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Gene Review

ANPEP  -  alanyl (membrane) aminopeptidase

Bos taurus

Synonyms: APN, CD13, P150
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Disease relevance of ANPEP


High impact information on ANPEP

  • From reversed-phase high-performance liquid chromatography tryptic mapping, leucyl aminopeptidase M digestion, and microsequence analysis, it is clear that diiodination of the tyrosine residues is not favored for the beta-subunit with the exception of beta-Tyr-7, whereas diiodination was observed with alpha-Tyr-21 and alpha-Tyr-92/93 [3].
  • Digestion of this peptide with aminopeptidase M and carboxypeptidase B yielded a tetrapeptide (residues 6 through 9) [4].
  • Aromatic and aliphatic substituents placed at this position strongly interact with the LAP S1' binding pocket, while a significant increase in binding affinity toward APN was observed for compounds containing aromatic versus leucine side chains at the P1' position [5].
  • A role for aminopeptidase N in Na(+)-dependent amino acid transport in bovine renal brush-border membranes [6].
  • On the basis of its N-terminal amino acid sequence, the 120-kDa biotin-containing protein is totally distinct from the 120-kDa aminopeptidase N reported to be a receptor for Cry1Ac toxin [7].

Biological context of ANPEP

  • PsA inhibited the APN activity with an IC50 of 18 microM in a non-competitive manner [8].
  • The oligopeptides produced in the tryptic digest before and after aminopeptidase N treatment were identified by analysis of the N- and C-terminal amino acid sequences and amino acid compositions of the isolated peptides and by on-line liquid chromatography-mass spectrometry [2].
  • Incubation of purified peptides with aminopeptidase N resulted in complete hydrolysis of many peptides, while others were only partially hydrolyzed or not hydrolyzed [2].
  • The Arg-Phe-[3H]anilide:AmN reaction obeyed first-order enzyme kinetics when human serum, human seminal plasma, guinea pig serum, or homogeneous porcine kidney AmN was used as enzyme source and substrate was within the concentration range of 1-200 nM [9].
  • Gestational age x feeding interactions indicated increased activities of aminopeptidase N and reduced lactase activities only in F8 and reduced dipeptidylpeptidase IV activities only in P8 [10].

Anatomical context of ANPEP


Associations of ANPEP with chemical compounds

  • Compound 1 potently inhibited APN activity with a K(i) value of 3.5 microM [16].
  • Interestingly, the permeability coefficient of Met-Enk was increased 4-fold in the presence of specific inhibitors of APM and ACE [17].
  • The effect of specific inhibitors of APM, ACE and NEP on the permeability of [Met5]enkephalin (Met-Enk) and a conformationally constrained and enzymatically stable analog, DPDPE, also was determined [17].
  • We have confirmed that alleged substrates such as angiotensin III and Met-Lys- and Lys-bradykinin are bound by AmN with high affinities (Km values, 5.7, 9.1, and 14.3 microM) [9].
  • Purified milk proteins (alpha-lactalbumin, beta-lactoglobulin, and beta-casein) were hydrolyzed in 0.1 M Hepes buffer (pH 7.5) containing pronase E, aminopeptidase M, and prolidase at 37 degrees C for 20 h [18].

Other interactions of ANPEP


Analytical, diagnostic and therapeutic context of ANPEP

  • To determine optimal conditions for treatment of donor eyes before transplantation, activities of key proteases (aminopeptidase M, dipeptidylpeptidase II and IV and gamma-glutamyltranspeptidase) as indicators of RPE cell quality (viability and functional state) were measured [20].
  • Fractionation of the plasma membranes by centrifugation on a Percoll density gradient resulted in clear separation of the basolateral membranes (BLM) from the brush-border membranes (BBM), with Na+,K+-ATPase and aminopeptidase M as their respective marker enzymes [21].


