Magnolysin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.62 magnolysin
Meprin B is a brush-border membrane zinc metalloendopeptidase found in the intestine of all tested mouse strains and the kidney of certain inbred strains, in peptidase family M12 (astacin family). It is a tetramer of meprin beta subunits, in contrast to meprin A which contains both alpha and beta subunits, occurs in kidney as a proenzyme activated by trypsin, and is inhibited by EDTA and 1,10-phenanthroline but not by phosphoramidon, captopril or thiorphan. It hydrolyzes proteins including azocasein and peptides, cleaving -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- in the insulin B chain. In kidney and intestine it processes cytokines and growth factors. It features an astacin-like catalytic ectodomain.
Meprin B is a brush-border membrane zinc metalloendopeptidase found in the intestine of all tested mouse strains and the kidney of certain inbred strains, in peptidase family M12 (astacin family). It is a tetramer of meprin beta subunits, in contrast to meprin A which contains both alpha and beta subunits, occurs in kidney as a proenzyme activated by trypsin, and is inhibited by EDTA and 1,10-phenanthroline but not by phosphoramidon, captopril or thiorphan. It hydrolyzes proteins including azocasein and peptides, cleaving -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- in the insulin B chain. In kidney and intestine it processes cytokines and growth factors. It features an astacin-like catalytic ectodomain.
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