EC 3.4.24.63

Reaction: Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His⁵Leu-, -Leu⁶Cys-, -Ala¹⁴Leu- and -Cys¹⁹Gly- bonds in insulin B chain

Other names: meprin-b

Comments: A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin β subunits (in contrast to meprin A, which contains both α and β subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family)

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 150679-52-0

References

1. Kounnas, M.Z., Wolz, R.L., Gorbea, C.M. and Bond, J.S. Meprin-A and -B. Cell surface endopeptidases of the mouse kidney. J. Biol. Chem. 266 (1991) 17350-17357. [PMID: 1894622]

2. Gorbea, C.M., Marchand, P., Jiang, W., Copeland, N.G., Gilbert, D.J., Jenkins, N.A. and Bond, J.S. Cloning, expression, and chromosomal localization of the mouse meprin β subunit. J. Biol. Chem. 268 (1993) 21035-21043. [PMID: 8407940]

3. Johnson, G.D. and Hersh, L.B. Expression of meprin subunit precursors. Membrane anchoring through the β subunit and mechanism of zymogen activation. J. Biol. Chem. 269 (1994) 7682-7688. [PMID: 7510289]

4. Wolz, R.L. and Bond, J.S. Meprins A and B. Methods Enzymol. 248 (1995) 325-345. [PMID: 7674930]