IUBMB Enzyme Nomenclature


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 entries:
amastatin = Leu[1ψ2,CHOHCONH]ValValAsp
arphamenine A = Arg[1ψ2,COCH2]Phe
arphamenine B = Arg[1ψ2,COCH2]Tyr
bestatin = Phe[1ψ2,CHOHCONH]Leu

Other names: 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, leukotriene-A4 hydrolase [5,6]. Potently inhibited by arphamenine B, and also inhibited by chelating agents, N-ethylmaleimide, arphamenine A, amastatin and bestatin. A zinc metallopeptidase in family family M1 (membrane alanyl aminopeptidase family) [4,5].

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 9073-92-1


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 beta-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) 11269-112673. [PMID: 8157657]

[EC created 1972, modified 1997]

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