CINECA IRIS Institutional Research Information System
IRIS è l'Anagrafe della ricerca dell'Università degli Studi di Trento, e ha lo scopo di raccogliere, documentare, conservare e diffondere, anche ad accesso aperto, la produzione scientifica degli autori afferenti all'Università degli Studi di Trento.
EnglishProlyl peptidases of the MEROPS S28 family are of particular interest because they are key enzymes in the digestion of proline-rich peptides. A BLAST analysis of the Aspergillus oryzae genome revealed sequences coding for four proteases of the S28 family. Three of these proteases, AoS28A, AoS28B, and AoS28C, were previously characterized as acidic prolyl endopeptidases. The fourth protease, AoS28D, showed high sequence divergence with other S28 proteases and belongs to a phylogenetically distinct cluster together with orthologous proteases from other Aspergillus species. The objective of the present paper was to characterize AoS28D protease in terms of substrate specificity and activity. AoS28D produced by gene overexpression in A. oryzae and in Pichia pastoris was a 70-kDa glycoprotein with a 10-kDa sugar moiety. In contrast with other S28 proteases, AoS28D did not hydrolyze internal Pro-Xaa bonds of several tested peptides. Similarly, to human lysosomal Pro-Xaa carboxypeptidase, AoS28D demonstrated selectivity for cleaving C-terminal Pro-Xaa bonds which are resistant to carboxypeptidases of the S10 family concomitantly secreted by A. oryzae. Therefore, AoS28D could act in synergy with these enzymes during sequential degradation of a peptide from its C-terminus.
AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae / Salamin, Karine; Eugster, Philippe J; Jousson, Olivier; Waridel, Patrice; Grouzmann, Eric; Monod, Michel. - In: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. - ISSN 0175-7598. - 101(2017), pp. 4129-4137. [10.1007/s00253-017-8186-8]
Scheda prodotto non validato
I dati visualizzati non sono stati ancora sottoposti a validazione formale da parte dello Staff di IRIS, ma sono stati ugualmente trasmessi al Sito Docente Cineca (Loginmiur).
| Titolo: | AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae | |
| Autori: | Salamin, Karine; Eugster, Philippe J; Jousson, Olivier; Waridel, Patrice; Grouzmann, Eric; Monod, Michel | |
| Autori Unitn: | ||
| Titolo del periodico: | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | |
| Anno di pubblicazione: | 2017 | |
| Codice identificativo Scopus: | 2-s2.0-85013387708 | |
| Codice identificativo Pubmed: | 28229206 | |
| Codice identificativo ISI: | WOS:000400069500015 | |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1007/s00253-017-8186-8 | |
| Handle: | http://hdl.handle.net/11572/173003 | |
| Citazione: | AoS28D, a proline-Xaa carboxypeptidase secreted by Aspergillus oryzae / Salamin, Karine; Eugster, Philippe J; Jousson, Olivier; Waridel, Patrice; Grouzmann, Eric; Monod, Michel. - In: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. - ISSN 0175-7598. - 101(2017), pp. 4129-4137. [10.1007/s00253-017-8186-8] | |
| Appare nelle tipologie: | 03.1 Articolo su rivista (Journal article) |
File in questo prodotto:
| File | Descrizione | Tipologia | Licenza | |
|---|---|---|---|---|
| 2017Salamin_ApplMicrobiolBiotechnol.pdf | Versione editoriale (Publisher’s layout) | Tutti i diritti riservati (All rights reserved) | Administrator |
Copyright © 2021