Sedolisins, a new class of secreted proteases from Aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs

Détails

ID Serval
serval:BIB_32047F1B80C0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Sedolisins, a new class of secreted proteases from Aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs
Périodique
Applied and Environmental Microbiology
Auteur⸱e⸱s
Reichard  U., Lechenne  B., Asif  A. R., Streit  F., Grouzmann  E., Jousson  O., Monod  M.
ISSN
0099-2240 (Print)
Statut éditorial
Publié
Date de publication
03/2006
Volume
72
Numéro
3
Pages
1739-48
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Mar
Résumé
The secreted proteolytic activity of Aspergillus fumigatus is of potential importance as a virulence factor and in the industrial hydrolysis of protein sources. The A. fumigatus genome contains sequences that could encode a five-member gene family that produces proteases in the sedolisin family (MEROPS S53). Four putative secreted sedolisins with a predicted 17- to 20-amino-acid signal sequence were identified and termed SedA to SedD. SedA produced heterologously in Pichia pastoris was an acidic endoprotease. Heterologously produced SedB, SedC, and SedD were tripeptidyl-peptidases (TPP) with a common specificity for tripeptide-p-nitroanilide substrates at acidic pHs. Purified SedB hydrolyzed the peptide Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe to Arg-Pro-Gly, Asp-Arg-Ile, and Tyr-Val-His-Pro-Phe, thereby confirming TPP activity of the enzyme. SedB, SedC, and SedD were detected by Western blotting in culture supernatants of A. fumigatus grown in a medium containing hemoglobin as the sole nitrogen source. A degradation product of SedA also was observed. A search for genes encoding sedolisin homologues in other fungal genomes indicates that sedolisin gene families are widespread among filamentous ascomycetes.
Mots-clé
Animals Aspergillus fumigatus/*enzymology/genetics/growth & development Carboxypeptidases/chemistry/genetics/metabolism/*secretion Culture Media, Conditioned Endopeptidases/metabolism Fungal Proteins/genetics/metabolism Humans Hydrogen-Ion Concentration Phylogeny Pichia/enzymology/genetics Rabbits Serine Endopeptidases/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 11:55
Dernière modification de la notice
20/08/2019 14:17
Données d'usage