Meprin B
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
Meprin B | |||||||||
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Identifiers | |||||||||
EC number | 3.4.24.63 | ||||||||
CAS number | 150679-52-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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This membrane-bound metalloendopeptidase is present in mouse intestines.
References
- 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. 248: 325–45. doi:10.1016/0076-6879(95)48022-6. PMID 7674930.
External links
- Meprin+B at the US National Library of Medicine Medical Subject Headings (MeSH)
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