O-sialoglycoprotein endopeptidase
Appearance
(Redirected from Glycoprotease)
O-sialoglycoprotein endopeptidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.24.57 | ||||||||
CAS no. | 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
[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
[edit]- O-sialoglycoprotein+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)