hepsin

Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases

Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys

This type-II membrane-associated serine peptidase has been implicated in cell growth and development [1,3]. The enzyme has been shown to activate blood coagulation factor VII by cleavage of the Arg152!Ile153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation [2]. There is no cleavage after aromatic or aliphatic residues [1]. The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue. The nature of the residue at S3 also affects hydrolysis, with Gln being much more favourable than Ala [1]. Belongs in peptidase family S1A.

1  [PMID:9003440]

Zhukov A, Hellman U, Ingelman-Sundberg M.

Purification and characterization of hepsin from rat liver microsomes.

Biochim. Biophys. Acta. 1337 (1997) 85-95.

Rattus norvegicus [GN:rno]

2  [PMID:7814421]

Kazama Y, Hamamoto T, Foster DC, Kisiel W.

Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation.

J. Biol. Chem. 270 (1995) 66-72.

Homo sapiens [GN:hsa]

3  [PMID:8346233]

Torres-Rosado A, O'Shea KS, Tsuji A, Chou SH, Kurachi K.

Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth.

Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 7181-5.

Homo sapiens [GN:hsa]