English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/87718
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


Structural evidence for standard-mechanism inhibition in metallopeptidases from a complex poised to resynthesize a peptide bond

AuthorsArolas, Joan L. ; Botelho, Tiago O.; Vilcinskas, Andreas; Gomis-Rüth, F. Xavier
Issue Date2011
CitationAngewandte Chemie International Edition 50(44): 10357-10360 (2011)
AbstractIt goes both ways: An unprecedented mechanism of metalloendopeptidase inhibition has been identified for the insect metalloproteinase inhibitor, which is both cleaved and rejoined at bond Asn56-Ile57 by thermolysin under appropriate conditions. A two-product complex is formed after hydrolysis and, simultaneously, a Michaelis complex is poised for synthesis of a peptide bond (see crystal structure). Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Identifiersdoi: 10.1002/anie.201103262
issn: 1433-7851
e-issn: 1521-3773
Appears in Collections:(IBMB) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.