyr interacting with CPA.

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