ExplorEnz: Search Results

3.4.11.6

Accepted name:

aminopeptidase B

Reaction:

Release of N-terminal Arg and Lys from oligopeptides when P1′ is not Pro. Also acts on arylamides of Arg and Lys

Glossary:

amastatin = Leu[1Ψ2,CHOHCONH]ValValAsp
arphamenine A = Arg[1Ψ2,COCH₂]Phe
arphamenine B = Arg[1Ψ2,COCH₂]Tyr
bestatin = Phe[1Ψ2,CHOHCONH]Leu

Other name(s):

arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl^--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase

Comments:

Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family) [4,5].

References:

1.	Gainer, H., Russell, J.T. and Loh, Y.P. An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from β-lipotropin(60-65). FEBS Lett. 175 (1984) 135–139. [PMID: 6434344]
2.	Belhacène, N., Mari, B., Rossi, B. and Auberger, P. Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation. Eur. J. Immunol. 23 (1993) 1948–1955. [PMID: 8344358]
3.	Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D. and Cohen, P. Aminopeptidase-B in the rat testes: Isolation, functional properties and cellular localization in the seminiferous tubules. Mol. Cell. Endocrinol. 110 (1995) 149–160. [PMID: 7672445]
4.	Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S. and Harada, M. Molecular cloning and expression of rat liver aminopeptidase B. J. Biol. Chem. 271 (1996) 30731–30735. [PMID: 8940051]
5.	Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noel, N. and Cohen, P. Aminopeptidase B from the rat testis is a bifunctional enzyme structually related to leukotriene-A₄ hydrolase. Proc. Natl. Acad. Sci. USA 94 (1997) 2963–2968. [PMID: 9096329]
6.	Orning, L., Gierse, J.K. and Fitzpatrick, F.A. The bifunctional enzyme leukotriene-A₄ hydrolase is an arginine aminopeptidase of high efficiency and specificity. J. Biol. Chem. 269 (1994) 11269. [PMID: 8157657]

[EC 3.4.11.6 created 1972, modified 1997]