Biology:X-Pro dipeptidase
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Xaa-Pro dipeptidase | |||||||||
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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 | ||||||||
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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
- ↑ "Purification and some properties of prolidase of swine kidney". The Journal of Biological Chemistry 224 (1): 261–75. January 1957. PMID 13398404.
- ↑ "Purification and specificity of pig intestinal prolidase". Biochimica et Biophysica Acta (BBA) - Enzymology 327 (2): 457–70. December 1973. doi:10.1016/0005-2744(73)90429-4. PMID 4778946.
- ↑ "Purification and properties of prolidase (imidodipeptidase) from monkey small intestine". Indian Journal of Biochemistry & Biophysics 11 (1): 7–11. March 1974. PMID 4435812.
- ↑ "The purification and characterization of a proline dipeptidase from guinea pig brain". The Journal of Biological Chemistry 258 (10): 6147–54. May 1983. PMID 6853481.
External links
- Xaa-Pro+dipeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/X-Pro dipeptidase.
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