Biology:Xaa-Pro aminopeptidase
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Short description: Class of enzymes
| Xaa-Pro aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.9 | ||||||||
| CAS number | 37288-66-7 | ||||||||
| 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 aminopeptidase (EC 3.4.11.9, X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, aminoacylproline aminopeptidase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide
This enzyme is Mn2+-dependent.
References
- ↑ "Aminopeptidase-P". Biochemical and Biophysical Research Communications 32 (4): 658–63. August 1968. doi:10.1016/0006-291x(68)90289-1. PMID 4878817.
- ↑ Yaron, A.; Berger, A. (1970). "Aminopeptidase-P". Methods Enzymol. 19: 522–534. doi:10.1016/0076-6879(70)19039-2.
- ↑ "Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung". European Journal of Biochemistry 125 (3): 609–15. July 1982. doi:10.1111/j.1432-1033.1982.tb06726.x. PMID 6749499.
- ↑ "Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation". Molecular and Cellular Biochemistry 75 (2): 123–32. June 1987. doi:10.1007/bf00229900. PMID 3627107.
- ↑ "Purification and characterization of pig kidney aminopeptidase P. A glycosyl-phosphatidylinositol-anchored ectoenzyme". The Biochemical Journal 267 (2): 509–15. April 1990. doi:10.1042/bj2670509. PMID 2139778.
External links
- Xaa-Pro+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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