Meprin B (EC 3.4.24.63, meprin-b) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-Leu-, -Leu6-Cys-, -Ala14-Leu- and -Cys19-Gly- bonds in insulin B chain
Even though it is primarily found and embedded into the cell membrane it can also be found in the extracellular space.[5] Like other meprins it can hydrolyze different molecules.[5]
This membrane-bound metalloendopeptidase is present in mouse intestines.
References
edit- ^ Kounnas MZ, Wolz RL, Gorbea CM, Bond JS (September 1991). "Meprin-A and -B. Cell surface endopeptidases of the mouse kidney". The Journal of Biological Chemistry. 266 (26): 17350–7. PMID 1894622.
- ^ Gorbea CM, Marchand P, Jiang W, Copeland NG, Gilbert DJ, Jenkins NA, Bond JS (October 1993). "Cloning, expression, and chromosomal localization of the mouse meprin beta subunit". The Journal of Biological Chemistry. 268 (28): 21035–43. PMID 8407940.
- ^ Johnson GD, Hersh LB (March 1994). "Expression of meprin subunit precursors. Membrane anchoring through the beta subunit and mechanism of zymogen activation". The Journal of Biological Chemistry. 269 (10): 7682–8. PMID 7510289.
- ^ Wolz RL, Bond JS (1995). Meprins A and B. Methods in Enzymology. Vol. 248. pp. 325–45. doi:10.1016/0076-6879(95)48022-6. PMID 7674930.
- ^ a b Ishmael, Faoud T.; Shier, Vincent K.; Ishmael, Susan S.; Bond, Judith S. (February 2005). "Intersubunit and Domain Interactions of the Meprin B Metalloproteinase DISULFIDE BONDS AND PROTEIN-PROTEIN INTERACTION IN THE MAM AND TRAF DOMAINS". Journal of Biological Chemistry. 280: 13895–13901.
External links
edit- Meprin+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
