3.4.24.57: O-sialoglycoprotein endopeptidase
This is an abbreviated version!
For detailed information about O-sialoglycoprotein endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.57
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3.4.24.57
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o-sialoglycoproteins
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pasteurella
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haemolytica
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neuraminidase
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psgl-1
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p-selectin
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ligand-1
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pasteurellosis
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sialomucins
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leukotoxin
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drug development
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medicine
- 3.4.24.57
- o-sialoglycoproteins
- pasteurella
- haemolytica
- neuraminidase
- psgl-1
-
p-selectin
- ligand-1
- pasteurellosis
-
sialomucins
- leukotoxin
- drug development
- medicine
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 =
Synonyms
Gcp, Glycophorin A proteinase, Glycoprotease, Glycoproteinase, O-sialoglycoprotein endopeptidase, OSE, OSGE, PG0778, PG1724, Proteinase, glyco-, Sialoglycoprotease, Sialoglycoproteinase
ECTree
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Disease
Disease on EC 3.4.24.57 - O-sialoglycoprotein endopeptidase
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Carcinoma
Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica.
Neoplasms
Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica.
Pasteurellosis, Pneumonic
Comparison of the recombinant and authentic forms of the Pasteurella haemolytica A1 glycoprotease.
Pneumonia
Cleavage of epitectin, a mucin-type sialoglycoprotein, from the surface of human laryngeal carcinoma cells by a glycoprotease from Pasteurella haemolytica.
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