http://purl.uniprot.org/citations/16517617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16517617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16517617 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.org/dc/terms/identifier | "doi:10.1128/aem.72.3.1739-1748.2006"xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.org/dc/terms/identifier | "doi:10.1128/aem.72.3.1739-1748.2006"xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.org/dc/terms/identifier | "doi:10.1128/AEM.72.3.1739-1748.2006"xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Monod M."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Monod M."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Reichard U."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Reichard U."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Lechenne B."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Lechenne B."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Jousson O."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Jousson O."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Grouzmann E."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Grouzmann E."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Asif A.R."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Asif A.R."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Streit F."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/author | "Streit F."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/name | "Appl. Environ. Microbiol."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/name | "Appl. Environ. Microbiol."xsd:string |
http://purl.uniprot.org/citations/16517617 | http://purl.uniprot.org/core/pages | "1739-1748"xsd:string |