EC - Meprin A

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IntEnz Enzyme Nomenclature


Accepted name:
meprin A
Other names:
N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase
PABA-peptide hydrolase
Systematic name:




A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC include insensitivity to phosphoramidon and thiorphan. PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli [4]. In peptidase family M12 (astacin family). Formerly included in EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004222
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 : 591-598 (1981). [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 : 229-235 (1987). [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 : 45-51 (1988). [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 : 105-118 (1988). [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 : 335-346 (1989). [PMID: 2690825]

[EC created 1992]