Accepted name: meprin A
Reaction: Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Other name(s): endopeptidase-2; meprin-a; meprin; N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; PABA-peptide hydrolase; PPH
Comments: A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC (astacin family). Formerly included in EC
1.  Beynon, R.J., Shannon, J.D. and Bond, J.S. Purification and characterization of a metallo-endoproteinase from mouse kidney. Biochem. J. 199 (1981) 591–598. [PMID: 7041888]
2.  Butler, P.E., McKay, M.J. and Bond, J.S. Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney. Biochem. J. 241 (1987) 229–235. [PMID: 3105525]
3.  Stephenson, S.L. and Kenny, A.J. The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme 'endopeptidase-2′ and by rat microvillar membranes. Biochem. J. 255 (1988) 45–51. [PMID: 2461706]
4.  Sterchi, E.E., Naim, H.Y., Lentze, M.J., Hauri, H.-P. Fransen, J.A.M. N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides. Arch. Biochem. Biophys. 265 (1988) 105–118. [PMID: 3261961]
5.  Barnes, K., Ingram, J. and Kenny, A.J. Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse. Biochem. J. 264 (1989) 335–346. [PMID: 2690825]
[EC created 1992]