EC 126.96.36.199 - Furin
IntEnz Enzyme Nomenclature
dibasic processing enzyme
paired basic amino acid cleaving enzyme
paired basic amino acid converting enzyme
serine proteinase PACE
- Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg┼ bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
One of a group of peptidases in peptidase family S8 (subtilisin family) that is structurally and functionally similar to kexin. All are activated by Ca2+, contain Cys near the active site His, and are inhibited by p-mercuribenzoate. At least three related enzymes are recognized in mammals: PC2, PC3 and PC4, which have somewhat different specificities.
Links to other databases
Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes.Mol. Biol. Rep. 14: 265-275 (1990). [PMID: 2094803]
Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway.Enzyme 45: 257-270 (1991). [PMID: 1843280]
Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.J. Biochem. (Tokyo) 111: 296-301 (1992). [PMID: 1587790]
Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives.Trends Endocrinol. Metab. 3: 133-140 (1992).
The new enzymology of precursor processing endoproteases.J. Biol. Chem. 267: 23435-23438 (1992). [PMID: 1429684]
[EC 188.8.131.52 created 1993]