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 3.4.13.18     
Accepted name: cytosol nonspecific dipeptidase
Reaction: Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids
Other name(s): N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipeptidase; prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase; glycyl-L-leucine hydrolase; glycyl-glycine dipeptidase
Comments: A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-31-4
References:
1.  Bauer, K. Cytosol non-specific dipeptidase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1520–1522.
[EC 3.4.13.18 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.18, modified 2000 (EC 3.4.13.15 created 1989, incorporated 1992)]
 
 
EC 3.4.13.19     
Accepted name: membrane dipeptidase
Reaction: Hydrolysis of dipeptides
Other name(s): renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP
Comments: A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-99-6
References:
1.  Campbell, B., Lin, H., Davis, R. and Ballew, E. The purification and properties of a particulate renal dipeptidase. Biochim. Biophys. Acta 118 (1966) 371–386. [PMID: 5961612]
2.  Campbell, B.J. Renal dipeptidase. Methods Enzymol. 19 (1970) 722–729.
3.  Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M. Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I. Antimicrob. Agents Chemother. 22 (1982) 62–70. [PMID: 7125632]
4.  Hooper, N.M., Keen, J.N. and Turner, A.J. Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. Biochem. J. 265 (1990) 429–433. [PMID: 2137335]
[EC 3.4.13.19 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.19, modified 2011]
 
 
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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