Abstract
Peptidases are grouped according to their mechanism of catalysis in serine-type, cysteine-type, aspartic-type and metallo-type peptidases. Amongst these groups, the metallopeptidases represent the most diverse group, comprising 25 different families (1,2). Most of the Zn-binding metallopeptidases, named zincins, have the HEXXH motif for Zn-binding. Some other Zn-binding motifs have been defined, as there are the HXXEH, the HXXE, and the HXH motif (3). X-prolyl aminopeptidase (aminopeptidase P, EC 3.4.11.9), is an aminopeptidase that has been reported to bind zinc, and is activated by manganese ions, but does not contain any of these Zn-binding motifs. Aminopeptidase P from Escherichia coli was classified in the peptidase family M24, a family of metallopeptidases in which the ligands for metal ion binding are predominantly carboxylic acids (2). Apart from E. coli aminopeptidase P, this family comprises E. coli methionyl aminopeptidase (EC 3.4.11.18) and E. coli and human proline dipeptidase (EC 3.4.13.9). We have been studying the soluble form of aminopeptidase P in human lymphocytes and platelets (4,5), and were interested in determining the nucleotide sequence that would provide useful information for the development of potent and specific inhibitors. Aminopeptidase P is a proline-specific metallo-aminopeptidase that catalyses specifically the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Due to its specificity towards proline, it has been suggested that aminopeptidase P is important
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References
Rawlings, N.D., Barrett, A.J. Evolutionary families of peptidases. Biochem J. 290, 205–218 (1993)
Rawlings, N.D., Barrett, A.J. Evolutionary families of metallopeptidases. In: Methods in Enzymology 248. 183–210 (1995)
Hooper, N.M. Families of zinc metalloproteases. FEBS Letters, 354, 1 -f, 11994)
Hendriks, D., De Meester, I., Umiel, T., Vanhoof, G., van Sande, M., Scharpé, S., Yaron, A. Aminopeptidase P and dipeptidyl peptidase IV activity in human leukocytes and in stimulated lymphocytes. Clinica Chimica Acta, 196, 87–96 (1991)
Vanhoof, G., De Meester, I., Goossens, F., Hendriks, D., Scharpé, S., Yaron, A. Kininase activity in human platelets: cleavage of the Argo-Pro’ bond of bradykinin by aminopeptidase P. Biochem Pharmacol 44. 479–487 (1992b)
Vanhoof, G., Goossens, F., De Meester, I., Hendriks, D., Scharpé, S. Proline motifs in peptides and their biological processing. FASEB J 9, 736–744 (1995)
Yaron, A., and Naider, F. Proline dependent structural and biological properties of peptides and proteins. Crit Rev Biochen, Molec Biol 28, 31–81 (1993)
Kitamura, S., Carbini, L.A., Carretero, O.A., Simmons, W.H., Seicli, A.G. Potentiation by aminopeptidase P of blood pressure response to bradykinin. Brit J Pharmacol 114, 6–7 (1995)
Yoshimoto, T., Tone, H., Honda, T., Osatomi, K., Kobayashi. R., Tsuru, D. Sequencing and high expression of aminopeptidase P gene from Escherichia coil HB 101. J Biochem (Tokyo) 105, 412–416 (1989)
Butler, M.J., Aphale, J.S., DiZonno, M.A., Krygsman, P., Walczyk, E., Malek, L.T.: Intracellular aminopeptidases in Streptomyces lividans 66. J Ind Microbiol 13, 24–29 (1994)
Fleischmann, R.D., Adams, M.D., White, O., Clayton, R.A., Kirkness, E.F., Kerlavage, A.R., Bult, C..I., et al. Whole-genome random sequencing and assembly of Haemophilus in/luen_ae RD. Science 269, 496–512 (1995)
Fraser, M.C., Gocayne, J.D., White, O., Adams, M.D., Clayton, R.A., Fleischmann, R.D., Bult, C.J. et al. The minimal gene complement of Mvcoplasma genitalium. Science 270, 397–403 (1995)
Vergas Romero, C., Neudorfer, I., Mann, K., Schäfer, W. Purification and amino acid sequence of aminopeptidase P from pig kidney. Eur J Biochem 279, 262–269 (1995)
Hyde, R.J., Hooper, N.M., Turner, A.J. Molecular cloning and expression in COS-cells of pig kidney aminopeptidase P. Biochem. J. 319, 197–201 (1996)
Altschul, S.F., Gisch, W., Miller, W., Myers, E.W., and Lipman, D.J. Basic local alignment search tool. J Mol Biol 215, 403–410 (1990)
Rost, B., and Sander, C. Improved prediction of protein secondary structure by use of sequence profiles and neural networks, Proc Natl Acad Sei, USA 90, 7758–7762 (1993)
Bazan, J.F., Weaver, L.H., Roderick, S.L., Huber, R., Matthews, B.W. Sequencee and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. Proc Natl Acad Sei, USA 91, 2473–2477 (1994)
Li, X., Chang, Y.H. Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67). Biochim Biophys Acta, 1260, 333–336 (1995)
LI, X., Chang, Y.H. Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase. Biochem. Biophys. Res. Comm. 227, 157–159 (1996)
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Vanhoof, G. et al. (1997). Human Lymphocyte X-Prolyl Aminopeptidase (Aminopeptidase P)-Like Protein. In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_4
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_4
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