O-sialoglycoprotein endopeptidase (EC 3.4.24.57, glycoprotease, glycophorin A proteinase, glycoproteinase, sialoglycoprotease, sialoglycoproteinase, "OSGE") is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
Hydrolysis of O-sialoglycoproteins; cleaves -Arg31-Asp- bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated
This enzyme is secreted by the bacterium Pasteurella haemolytica.
Referencesedit
^Abdullah KM, Lo RY, Mellors A (September 1991). "Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene". Journal of Bacteriology. 173 (18): 5597–603. doi:10.1128/jb.173.18.5597-5603.1991. PMC208286. PMID 1885539.
^Abdullah KM, Udoh EA, Shewen PE, Mellors A (January 1992). "A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins". Infection and Immunity. 60 (1): 56–62. PMC257502. PMID 1729196.
^Sutherland DR, Abdullah KM, Cyopick P, Mellors A (March 1992). "Cleavage of the cell-surface O-sialoglycoproteins CD34, CD43, CD44, and CD45 by a novel glycoprotease from Pasteurella haemolytica". Journal of Immunology. 148 (5): 1458–64. PMID 1371528.
External linksedit
O-sialoglycoprotein+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
sialoglycoprotein, endopeptidase, glycoprotease, glycophorin, proteinase, glycoproteinase, sialoglycoprotease, sialoglycoproteinase, osge, enzyme, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 57cas, 129430, 1databasesintenzintenz, viewb. O sialoglycoprotein endopeptidase EC 3 4 24 57 glycoprotease glycophorin A proteinase glycoproteinase sialoglycoprotease sialoglycoproteinase OSGE is an enzyme 1 2 3 This enzyme catalyses the following chemical reactionO sialoglycoprotein endopeptidaseIdentifiersEC no 3 4 24 57CAS no 129430 53 1DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Hydrolysis of O sialoglycoproteins cleaves Arg31 Asp bond in glycophorin A Does not cleave unglycosylated proteins desialylated glycoproteins or glycoproteins that are only N glycosylatedThis enzyme is secreted by the bacterium Pasteurella haemolytica References edit Abdullah KM Lo RY Mellors A September 1991 Cloning nucleotide sequence and expression of the Pasteurella haemolytica A1 glycoprotease gene Journal of Bacteriology 173 18 5597 603 doi 10 1128 jb 173 18 5597 5603 1991 PMC 208286 PMID 1885539 Abdullah KM Udoh EA Shewen PE Mellors A January 1992 A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O sialoglycoproteins Infection and Immunity 60 1 56 62 PMC 257502 PMID 1729196 Sutherland DR Abdullah KM Cyopick P Mellors A March 1992 Cleavage of the cell surface O sialoglycoproteins CD34 CD43 CD44 and CD45 by a novel glycoprotease from Pasteurella haemolytica Journal of Immunology 148 5 1458 64 PMID 1371528 External links editO sialoglycoprotein endopeptidase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title O sialoglycoprotein endopeptidase amp oldid 1172355783, wikipedia, wiki, book, books, library,
