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Gene Review

Rnpep  -  arginyl aminopeptidase (aminopeptidase B)

Rattus norvegicus

Synonyms: AP-B, Aminopeptidase B, Arginine aminopeptidase, Arginyl aminopeptidase, Cytosol aminopeptidase IV
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Disease relevance of Rnpep


High impact information on Rnpep


Biological context of Rnpep

  • From sequence-homology searches, Ap B is known to be closely related to leukotriene (LT)-A4 hydrolase (EC [6].
  • Aminopeptidase B (Ap B; EC is a zinc-binding protein that contains the consensus sequence HEXXHX18E (324-347), conserved among the M1 family of metallopeptidases [6].
  • OBJECTIVE: The aim of the present study was to elucidate the presence in rat cardiac fibroblastic cells of arginine-aminopeptidase and its involvement in the hydrolysis of angiotensin peptides [1].
  • These results are in agreement with the known substrate specificity of arginine aminopeptidase [7].
  • Previous investigations have suggested an important role for cationic residues in determination of toxin activity, and our single-site mutagenesis studies have indicated that isoform discrimination can be partially explained by the unique cationic residues Arg-12 and Lys-49 of anthopleurin B (ApB) [8].

Anatomical context of Rnpep


Associations of Rnpep with chemical compounds

  • Aminopeptidase B (EC is a Zn(2+)-dependent exopeptidase which selectively removes arginine and/or lysine residues from the NH2-terminus of several peptide substrates including Arg0-Leu-enkephalin, Arg0-Met-enkephalin and Arg-1-Lys0-somatostatin-14 [13].
  • Whereas the endoprotease cleaves a single peptide bond, between Glu12 and Arg13 of S-28, the aminopeptidase B-like enzyme removes both Arg13 and Lys14 stepwise from the NH2 terminus of the corresponding COOH-terminal fragment [14].
  • It is proposed that S-28 processing involves a divalent cation-sensitive endoprotease that is sensitive to thiol reagents, which cleaves before the Arg-Lys doublet, which is not trypsin-like, and whose action is coupled to an aminopeptidase B-like enzyme [14].
  • Inhibition of arginine aminopeptidase by bestatin and arphamenine analogues. Evidence for a new mode of binding to aminopeptidases [7].
  • CONCLUSIONS: Our data show that chloride-insensitive Arginine-aminopeptidase could contribute to the hydrolysis of all studied angiotensin peptides in concert with other peptidases present in fibroblasts [1].

Other interactions of Rnpep


Analytical, diagnostic and therapeutic context of Rnpep


  1. Arginine-aminopeptidase in rat cardiac fibroblastic cells participates in angiotensin peptide turnover. Petrov, V.V., Fagard, R.H., Lijnen, P.J. Cardiovasc. Res. (2004) [Pubmed]
  2. Inhibitors of aminopeptidase B suppress the development of hypertension in spontaneously hypertensive rats. Aoyagi, T., Wada, T., Kojima, F., Nagai, M., Harada, S., Hachisu, M., Murata, S., Umezawa, H. Chem. Pharm. Bull. (1986) [Pubmed]
  3. Expression and purification of rat recombinant aminopeptidase B secreted from baculovirus-infected insect cells. Cadel, S., Gouzy-Darmon, C., Petres, S., Piesse, C., Pham, V.L., Beinfeld, M.C., Cohen, P., Foulon, T. Protein Expr. Purif. (2004) [Pubmed]
  4. Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase. Cadel, S., Foulon, T., Viron, A., Balogh, A., Midol-Monnet, S., Noël, N., Cohen, P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Molecular cloning and expression of rat liver aminopeptidase B. Fukasawa, K.M., Fukasawa, K., Kanai, M., Fujii, S., Harada, M. J. Biol. Chem. (1996) [Pubmed]
  6. Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity. Fukasawa, K.M., Fukasawa, K., Harada, M., Hirose, J., Izumi, T., Shimizu, T. Biochem. J. (1999) [Pubmed]
  7. Inhibition of arginine aminopeptidase by bestatin and arphamenine analogues. Evidence for a new mode of binding to aminopeptidases. Harbeson, S.L., Rich, D.H. Biochemistry (1988) [Pubmed]
  8. Multiple cationic residues of anthopleurin B that determine high affinity and channel isoform discrimination. Khera, P.K., Benzinger, G.R., Lipkind, G., Drum, C.L., Hanck, D.A., Blumenthal, K.M. Biochemistry (1995) [Pubmed]
  9. Neurotensin and neuromedin N are differently metabolized in ventral tegmental area and nucleus accumbens. Checler, F., Dauch, P., Masuo, Y., Vincent, J.P. J. Neurochem. (1991) [Pubmed]
  10. Aminopeptidase B-like enzymes in leukocytes. Söderling, E., Knuttila, M., Mäkinen, K.K. FEBS Lett. (1977) [Pubmed]
  11. Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules. Cadel, S., Pierotti, A.R., Foulon, T., Créminon, C., Barré, N., Segrétain, D., Cohen, P. Mol. Cell. Endocrinol. (1995) [Pubmed]
  12. Influence of aminopeptidase inhibitors on brain angiotensin metabolism and drinking in rats. Wright, J.W., Quirk, W.S., Hanesworth, J.M., Harding, J.W. Brain Res. (1988) [Pubmed]
  13. Aminopeptidase B (EC Foulon, T., Cadel, S., Cohen, P. Int. J. Biochem. Cell Biol. (1999) [Pubmed]
  14. 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. Gluschankof, P., Gomez, S., Morel, A., Cohen, P. J. Biol. Chem. (1987) [Pubmed]
  15. Role of angiotensin converting enzyme and other peptidases in in vivo metabolism of kinins. Ishida, H., Scicli, A.G., Carretero, O.A. Hypertension (1989) [Pubmed]
  16. Purification and characterization of an enkephalin aminopeptidase from rat brain membranes. Hui, K.S., Wang, Y.J., Lajtha, A. Biochemistry (1983) [Pubmed]
  17. Acute doxorubicin (adriamycin) dosage does not reduce cardiac protein synthesis in vivo, but decreases diaminopeptidase I and proline endopeptidase activities. Zima, T., Tesar, V., Mantle, D., Koll, M., Patel, V., Richardson, P.J., Preedy, V.R. Exp. Mol. Pathol. (2001) [Pubmed]
  18. NRD convertase and aminopeptidase B: two processing metallopeptidases with a selectivity for basic residues. Foulon, T., Cadel, S., Prat, A., Chesneau, V., Hospital, V., Segrétain, D., Cohen, P. Ann. Endocrinol. (Paris) (1997) [Pubmed]
  19. Expression of aminopeptidase B in the developing and adult rat retina. Piesse, C., Cadel, S., Gouzy-Darmon, C., Jeanny, J.C., Carrière, V., Goidin, D., Jonet, L., Gourdji, D., Cohen, P., Foulon, T. Exp. Eye Res. (2004) [Pubmed]
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