Biology:Oligopeptidase A
From HandWiki
| Oligopeptidase A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.70 | ||||||||
| CAS number | 394250-11-4 | ||||||||
| 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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Oligopeptidase A (EC 3.4.24.70, 68000-M signalpeptide hydrolase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
This enzyme is known from Escherichia coli and Salmonella typhimurium.
References
- ↑ "Degradation of a signal peptide by protease IV and oligopeptidase A". Journal of Bacteriology 170 (11): 5067–75. November 1988. doi:10.1128/jb.170.11.5067-5075.1988. PMID 3053642.
- ↑ "Oligopeptidase A is required for normal phage P22 development". Journal of Bacteriology 174 (18): 5869–80. September 1992. doi:10.1128/jb.174.18.5869-5880.1992. PMID 1522065.
- ↑ "Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene". Journal of Bacteriology 174 (18): 5881–7. September 1992. doi:10.1128/jb.174.18.5881-5887.1992. PMID 1325967.
- ↑ Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium. Methods in Enzymology. 248. 1995. pp. 567–79. doi:10.1016/0076-6879(95)48036-6.
External links
- Oligopeptidase+A at the US National Library of Medicine Medical Subject Headings (MeSH)
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