Biology:Meprin B

From HandWiki
Meprin B
Identifiers
EC number3.4.24.63
CAS number150679-52-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

  1. "Meprin-A and -B. Cell surface endopeptidases of the mouse kidney". The Journal of Biological Chemistry 266 (26): 17350–7. September 1991. PMID 1894622. 
  2. "Cloning, expression, and chromosomal localization of the mouse meprin beta subunit". The Journal of Biological Chemistry 268 (28): 21035–43. October 1993. PMID 8407940. 
  3. "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. March 1994. PMID 7510289. 
  4. Meprins A and B. Methods in Enzymology. 248. 1995. pp. 325–45. doi:10.1016/0076-6879(95)48022-6. 
  5. 5.0 5.1 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. https://www.jbc.org/content/280/14/13895.full. 

External links