Asp- bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated
Reaction: Hydrolysis of O-sialoglycoproteins; cleaves -Arg31Asp- bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated
Other names: glycoprotease; glycophorin A proteinase; glycoproteinase; sialoglycoprotease; sialoglycoproteinase
Comments: An enzyme secreted by the bacterium Pasteurella haemolytica. Inhibited by EDTA (100 mM) and 1,10-phenanthroline. Type example of peptidase family M22
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 129430-53-1
References
1. Abdullah, K.M., Lo, R.Y.C. and Mellors, A. Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene. J. Bacteriol. 173 (1991) 5597-5603. [PMID: 1885539]
2. Abdullah, K.M., Udoh, E.A., Shewen, P.E. and Mellors, A. A neutral glycoprotease of Pasteurella haemolytica A1 specifically cleaves O-sialoglycoproteins. Infect. Immun. 60 (1992) 56-62. [PMID: 1729196]
3. Sutherland, D.R., Abdullah, K.M., Cyopick, P. and Mellors, A. Cleavage of the cell-surface O-sialoglycoproteins CD34, CD43, CD44, and CD45 by a novel glycoprotease from Pasteurella haemolytica. J. Immunol. 148 (1992) 1458-1464. [PMID: 1371528]