Reaction: Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'
Other names: neutral endopeptidase; endopeptidase 24.11; kidney-brush-border neutral peptidase; enkephalinase (misleading); endopeptidase-2; CALLA (common acute lymphoblastic leukemia-associated) antigens; CALLA antigen; endopeptidase; membrane metalloendopeptidase; kidney-brush-border neutral endopeptidase; kidney-brush-border neutral proteinase; endopeptidase-2; CALLA glycoprotein; CALLA; common acute lymphoblastic leukemia antigen; CALLA glycoproteins; common acute lymphoblastic leukemia-associated antigens; neutral metallendopeptidase; membrane metalloendopeptidase; NEP; neutral endopeptidase 24.11; CD10; neutral endopeptidase; acute lymphoblastic leukemia antigen
Comments: A membrane-bound glycoprotein widely distributed in animal tissues. Inhibited by phosphoramidon and thiorphan. Common acute lymphoblastic leukemia antigen (CALLA). Type example of peptidase family M13
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 82707-54-8
References:
1. Matsas, R., Fulcher, I.S., Kenny, A.J. and Turner, A.J. Substance P and [Leu]enkephalin are hydrolyzed by an enzyme in pig caudate synaptic membranes that is identical with the endopeptidase of kidney microvilli. Proc. Natl. Acad. Sci. USA 80 (1983) 3111-3115. [PMID: 6190172]
2. Malfroy, B., Schofield, P.R., Kuang, W.-J., Seeburg, P.H., Mason, A.J. Henzel, W.J. Molecular cloning and amino acid sequence of rat enkephalinase. Biochem. Biophys. Res. Commun. 144 (1987) 59-66. [PMID: 3555489]
3. Letarte, M., Vera, S., Tran, R., Addis, J.B.L., Onizuka, R.J., Quackenbush, E J., Jongneel, C.V. and McInnes, R.R. Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. J. Exp. Med. 168 (1988) 1247-1253. [PMID: 2971756]
4. Erdös, E.G. and Skidgel, R.A. Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3 (1989) 145-151. [PMID: 2521610]