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http://purl.uniprot.org/citations/12496260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12496260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12496260http://www.w3.org/2000/01/rdf-schema#comment"Recent studies of peptidoglycan recognition protein (PGRP) have shown that 2 of the 13 Drosophila PGRP genes encode proteins that function as receptors mediating immune responses to bacteria. We show here that another member, PGRP-SC1B, has a totally different function because it has enzymatic activity and thereby can degrade peptidoglycan. A mass spectrometric analysis of the cleavage products demonstrates that the enzyme hydrolyzes the lactylamide bond between the glycan strand and the cross-linking peptides. This result assigns the protein as an N-acetylmuramoyl-l-alanine amidase (EC ), and the corresponding gene is thus the first of this class to be described from a eukaryotic organism. Mutant forms of PGRP-SC1B lacking a potential zinc ligand are enzymatically inactive but retain their peptidoglycan affinity. The immunostimulatory properties of PGRP-SC1B-degraded peptidoglycan are much reduced. This is in striking contrast to lysozyme-digested peptidoglycan, which retains most of its elicitor activity. This points toward a scavenger function for PGRP-SC1B. Furthermore, a sequence homology comparison with phage T7 lysozyme, also an N-acetylmuramoyl-l-alanine amidase, shows that as many as six of the Drosophila PGRPs could belong to this class of proteins."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m208900200"xsd:string
http://purl.uniprot.org/citations/12496260http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m208900200"xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Karlsson J."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Karlsson J."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Steiner H."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Steiner H."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Mellroth P."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/author"Mellroth P."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/pages"7059-7064"xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/pages"7059-7064"xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/title"A scavenger function for a Drosophila peptidoglycan recognition protein."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/title"A scavenger function for a Drosophila peptidoglycan recognition protein."xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12496260http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12496260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12496260
http://purl.uniprot.org/citations/12496260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12496260
http://purl.uniprot.org/citations/12496260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12496260
http://purl.uniprot.org/citations/12496260http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12496260