X-Pro dipeptidase
| Xaa-Pro dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
Ochratoxinase oktamer, Aspergillus niger | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.13.9 | ||||||||
| CAS number | 9025-32-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Xaa-Pro dipeptidase (EC 3.4.13.9, prolidase, imidodipeptidase, proline dipeptidase, peptidase D, gamma-peptidase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of Xaa!Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs
This enzyme is Mn2+-activated.
References
- ↑ Davis, N.C.; Smith, E.L. (1957). "Purification and some properties of prolidase of swine kidney". J. Biol. Chem. 224: 261–275. PMID 13398404.
- ↑ Sjöström, H.; Norén O.; Josefsson, L. (1973). "Purification and specificity of pig intestinal prolidase". Biochim. Biophys. Acta. 327: 457–470. doi:10.1016/0005-2744(73)90429-4. PMID 4778946.
- ↑ Baksi, K.; Radhakrishnan, A.N. (1974). "Purification and properties of prolidase (imidodipeptidase) from monkey small intestine". Indian J. Biochem. Biophys. 11: 7–11. PMID 4435812.
- ↑ Browne, P.; O'Cuinn, G. (1983). "The purification and characterization of a proline dipeptidase from guinea pig brain". J. Biol. Chem. 258: 6147–6154. PMID 6853481.
External links
- Xaa-Pro dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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