ExplorEnz: EC 3.4.21.106

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3.4.21.106

Accepted name:

hepsin

Reaction:

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

Comments:

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.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 112398-23-9

References:

1.	Zhukov, A., Hellman, U. and Ingelman-Sundberg, M. Purification and characterization of hepsin from rat liver microsomes. Biochim. Biophys. Acta 1337 (1997) 85–95. [DOI] [PMID: 9003440]
2.	Kazama, Y., Hamamoto, T., Foster, D.C. and 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. [DOI] [PMID: 7814421]
3.	Torres-Rosado, A., O'Shea, K.S., Tsuji, A., Chou, S.H. and Kurachi, K. Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth. Proc. Natl. Acad. Sci. USA 90 (1993) 7181–7185. [DOI] [PMID: 8346233]

[EC 3.4.21.106 created 2006]