Dipeptidyl-peptidase II

Dipeptidyl-peptidase II (EC 3.4.14.2, dipeptidyl aminopeptidase II, dipeptidyl arylamidase II, carboxytripeptidase, dipeptidyl peptidase II, DAP II, dipeptidyl(amino)peptidase II, dipeptidylarylamidase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction:

Release of an N-terminal dipeptide, Xaa-Yaa!, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides
Dipeptidyl-peptidase II
Identifiers
EC no.3.4.14.2
CAS no.76199-23-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

This lysosomal serine-type peptidase is maximally active at acidic pH.

References

  1. McDonald JK, Leibach FH, Grindeland RE, Ellis S (August 1968). "Purification of dipeptidyl aminopeptidase II (dipeptidyl arylamidase II) of the anterior pituitary gland. Peptidase and dipeptide esterase activities". The Journal of Biological Chemistry. 243 (15): 4143–50. doi:10.1016/S0021-9258(18)93291-6. PMID 4969969.
  2. McDonald JK, Schwabe C (1977). "Intracellular exopeptidases". In Barrett AJ (ed.). Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.