J. L. Balwierczak, P. J. Kukkola, P. Savage, and A. Y. Jeng, Effects of metalloprotease inhibitors on smooth muscle endothelindashconverting enzyme activity, Biochemical Pharmacology, vol.49, issue.3, pp.291-296, 1995.
DOI : 10.1016/0006-2952(94)00508-J

A. Beaumont, M. J. O-'donohue, N. Paredes, N. Rousselet, M. Assicot et al., The Role of Histidine 231 in Thermolysin-like Enzymes.: A SITE-DIRECTED MUTAGENESIS STUDY, Journal of Biological Chemistry, vol.270, issue.28, pp.16803-16808, 1995.
DOI : 10.1074/jbc.270.28.16803

T. Benchetrit, M. C. Fournié-zaluski, and B. P. Roques, Relationship between the inhibitory potencies of thiorphan and retrothiorphan enantiomers on thermolysin and neutral endopeptidase 24.11 and their interactions with the thermolysin active site by computer modelling, Biochemical and Biophysical Research Communications, vol.147, issue.3, pp.1034-1040, 1987.
DOI : 10.1016/S0006-291X(87)80174-2

T. Benchetrit, V. Bissery, J. P. Mornon, A. Devault, P. Crine et al., Primary structure homologies between two zinc metallopeptidases, the neutral endopeptidase 24.11 ("enkephalinase") and thermolysin, through clustering analysis, Biochemistry, vol.27, issue.2, pp.592-596, 1988.
DOI : 10.1021/bi00402a014

S. Bron, In Modern microbiological methods series Molecular biological methods for, 1990.

N. Dion, L. Moual, H. Crine, P. Boileau, and G. , Kinetic evidence that His-711 of neutral endopeptidase 24.11 is involved in stabilization of the transition state, FEBS Letters, vol.2, issue.3, pp.301-304, 1993.
DOI : 10.1016/0014-5793(93)80533-Z

N. Dion, L. Moual, H. Fournié-zaluski, M. C. Roques, B. P. Crine et al., ??? residue of substrates and inhibitors, Biochemical Journal, vol.311, issue.2, pp.623-627, 1995.
DOI : 10.1042/bj3110623

V. G. Eijsink, G. Vriend, B. Van-der-burg, G. Venema, and B. K. Stulp, neutral protease, "Protein Engineering, Design and Selection", vol.4, issue.1, pp.99-104, 1990.
DOI : 10.1093/protein/4.1.99

N. Emoto and M. Yanagisawa, Endothelin-converting Enzyme-2 Is a Membrane-bound, Phosphoramidon-sensitive Metalloprotease with Acidic pH Optimum, Journal of Biological Chemistry, vol.270, issue.25, pp.15262-15268, 1995.
DOI : 10.1074/jbc.270.25.15262

M. C. Fournié-zaluski, E. Lucas, J. Devin, and B. P. Roques, Proton NMR configurational correlation for retro-inverso dipeptides: application to the determination of the absolute configuration of "enkephalinase" inhibitors. Relationships between stereochemistry and enzyme recognition, Journal of Medicinal Chemistry, vol.29, issue.5, pp.751-757, 1986.
DOI : 10.1021/jm00155a027

I. S. Fulcher, R. Matsas, A. J. Turner, and A. J. Kenny, Kidney neutral endopeptidase and the hydrolysis of enkephalin by synaptic membranes show similar sensitivity to inhibitors, Biochemical Journal, vol.203, issue.2, pp.519-522, 1982.
DOI : 10.1042/bj2030519

M. A. Holmes and B. W. Matthews, Structure of thermolysin refined at 1.6 ?? resolution, Journal of Molecular Biology, vol.160, issue.4, pp.623-639, 1982.
DOI : 10.1016/0022-2836(82)90319-9

M. Izquierdo-martin and R. L. Stein, Mechanistic studies on the inhibition of thermolysin by a peptide hydroxamic acid, Journal of the American Chemical Society, vol.114, issue.1, pp.325-331, 1992.
DOI : 10.1021/ja00027a042

Y. A. Kim, B. Shriver, and L. B. Hersh, Mutational analysis reveals only one catalytic histidine in neutral endopeptidase (???enkephalinase???), Biochemical and Biophysical Research Communications, vol.184, issue.2, pp.883-887, 1992.
DOI : 10.1016/0006-291X(92)90673-9

S. Kunugi, H. Hirohara, and N. Ise, pH and Temperature Dependences of Thermolysin Catalysis. Catalytic Role of Zinc-Coordinated Water, European Journal of Biochemistry, vol.267, issue.1, pp.157-163, 1982.
DOI : 10.1016/0006-291X(69)90739-6

L. Moual, H. Dion, N. Roques, B. P. Crine, P. Boileau et al., Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11, European Journal of Biochemistry, vol.158, issue.1, pp.475-480, 1994.
DOI : 10.1038/351761a0