  1. Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus. Benbacer, L., Kut, E., Besnardeau, L., Laude, H., Delmas, B. J. Virol. (1997) [Pubmed]
  2. Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2. Tan, P.S., van Kessel, T.A., van de Veerdonk, F.L., Zuurendonk, P.F., Bruins, A.P., Konings, W.N. Appl. Environ. Microbiol. (1993) [Pubmed]
  3. The iodination sites of bovine thyrotropin. Stanton, P.G., Hearn, M.T. J. Biol. Chem. (1987) [Pubmed]
  4. Vitamin K and the biosynthesis of prothrombin. V. Gamma-carboxyglutamic acids, the vitamin K-dependent structures in prothrombin. Fernlund, P., Stenflo, J., Roepstorff, P., Thomsen, J. J. Biol. Chem. (1975) [Pubmed]
  5. The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity. Grembecka, J., Mucha, A., Cierpicki, T., Kafarski, P. J. Med. Chem. (2003) [Pubmed]
  6. A role for aminopeptidase N in Na(+)-dependent amino acid transport in bovine renal brush-border membranes. Plakidou-Dymock, S., Tanner, M.J., McGivan, J.D. Biochem. J. (1993) [Pubmed]
  7. The Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins. Du, C., Nickerson, K.W. Appl. Environ. Microbiol. (1996) [Pubmed]
  8. Psammaplin A, a marine natural product, inhibits aminopeptidase N and suppresses angiogenesis in vitro. Shim, J.S., Lee, H.S., Shin, J., Kwon, H.J. Cancer Lett. (2004) [Pubmed]
  9. A radiochemical assay for aminopeptidase N. Ryan, J.W., Chung, A.Y., Nearing, J.A., Valido, F.A., Shun-Cun, C., Berryer, P. Anal. Biochem. (1993) [Pubmed]
  10. Preterm as compared with full-term neonatal calves are characterized by morphological and functional immaturity of the small intestine. Bittrich, S., Philipona, C., Hammon, H.M., Romé, V., Guilloteau, P., Blum, J.W. J. Dairy Sci. (2004) [Pubmed]
  11. Betulinic acid inhibits growth factor-induced in vitro angiogenesis via the modulation of mitochondrial function in endothelial cells. Kwon, H.J., Shim, J.S., Kim, J.H., Cho, H.Y., Yum, Y.N., Kim, S.H., Yu, J. Jpn. J. Cancer Res. (2002) [Pubmed]
  12. Amastatin interferes with the antagonist properties of MEN 10,208 in the rabbit pulmonary artery but not in the hamster trachea. Patacchini, R., Maggi, C.A. Eur. J. Pharmacol. (1993) [Pubmed]
  13. Intestinal development in neonatal calves: effects of glucocorticoids and dependence of colostrum feeding. Sauter, S.N., Roffler, B., Philipona, C., Morel, C., Romé, V., Guilloteau, P., Blum, J.W., Hammon, H.M. Biol. Neonate (2004) [Pubmed]
  14. Evaluation of the inhibition effect of thiolated poly(acrylates) on vaginal membrane bound aminopeptidase N and release of the model drug LH-RH. Valenta, C., Marschütz, M., Egyed, C., Bernkop-Schnürch, A. J. Pharm. Pharmacol. (2002) [Pubmed]
  15. Morphogenesis of the bovine rete testis: the intratesticular rete and its connection to the seminiferous tubules. Wrobel, K.H. Anat. Embryol. (2000) [Pubmed]
  16. N-hydroxy-2-(naphthalene-2-ylsulfanyl)-acetamide, a novel hydroxamic acid-based inhibitor of aminopeptidase N and its anti-angiogenic activity. Lee, J., Shim, J.S., Jung, S.A., Lee, S.T., Kwon, H.J. Bioorg. Med. Chem. Lett. (2005) [Pubmed]
  17. Effect of peptidases at the blood brain barrier on the permeability of enkephalin. Brownson, E.A., Abbruscato, T.J., Gillespie, T.J., Hruby, V.J., Davis, T.P. J. Pharmacol. Exp. Ther. (1994) [Pubmed]
  18. Quantification of glutamine in proteins and peptides using enzymatic hydrolysis and reverse-phase high-performance liquid chromatography. Tsao, M., Otter, D.E. Anal. Biochem. (1999) [Pubmed]
  19. Effect of secretory particles in bovine seminal vesicle secretion on sperm motility and acrosome reaction. Agrawal, Y., Vanha-Perttula, T. J. Reprod. Fertil. (1987) [Pubmed]
  20. Regional differences and post-mortem stability of enzymatic activities in the retinal pigment epithelium. Fröhlich, E., Klessen, C. Graefes Arch. Clin. Exp. Ophthalmol. (2003) [Pubmed]
  21. Analysis of the distribution of Na+/H+ exchanger isoforms among the plasma membrane subfractions of bovine kidney cortex: reevaluation of methods for fractionating the brush-border and the basolateral membranes. Yoshioka, S., Suzuki, T., Kawakita, M. J. Biochem. (1997) [Pubmed]
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