H. NH2 Bond cleavage (R145) n-1 NH, .(H69) Zn² (E72) (H196) (E270) H NH, (R145) 'n-1 NH, (H69) (E72) (H196) (E270) NH, (R145) H I., NH, Rn-1 Но (H69) Zn2 (E72) (H196) (E270) Release products and blnd water A FIGURE 8.19 The mechanism of the protease carboxypeptidase A. The zinc ion (orange circle) binds a water molecule (blue) and serves as an electrostatic catalyst to promote hydrolysis of the C-terminal amino acid from a peptide substrate (green). It does so by stabilizing the nega- tive charge on the oxygen in the tetrahedral transition state. Enzyme active site residues are indicated by black coloring. The bond cleaved is indicated by the dashed red arrow.

H. NH2 Bond cleavage (R145) n-1 NH, .(H69) Zn² (E72) (H196) (E270) H NH, (R145) 'n-1 NH, (H69) (E72) (H196) (E270) NH, (R145) H I., NH, Rn-1 Но (H69) Zn2 (E72) (H196) (E270) Release products and blnd water A FIGURE 8.19 The mechanism of the protease carboxypeptidase A. The zinc ion (orange circle) binds a water molecule (blue) and serves as an electrostatic catalyst to promote hydrolysis of the C-terminal amino acid from a peptide substrate (green). It does so by stabilizing the nega- tive charge on the oxygen in the tetrahedral transition state. Enzyme active site residues are indicated by black coloring. The bond cleaved is indicated by the dashed red arrow.

Organic Chemistry

8th Edition

ISBN:9781305580350

Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Chapter20: Dienes, Conjugated Systems, And Pericyclic Reactions

Section: Chapter Questions

Problem 20.48P

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