The Enzyme Database

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EC 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9073-92-1
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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]
 
 
EC 3.4.11.7     
Accepted name: glutamyl aminopeptidase
Reaction: Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide
Other name(s): aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2
Comments: Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9074-83-3
References:
1.  Glenner, G.G., McMillan, P.J. and Folk, J.E. A mammalian peptidase specific for the hydrolysis of N-terminal α-L-glutamyl and aspartyl residues. Nature 194 (1962) 867. [PMID: 13899213]
2.  Chulkova, T.M. and Orekhovich, V.N. Isolation and properties of aminopeptidase A from bovine kidneys. Biokhimiya 43 (1978) 964–969. [PMID: 508862]
3.  Danielsen, E.M., Norén, O., Sjöström, H., Ingram, J. and Kenny, J. Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Biochem. J. 189 (1980) 591–603. [PMID: 7011318]
4.  Tobe, H., Kojima, F., Aoyagi, T. and Umezawa, H. Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney. Biochim. Biophys. Acta 613 (1980) 459–468. [DOI] [PMID: 7448199]
5.  Wu, Q., Lahti, J.M., Air, G.M., Burrows, P.D. and Cooper, M.D. Molecular cloning of the murine BP-1/6C3 antigen: a member of the zinc-dependent metallopeptidase family. Proc. Natl. Acad. Sci. USA 87 (1990) 993–997. [DOI] [PMID: 1689065]
[EC 3.4.11.7 created 1972]
 
 
EC 3.4.24.61     
Accepted name: nardilysin
Reaction: Hydrolysis of polypeptides, preferably at -Xaa┼Arg-Lys-, and less commonly at -Arg┼Arg-Xaa-, in which Xaa is not Arg or Lys
Other name(s): N-arginine dibasic convertase; NRD-convertase
Comments: Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 292850-69-2
References:
1.  Gomez, S., Gluschankof, P., Morel, A. and Cohen, P. The somatostatin-28 convertase of rat brain cortex is associated with secretory granule membranes. J. Biol. Chem. 260 (1985) 10541–10545. [PMID: 3897221]
2.  Gluschankof, P., Gomez, S., Morel, A. and Cohen, P. Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex. J. Biol. Chem. 262 (1987) 9615–9620. [PMID: 2885328]
3.  Chesneau, V., Pierotti, A.R., Barré, N., Créminon, C., Tougard, C. and Cohen, P. Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues. J. Biol. Chem. 269 (1994) 2056–2061. [PMID: 8294457]
4.  Pierotti, A.R., Prat, A., Chesneau, V., Gaudoux, F., Leseney, A.-M., Foulon, T. and Cohen, P. N-Arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes. Proc. Natl. Acad. Sci. USA 91 (1994) 6078–6082. [DOI] [PMID: 8016118]
[EC 3.4.24.61 created 1995]
 
 


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