| EC |
3.4.24.63 |
| Accepted name: |
meprin B |
| Reaction: |
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5┼Leu-, -Leu6┼Cys-, -Ala14┼Leu- and -Cys19┼Gly- bonds in insulin B chain |
| Other name(s): |
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, Gene, KEGG, MetaCyc, MEROPS, 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] |
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| [EC 3.4.24.63 created 1995] |
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