BioPAX pathway converted from "PGLYRP2 binds bacterial peptidoglycan" in the Reactome database.LEFT-TO-RIGHTPGLYRP2 binds bacterial peptidoglycanThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>PGNGlcNac-(1-->4)MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2N-acetyl-beta-D-glycosaminyl-(1->4)-N-acetylmuramoyl peptidebeta-GlcNAc-(1->4)-MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2peptidoglycanReactome DB_ID: 6789198cell wallGENE ONTOLOGYGO:0005618beta-GlcNAc-(1->4)-MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2 [ChEBI:55424]beta-GlcNAc-(1->4)-MurNAc-L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2ChEBICHEBI:55424Reactome Database ID Release 756789198Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6789198ReactomeR-ALL-67891983Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-ALL-6789198.3Reactomehttp://www.reactome.orgPGLYRP2 dimerReactome DB_ID: 9797984extracellular regionGENE ONTOLOGYGO:0005576Q8VCS0Pglyrp2PGLYRP2Reactome DB_ID: 9797982UniProt:Q8VCS0Pglyrp2Mus musculusNCBI Taxonomy10090UniProtQ8VCS022EQUAL576EQUALReactome Database ID Release 759797982Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9797982ReactomeR-MMU-67992961Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-6799296.12Reactome Database ID Release 759797984Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9797984ReactomeR-MMU-89334681Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-8933468.1PGLYRP2:peptidoglycanReactome DB_ID: 9797986PeptidoglycanGlcNAc(1-->4)MurNAc:L-Ala-gamma-D-Glu-L-Lys-(D-Ala)2GlcNAc(1-->4)MurNAc:peptideReactome DB_ID: 6788957Reactome Database ID Release 756788957Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6788957ReactomeR-ALL-67889572Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-ALL-6788957.2ChEBI8005additional informationMIMI:036111Reactome Database ID Release 759797986Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9797986ReactomeR-MMU-67999881Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-6799988.1Reactome Database ID Release 759797991Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9797991ReactomeR-MMU-67999811Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-6799981.1Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are innate immunity molecules that contain a conserved peptidoglycan‑binding type 2 amidase domain that is homologous to bacteriophage and bacterial type 2 amidases (Kang D et al. 1998; Liu C et al. 2001; Royet J and Dziarski R 2007; Royet J et al. 2011; Dziarski R et al. 2016). Mammals have a family of four PGRPs (PGLYRP1, 2, 3 & 4) that are differentially expressed in a cell‑type‑ or tissue‑specific manner. PGLYRP2 (also known as PGRP-L) is constitutively expressed in the liver, from which it is secreted into blood as non-disulfide‑linked dimers (Liu C et al. 2001; Zhang Y et al. 2005; De Pauw P et al. 1995; Hoijer MA et al. 1996). PGLYRP2 expression can be also induced in the skin and intestine upon exposure to bacteria or pro-inflammatory cytokines (Wang H et al. 2005; Li X et al. 2006). The constitutive expression of PGLYRP2 in the liver and induced expression in epithelial cells is regulated by different transcription factors, the binding sequences for which are located in different regions of the pglyrp2 promoter (Li X et al. 2006). PGRP2 binds to bacterial cell wall peptidoglycan and functions as N‑acetylmuramoyl‑L‑alanine amidase that hydrolyzes the amide bond between the MurNAc and L‑alanine in peptidoglycan (Wang ZM et al. 2003; Zhang Y et al. 2005). The minimal peptidoglycan fragment hydrolyzed by PGLYRP2 is MurNAc-tripeptide (Wang ZM et al. 2003). PGLYRP2 has a conserved Zn(2+)‑binding site in the peptidoglycan‑binding groove, which is also