| EC |
3.4.24.57 |
| Accepted name: |
O-sialoglycoprotein endopeptidase |
| 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 |
| Other name(s): |
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, MetaCyc, MEROPS, PDB, 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. [DOI] [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, CD 43, CD 44, and CD45 by a novel glycoprotease from Pasteurella haemolytica. J. Immunol. 148 (1992) 1458–1464. [PMID: 1371528] |
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| [EC 3.4.24.57 created 1993] |
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