Wikipedia
X-Pro dipeptidase
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
| Xaa-Pro dipeptidase | |
|---|---|
Ochratoxinase oktamer, Aspergillus niger | |
| Identifiers | |
| EC no. | 3.4.13.9 |
| CAS no. | 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 |
- Hydrolysis of Xaa!Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs
This enzyme is Mn2+-activated.
References edit
- ^ Davis NC, Smith EL (January 1957). "Purification and some properties of prolidase of swine kidney". The Journal of Biological Chemistry. 224 (1): 261–75. PMID 13398404.
- ^ Sjöström H, Norén O, Josefsson L (December 1973). "Purification and specificity of pig intestinal prolidase". Biochimica et Biophysica Acta (BBA) - Enzymology. 327 (2): 457–70. doi:10.1016/0005-2744(73)90429-4. PMID 4778946.
- ^ Baksi K, Radhakrishnan AN (March 1974). "Purification and properties of prolidase (imidodipeptidase) from monkey small intestine". Indian Journal of Biochemistry & Biophysics. 11 (1): 7–11. PMID 4435812.
- ^ Browne P, O'Cuinn G (May 1983). "The purification and characterization of a proline dipeptidase from guinea pig brain". The Journal of Biological Chemistry. 258 (10): 6147–54. PMID 6853481.
External links edit
- Xaa-Pro+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)