Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:3162886). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (By similarity). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (By similarity). Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'. H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9) H2O + substance P = L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-7) H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11) H2O + neurotensin = L-tyrosyl-L-isoleucyl-L-leucine + neurotensin(1-10) Binds 1 zinc ion per subunit. Inhibited by mixanpril, an orally-active drug used for the treatment of hypertension. Myristoylation is a determinant of membrane targeting. Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. Belongs to the peptidase M13 family.