The Enzyme Database

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Accepted name: furin
Reaction: Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg┼ bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors
Other name(s): prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase
Comments: 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: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 141760-45-4
1.  Van de Ven, W.J.M., Voorberg, J., Fontijn, R., Pannekoek, H., van den Ouweland, A.M.W., van Duijnhoven, H.L.P., Roebroek, A.J.M. and Siezen, R.J. Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes. Mol. Biol. Rep. 14 (1990) 265–275. [PMID: 2094803]
2.  Van de Ven, W.J.M., Creemers, J.W.M. and Roebroek, A.J.M. Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway. Enzyme 45 (1991) 257–270. [PMID: 1843280]
3.  Hatsuzawa, K., Murakami, K. and Nakayama, K. 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 (1992) 296–301. [PMID: 1587790]
4.  Seidah, N.G. and Chrétien, M. Proprotein and prohormone convertases of the subtilisin family: recent developments and future perspectives. Trends Endocrinol. Metab. 3 (1992) 133–140. [PMID: 18407092]
5.  Steiner, D.F., Smeekens, S.P., Ohagi, S. and Chan, S.J. The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267 (1992) 23435–23438. [PMID: 1429684]
[EC created 1993]

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