Mechanisms of peptide hydrolysis by aspartyl and metalloproteases.
Phys Chem Chem Phys
; 18(36): 24790-24801, 2016 Sep 14.
Article
em En
| MEDLINE
| ID: mdl-27711373
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
Limite:
Animals
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article