The protein encoded by this gene, belongs to
peptidase family S1. It is first synthesized as an inactive single-chain precursor before being activated to a
heterodimeric form by endoproteolytic processing. It acts as
serine protease that converts
hepatocyte growth factor to the active form.[7]
Shimomura T, Ochiai M, Kondo J, Morimoto Y (1992). "A novel protease obtained from FBS-containing culture supernatant, that processes single chain form hepatocyte growth factor to two chain form in serum-free culture". Cytotechnology. 8 (3): 219–29.
doi:
10.1007/BF02522039.
PMID1368819.
S2CID24061579.
Shia S, Stamos J, Kirchhofer D, et al. (2005). "Conformational lability in serine protease active sites: structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B". J. Mol. Biol. 346 (5): 1335–49.
doi:
10.1016/j.jmb.2004.12.048.
PMID15713485.
The protein encoded by this gene, belongs to
peptidase family S1. It is first synthesized as an inactive single-chain precursor before being activated to a
heterodimeric form by endoproteolytic processing. It acts as
serine protease that converts
hepatocyte growth factor to the active form.[7]
Shimomura T, Ochiai M, Kondo J, Morimoto Y (1992). "A novel protease obtained from FBS-containing culture supernatant, that processes single chain form hepatocyte growth factor to two chain form in serum-free culture". Cytotechnology. 8 (3): 219–29.
doi:
10.1007/BF02522039.
PMID1368819.
S2CID24061579.
Shia S, Stamos J, Kirchhofer D, et al. (2005). "Conformational lability in serine protease active sites: structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B". J. Mol. Biol. 346 (5): 1335–49.
doi:
10.1016/j.jmb.2004.12.048.
PMID15713485.