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.
Word Map on EC 3.4.11.B4
-
3.4.11.B4
-
hyperthermophilic
-
archaeon
-
furiosus
-
thermococcus
-
cobalt
-
leu-pna
-
tetrahedral
-
aminopeptidases
-
onnurineus
-
exoprotease
-
dodecameric
-
oligomer
- 3.4.11.B4
-
hyperthermophilic
- archaeon
- furiosus
-
thermococcus
- cobalt
-
leu-pna
-
tetrahedral
- aminopeptidases
- onnurineus
-
exoprotease
-
dodecameric
- oligomer
Reaction
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. =
Synonyms
DAP1, DAP2, DAP3, DAPPh, DAPPh2, DAPPh3, deblocking aminopeptidase, PH0519, PH1527, PH1821