X-Pro dipeptidase

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
Search PMC articles PubMed articles NCBI proteins

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

1. Davis NC, Smith EL (January 1957). "Purification and some properties of prolidase of swine kidney". The Journal of Biological Chemistry. 224 (1): 261–75. doi: 10.1016/S0021-9258(18)65027-6 . PMID   13398404.
2. 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.
3. 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.
4. 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. doi: 10.1016/S0021-9258(18)32385-8 . PMID   6853481.

External links

• Xaa-Pro+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)