Hydrolysis: Peptide Bonds by P. D. Boyer

By P. D. Boyer

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The substrate molecule is shown as dots which do not match the contours of the protein or solution. (9) OR-TEP drawing of Fig. 6a: the C-terminal helix. (h) ORTEP drawing of Fig. (i) OR-TEP drawing of Fig. 6a: the region of the disulfide bond. 1. 29 CABBOXYPEPTIDASEl A -C-a9FN- i $ ? - -%O-N C-239- , i -2Od$-~-C-202-N-$-ZQl-~-C-2OO-l,+ 0 d \\ \ ? 5-F- I ? 0 ? -N-C-Sl-N-C-50-N-C-40-NI ? I 1 I I ? i o i 9 ? 1 I -32-C -N-33-C-N-34-C-K35C-N-38-C- b b Ro. 7. Schematic drawing of the pleated sheet bonds are shown as dashed lines.

W. H. Bishop, F. A. Quiocho, and F. M. Richards, Biochemistry 5, 4077 (1966). Carboxypeptidase B J . E. FOLK I . Introduction . . . . . . A. Historical Background . . . . 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 .

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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