ExplorEnz: EC 3.4.24.18

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3.4.24.18

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 3.4.24.11) (astacin family). Formerly included in EC 3.4.24.11

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 148938-24-3

References:

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 3.4.24.18 created 1992]