present in bacteriophage type 2 amidases, and PGLYRP2 requires Zn(2+) for its amidase activity (Wang ZM et al. 2003). The amidase activity of mammalian PGLYRP2 is though to eliminate the pro‑inflammatory peptidoglycan and, therefore, prevent over‑activation of the immune system and excessive inflammation (Hoijer MA et al. 1997; Royet J and Dziarski R 2007). In addition to its amidase activity, PGLYRP2 also has antibacterial activity against both Gram-positive and Gram-negative bacteria and Chlamydia (Bobrovsky P et al. 2016), similar to PGLYRP1, PGLYRP3, and PGLYRP4 (Lu X et al. 2006; Wang M et al. 2007).16714290Pubmed2006Differential expression of peptidoglycan recognition protein 2 in the skin and liver requires different transcription factorsLi, XinnaWang, ShiyongWang, HaitaoGupta, DipikaJ. Biol. Chem. 281:20738-488605233Pubmed1996Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodiesHoijer, M AMelief, M JKeck, WHazenberg, M PBiochim. Biophys. Acta 1289:57-649780123742797ISBN2016Peptidoglycan Recognition Proteins and LysozymeDziarski, RomanRoyet, JulienGupta, DipikaEncyclopedia of Immunobiology (Book)11461926Pubmed2001Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition moleculesLiu, CXu, ZGupta, DDziarski, RJ. Biol. Chem. 276:34686-949459617Pubmed1997Inflammatory properties of peptidoglycan are decreased after degradation by human N-acetylmuramyl-L-alanine amidaseHoijer, M AMelief, M JDebets, RHazenberg, M PEur. Cytokine Netw. 8:375-8122076558Pubmed2011Peptidoglycan recognition proteins: modulators of the microbiome and inflammationRoyet, JulienGupta, DipikaDziarski, RomanNat. Rev. Immunol. 11:837-5116354652Pubmed2006Peptidoglycan recognition proteins are a new class of human bactericidal proteinsLu, XiaofengWang, MinhuiQi, JinWang, HaitaoLi, XinnaGupta, DipikaDziarski, RomanJ. Biol. Chem. 281:5895-9077663175Pubmed1995Characterization of human serum N-acetylmuramyl-L-alanine amidase purified by affinity chromatographyDe Pauw, PNeyt, CVanderwinkel, EWattiez, RFalmagne, PProtein Expr. Purif. 6:371-817312159Pubmed2007Human peptidoglycan recognition proteins require zinc to kill both gram-positive and gram-negative bacteria and are synergistic with antibacterial peptidesWang, MinhuiLiu, Li-HuiWang, ShiyongLi, XinnaLu, XiaofengGupta, DipikaDziarski, RomanJ. Immunol. 178:3116-259707603Pubmed1998A peptidoglycan recognition protein in innate immunity conserved from insects to humansKang, DLiu, GLundström, AGelius, ESteiner, HProc. Natl. Acad. Sci. U.S.A. 95:10078-8216239516Pubmed2005Peptidoglycan recognition protein 2 (N-acetylmuramoyl-L-Ala amidase) is induced in keratinocytes by bacteria through the p38 kinase pathwayWang, HaitaoGupta, DipikaLi, XinnaDziarski, RomanInfect. Immun. 73:7216-2527160295Pubmed2016Recombinant Human Peptidoglycan Recognition Proteins Reveal Antichlamydial ActivityBobrovsky, PavelManuvera, ValentinPolina, NadezhdaPodgorny, OlegPrusakov, KirillGovorun, VadimLazarev, VassiliInfect. Immun. 84:2124-3014506276Pubmed2003Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidaseWang, Zheng-MingLi, XinnaCocklin, Ross RWang, MinhuiWang, MuFukase, KoichiInamura, SeiichiKusumoto, ShoichiGupta, DipikaDziarski, RomanJ. Biol. Chem. 278:49044-5216054449Pubmed2005Identification of serum N-acetylmuramoyl-l-alanine amidase as liver peptidoglycan recognition protein 2Zhang, Yinongvan der Fits, LeslieVoerman, Jane SMelief, Marie-JoseLaman, Jon DWang, MuWang, HaitaoWang, MinhuiLi, XinnaWalls, Chad DGupta, DipikaDziarski, RomanBiochim. Biophys. Acta 1752:34-4617363965Pubmed2007Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defencesRoyet, JulienDziarski, RomanNat. Rev. Microbiol. 5:264-77inferred from electronic annotationEVIDENCE CODEECO:0000203