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Mechanisms of peptide hydrolysis by aspartyl and metalloproteases.
Paul, Thomas J; Barman, Arghya; Ozbil, Mehmet; Bora, Ram Prasad; Zhang, Tingting; Sharma, Gaurav; Hoffmann, Zachary; Prabhakar, Rajeev.
Afiliação
  • Paul TJ; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Barman A; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Ozbil M; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Bora RP; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Zhang T; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Sharma G; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Hoffmann Z; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
  • Prabhakar R; Department of Chemistry, University of Miami, 1301 Memorial Drive, Coral Gables, Florida 33146, USA. rpr@miami.edu.
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.
Assuntos
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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
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Peptídeos Limite: Animals Idioma: En Ano de publicação: 2016 Tipo de documento: Article