The Enzyme Database

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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, KEGG, MetaCyc, MEROPS, 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]
[EC 3.4.24.63 created 1995]
 
 


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