Aminopeptidase B

Aminopeptidase B
Identifiers
EC number 3.4.11.6
CAS number 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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.

External links

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