Oligopeptidase A

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Oligopeptidase A
Identifiers
EC no.3.4.24.70
CAS no.394250-11-4
Databases
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BRENDABRENDA entry
ExPASyNiceZyme view
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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

  1. ^ Novak P, Dev IK (November 1988). "Degradation of a signal peptide by protease IV and oligopeptidase A". Journal of Bacteriology. 170 (11): 5067–75. doi:10.1128/jb.170.11.5067-5075.1988. PMC 211572. PMID 3053642.
  2. ^ Conlin CA, Vimr ER, Miller CG (September 1992). "Oligopeptidase A is required for normal phage P22 development". Journal of Bacteriology. 174 (18): 5869–80. doi:10.1128/jb.174.18.5869-5880.1992. PMC 207121. PMID 1522065.
  3. ^ Conlin CA, Trun NJ, Silhavy TJ, Miller CG (September 1992). "Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene". Journal of Bacteriology. 174 (18): 5881–7. doi:10.1128/jb.174.18.5881-5887.1992. PMC 207123. PMID 1325967.
  4. ^ Conlin CA, Miller CG (1995). Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium. Methods in Enzymology. Vol. 248. pp. 567–79. doi:10.1016/0076-6879(95)48036-6. PMID 7674945.

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