| Dipeptidyl-peptidase II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.14.2 | ||||||||
| CAS no. | 76199-23-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
This lysosomal serine-type peptidase is maximally active at acidic pH.
References
- ^ 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.
- ^ 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.
External links
- Dipeptidyl-peptidase+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
| Dipeptidyl-peptidase II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.14.2 | ||||||||
| CAS no. | 76199-23-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
This lysosomal serine-type peptidase is maximally active at acidic pH.
References
- ^ 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.
- ^ 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.
External links
- Dipeptidyl-peptidase+II at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
|
| This enzyme-related article is a stub. You can help Wikipedia by expanding it. |