EC 220.127.116.11 - Meprin A
IntEnz Enzyme Nomenclature
- Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.
A membrane-bound metalloendopeptidase of rat and mouse kidney and intestinal brush borders, and salivary ducts. Differences from neprilysin (EC 18.104.22.168) include insensitivity to phosphoramidon and thiorphan. PABA-peptide hydrolase is a very similar enzyme found in human intestinal microvilli . In peptidase family M12 (astacin family). Formerly included in EC 22.214.171.124.
Links to other databases
Purification and characterization of a metallo-endoproteinase from mouse kidney.Biochem. J. 199: 591-598 (1981). [PMID: 7041888]
Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney.Biochem. J. 241: 229-235 (1987). [PMID: 3105525]
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]
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]
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 126.96.36.199 created 1992]