3.4.11.B4: Pyrococcus horikoshii deblocking aminopeptidase
This is an abbreviated version, for detailed information about Pyrococcus horikoshii deblocking aminopeptidase, go to the full flat file.
The enzyme exhibits aminopeptidase activity and with lower efficiency deblocking activity (i.e. hydrolysis of acetylated amino acids from the N-terminus of peptides). The turnover number with Ac-Ala-Ala-Ala is 260-540fold lower compared to the activity with Ala-Ala-Ala. The turnover number with Ac-Ala-Ala is 350fold lower compared to the activity with Ala-Ala. Low hydrolytic activity for peptide substrates longer than 10 residues. The enzyme is activated by Co2+ or Zn2+. Contains 1.32 mol of Ca2+ per mol of monomer. =
DAP1, DAP2, DAP3, DAPPh, DAPPh2, DAPPh3, deblocking aminopeptidase, PH0519, PH1527, PH1821