Aminopeptidase B
| Aminopeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.6 | ||||||||
| CAS no. | 9073-92-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Aminopeptidase B (EC 3.4.11.6, arylamidase II, arginine aminopeptidase, arginyl aminopeptidase, Cl—activated arginine aminopeptidase, cytosol aminopeptidase IV, L-arginine aminopeptidase) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
This enzyme from mammalian tissues is activated by chloride ions and low concentrations of thiol compounds.
An inhibitor is bestatin (ubenimex).
References
- ^ Gainer, H., Russell, J.T. and Loh, Y.P. (1984). "An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from β-lipotropin(60-65)". FEBS Lett. 175 (1): 135–139. doi:10.1016/0014-5793(84)80586-4. PMID 6434344.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Belhacène, N., Mari, B., Rossi, B. and Auberger, P. (1993). "Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation". Eur. J. Immunol. 23: 1948–1955. doi:10.1002/eji.1830230833. PMID 8344358.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D. and Cohen, P. (1995). "Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules". Mol. Cell. Endocrinol. 110 (1–2): 149–160. doi:10.1016/0303-7207(95)03529-g. PMID 7672445.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S. and Harada, M. (1996). "Molecular cloning and expression of rat liver aminopeptidase B". J. Biol. Chem. 271 (48): 30731–30735. doi:10.1074/jbc.271.48.30731. PMID 8940051.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N. and Cohen, P. (1997). "Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase". Proc. Natl. Acad. Sci. USA. 94 (7): 2963–2968. doi:10.1073/pnas.94.7.2963. PMID 9096329.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Orning, L., Gierse, J.K. and Fitzpatrick, F.A. (1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity". J. Biol. Chem. 269 (15): 11269–11267. PMID 8157657.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Aminopeptidase+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)