Peptidyl-Asp metalloendopeptidase
| Peptidyl-Asp metalloendopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.33 | ||||||||
| CAS number | 55576-49-3 | ||||||||
| 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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Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of Xaa-Asp, Xaa-Glu and Xaa- cysteic acid bonds
This metalloenzyme is isolated from Pseudomonas fragi.
References
- ↑ Porzio, M.A.; Pearson, A.M. (1975). "Isolation of an extracellular neutral proteinase from Pseudomonas fragi". Biochim. Biophys. Acta. 384: 235–241. doi:10.1016/0005-2744(75)90112-6. PMID 236771.
- ↑ Drapeau, G.R. (1980). "Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi". J. Biol. Chem. 255: 839–840. PMID 7188696.
- ↑ Ingrosso, D.; Fowler, A.V.; Bleibaum, J.; Clarke, S. (1989). "Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins". Biochem. Biophys. Res. Commun. 162: 1528–1534. doi:10.1016/0006-291x(89)90848-6. PMID 2669754.
External links
- Peptidyl-Asp metalloendopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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