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Gene Review

ENPEP  -  glutamyl aminopeptidase (aminopeptidase A)

Sus scrofa

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High impact information on ENPEP

  • Immunopurification of sucrase-isomaltase, maltase-glucoamylase, aminopeptidase N and aminopeptidase A showed that these microvillar enzymes become sulfated [1].
  • An acute exploration of aminopeptidase A active site was performed by a combinatorial approach using (3-amino-2-mercapto-acyl)dipeptides able to fit its S(1), S(1)', and S(2)' subsites [2].
  • Hence, this compound is the first selective APA inhibitor reported, and as such, it should be an interesting probe to explore the physiological involvement of APA in the metabolism of neuropeptides like angiotensin II and CCK8 [3].
  • The effect of monensin and colchicine on the biogenesis of aminopeptidase N (EC, aminopeptidase A (EC, dipeptidyl peptidase IV (EC, sucrase (EC (EC and maltase-glucoamylase (EC was studied in organ-cultured pig small-intestinal explants [4].
  • The fact that the enzymes before reaching the microvillar membrane were found in a Ca2+-precipitated membrane fraction (intracellular and basolateral membranes), but not in soluble form, indicates that during biogenesis maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV are transported and assembled in a membrane-bound state [5].

Biological context of ENPEP

  • Screening of a rat genomic library with a partial rat APA cDNA resulted in isolation of a 12-kb clone found to contain the first exon and >3 kb of 5'-flanking sequence [6].
  • Aminopeptidase-A (APA) has a widespread tissue distribution consistent with a role in the metabolism of circulating or locally produced ANG II or CCK-8 [6].

Anatomical context of ENPEP


Associations of ENPEP with chemical compounds


Other interactions of ENPEP


  1. Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. Danielsen, E.M. EMBO J. (1987) [Pubmed]
  2. Investigation of subsite preferences in aminopeptidase A (EC led to the design of the first highly potent and selective inhibitors of this enzyme. David, C., Bischoff, L., Meudal, H., Mothé, A., De Mota, N., DaNascimento, S., Llorens-Cortes, C., Fournié-Zaluski, M.C., Roques, B.P. J. Med. Chem. (1999) [Pubmed]
  3. Differential inhibition of aminopeptidase A and aminopeptidase N by new beta-amino thiols. Chauvel, E.N., Llorens-Cortès, C., Coric, P., Wilk, S., Roques, B.P., Fournié-Zaluski, M.C. J. Med. Chem. (1994) [Pubmed]
  4. Biosynthesis of intestinal microvillar proteins. Role of the Golgi complex and microtubules. Danielsen, E.M., Cowell, G.M., Poulsen, S.S. Biochem. J. (1983) [Pubmed]
  5. Biosynthesis of intestinal microvillar proteins. Pulse-chase labelling studies on maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV. Danielsen, E.M., Sjöström, H., Norén, O. Biochem. J. (1983) [Pubmed]
  6. Aminopeptidase-A. II. Genomic cloning and characterization of the rat promoter. Jiang, Q., Troyanovskaya, M., Jayaraman, G., Healy, D.P. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2000) [Pubmed]
  7. Proteins of the kidney microvillar membrane. Aspartate aminopeptidase: purification by immunoadsorbent chromatography and properties of the detergent- and proteinase-solubilized forms. Danielsen, E.M., Norén, O., Sjöström, H., Ingram, J., Kenny, A.J. Biochem. J. (1980) [Pubmed]
  8. Angiotensin metabolism by cerebral microvascular aminopeptidase A. Bausback, H.H., Churchill, L., Ward, P.E. Biochem. Pharmacol. (1988) [Pubmed]
  9. Purification and characterization of an aminopeptidase A from hog intestinal brush-border membrane. Benajiba, A., Maroux, S. Eur. J. Biochem. (1980) [Pubmed]
  10. Histochemistry of some proteases in the normal rabbit, pig and ox corneas. Cejková, J., Lojda, Z. Histochemistry (1986) [Pubmed]
  11. Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression. Danielsen, E.M., Cowell, G.M. Biochem. J. (1986) [Pubmed]
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