Mechanisms of peptide hydrolysis by aspartyl and metalloproteases

Thomas J. Paul, Arghya Barman, Mehmet Ozbil, Ram Prasad Bora, Tingting Zhang, Gaurav Sharma, Zachary Hoffmann, Rajeev Prabhakar

Research output: Contribution to journalReview article

8 Scopus citations

Abstract

Peptide hydrolysis has been involved in a wide range of biological, biotechnological, and industrial applications. In this perspective, the mechanisms of three distinct peptide bond cleaving enzymes, beta secretase (BACE1), insulin degrading enzyme (IDE), and bovine lens leucine aminopeptidase (BILAP), have been discussed. BACE1 is a catalytic Asp dyad [Asp, Asp-] containing aspartyl protease, while IDE and BILAP are mononuclear [Zn(His, His, Glu)] and binuclear [Zn1(Asp, Glu, Asp)-Zn2(Lys, Glu, Asp, Asp)] core possessing metallopeptidases, respectively. Specifically, enzyme-substrate interactions and the roles of metal ion(s), the ligand environment, second coordination shell residues, and the protein environment in the functioning of these enzymes have been elucidated. This information will be useful to design small inhibitors, activators, and synthetic analogues of these enzymes for biomedical, biotechnological, and industrial applications.

Original languageEnglish (US)
Pages (from-to)24790-24801
Number of pages12
JournalPhysical Chemistry Chemical Physics
Volume18
Issue number36
DOIs
StatePublished - 2016

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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    Paul, T. J., Barman, A., Ozbil, M., Bora, R. P., Zhang, T., Sharma, G., Hoffmann, Z., & Prabhakar, R. (2016). Mechanisms of peptide hydrolysis by aspartyl and metalloproteases. Physical Chemistry Chemical Physics, 18(36), 24790-24801. https://doi.org/10.1039/c6cp02097f