Biology:O-sialoglycoprotein endopeptidase
From HandWiki
| O-sialoglycoprotein endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.57 | ||||||||
| CAS number | 129430-53-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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.
References
- ↑ "Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene". Journal of Bacteriology 173 (18): 5597–603. September 1991. doi:10.1128/jb.173.18.5597-5603.1991. PMID 1885539.
- ↑ "A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins". Infection and Immunity 60 (1): 56–62. January 1992. PMID 1729196.
- ↑ "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. March 1992. PMID 1371528.
External links
- O-sialoglycoprotein+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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