The Enzyme Database

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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
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 148938-24-3
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. [DOI] [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]

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