S. Lee, E. D. Zambas, W. L. Marsh, and C. M. Redman, Molecular cloning and primary structure of Kell blood group protein., Proceedings of the National Academy of Sciences, vol.88, issue.14, pp.6353-6357, 1991.
DOI : 10.1073/pnas.88.14.6353

M. Letarte, S. Vera, R. Tran, J. B. Addis, R. J. Onizuka et al., Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase, Journal of Experimental Medicine, vol.168, issue.4, pp.1247-1253, 1988.
DOI : 10.1084/jem.168.4.1247
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189092/pdf

W. Lian, D. Wu, W. N. Konings, I. Mierau, and L. B. Hersh, Heterologous Expression and Characterization of RecombinantLactococcus lactisNeutral Endopeptidase (Neprilysin), Archives of Biochemistry and Biophysics, vol.333, issue.1, pp.121-126, 1996.
DOI : 10.1006/abbi.1996.0372

C. Llorens, B. Malfroy, J. C. Schwartz, G. Gacel, B. P. Roques et al., Enkephalin Dipeptidyl Carboxypeptidase (Enkephalinase) Activity: Selective Radioassay, Properties, and Regional Distribution in Human Brain, Journal of Neurochemistry, vol.19, issue.4, pp.1081-1089, 1982.
DOI : 10.1016/0014-5793(79)80148-9

T. Maniatis, E. F. Fritsch, and F. Sambrook, in Molecular cloning: a laboratory manual, 1989.

B. W. Matthews, Structural basis of the action of thermolysin and related zinc peptidases, Accounts of Chemical Research, vol.21, issue.9, pp.333-340, 1988.
DOI : 10.1021/ar00153a003

K. Mciver, E. Kessler, and D. E. Ohman, Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase., Journal of Bacteriology, vol.173, issue.24, pp.7781-7789, 1991.
DOI : 10.1128/jb.173.24.7781-7789.1991

I. Mierau, P. S. Tan, A. J. Haandrikman, J. Kok, K. J. Leenhouts et al., Cloning and sequencing of the gene for a lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase., Journal of Bacteriology, vol.175, issue.7, pp.2087-2096, 1993.
DOI : 10.1128/jb.175.7.2087-2096.1993

W. L. Mock and M. Aksamawti, Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysis, Biochemical Journal, vol.302, issue.1, pp.57-68, 1994.
DOI : 10.1042/bj3020057

O. Donohue, M. J. Roques, B. P. Beaumont, and A. , Rokko coding for the thermostable metalloprotease thermolysin, Biochemical Journal, vol.300, issue.2, pp.599-603, 1994.
DOI : 10.1042/bj3000599

N. D. Rawlings and A. J. Barrett, [13] Evolutionary families of metallopeptidases, Methods Enzymol, vol.248, pp.183-228, 1995.
DOI : 10.1016/0076-6879(95)48015-3

S. L. Roderick, M. C. Fournié-zaluski, B. P. Roques, and B. W. Matthews, Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin, Biochemistry, vol.28, issue.4, pp.1493-1497
DOI : 10.1021/bi00430a011

B. P. Roques and A. Beaumont, Neutral endopeptidase-24.11 inhibitors: from analgesics to antihypertensives?, Trends in Pharmacological Sciences, vol.11, issue.6, pp.245-249, 1990.
DOI : 10.1016/0165-6147(90)90252-4
URL : https://hal.archives-ouvertes.fr/hal-00314275

B. P. Roques, M. C. Fournié-zaluski, E. Soroca, J. M. Lecomte, B. Malfroy et al., The enkephalinase inhibitor thiorphan shows antinociceptive activity in mice, Nature, vol.188, issue.5788, pp.286-287, 1980.
DOI : 10.1038/288286a0

M. Schmidt, B. Kröger, E. Jacob, H. Seulberger, T. Subkowski et al., Molecular characterization of human and bovine endothelin converting enzyme (ECE-1), FEBS Letters, vol.180, issue.2-3, pp.238-243, 1994.
DOI : 10.1016/0014-5793(94)01277-6

K. Shimada, M. Takahashi, A. J. Turner, and K. Tanzawa, with a similar catalytic mechanism and a distinct substrate binding mechanism compared with neutral endopeptidase-24.11, Biochemical Journal, vol.315, issue.3, pp.863-867, 1996.
DOI : 10.1042/bj3150863

D. E. Tronrud, A. F. Monzingo, and B. W. Matthews, Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin, European Journal of Biochemistry, vol.22, issue.2, pp.261-268, 1986.
DOI : 10.1016/0022-2836(82)90319-9

A. J. Turner and L. J. Murphy, Molecular pharmacology of endothelin converting enzymes, Biochemical Pharmacology, vol.51, issue.2, pp.91-102, 1996.
DOI : 10.1016/0006-2952(95)02036-5

S. J. Weiner, P. A. Kollman, D. T. Nguyen, and D. A. Case, An all atom force field for simulations of proteins and nucleic acids, Journal of Computational Chemistry, vol.82, issue.2, pp.230-235, 1986.
DOI : 10.1002/jcc.540070216