KEGG   ENZYME: 3.4.21.106Help
Entry
EC 3.4.21.106               Enzyme                                 

Name
hepsin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys
Comment
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.
Reference
1  [PMID:9003440]
  Authors
Zhukov A, Hellman U, Ingelman-Sundberg M.
  Title
Purification and characterization of hepsin from rat liver microsomes.
  Journal
Biochim. Biophys. Acta. 1337 (1997) 85-95.
  Organism
Rattus norvegicus [GN:rno]
Reference
2  [PMID:7814421]
  Authors
Kazama Y, Hamamoto T, Foster DC, Kisiel W.
  Title
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.
  Journal
J. Biol. Chem. 270 (1995) 66-72.
  Organism
Homo sapiens [GN:hsa]
Reference
3  [PMID:8346233]
  Authors
Torres-Rosado A, O'Shea KS, Tsuji A, Chou SH, Kurachi K.
  Title
Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 7181-5.
  Organism
Homo sapiens [GN:hsa]
  Sequence
[hsa:3249]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
112398-23-9

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