Which one among aspartyl protease, metallopeptidase, and artificial metallopeptidase is the most efficient catalyst in peptide hydrolysis?

Ram Prasad Bora, Arghya Barman, Xiaoxia Zhu, Mehmet Ozbil, Rajeev Prabhakar

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

In this comparative DFT study, the hydrolysis of a peptide bond (Phe1-Phe2) by the following three types of catalysts has been studied: (1) β-secretase (BACE2), (2) matrix metalloproteinase (MMP) and insulin degrading enzyme (IDE), and (3) [Pd(H2O)4]2+ (IMPC) and [Pd2(μ-OH)([18]aneN6)] 3+ (IDPC). The computed energetics predict that among these catalysts, the Zn2+ metal center containing MMP is the most efficient in catalyzing this reaction. The two active site aspartate residues containing BACE2 catalyze this reaction with 5.0 kcal/mol higher barrier than MMP. The substitution of a His ligand with Glu in the metal center of MMP generates the active site of IDE that catalyzes the reaction with a 6.9 kcal/mol higher barrier than MMP. Both artificial peptidases IMPC and I DPC catalyze this reaction with significantly high barriers of 35.4 and 31.0 kcal/mol, respectively. The computed energetics of all the catalysts are in line with the available experimental and theoretical data.

Original languageEnglish (US)
Pages (from-to)10860-10875
Number of pages16
JournalJournal of Physical Chemistry B
Volume114
Issue number33
DOIs
StatePublished - Aug 26 2010

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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