CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family

Enzyme Information
based on mapping to UniProt P05981
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. -!- The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation. -!- There is no cleavage after aromatic or aliphatic residues. -!- 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 favorable than Ala. -!- Belongs to peptidase family S1A.

UniProtKB Entries (1)

Homo sapiens
Serine protease hepsin

PDB Structure

External Links
Organism Pichia
Primary Citation
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA).
Katz, B.A., Luong, C., Ho, J.D., Somoza, J.R., Gjerstad, E., Tang, J., Williams, S.R., Verner, E., Mackman, R.L., Young, W.B., Sprengeler, P.A., Chan, H., Mortara, K., Janc, J.W., McGrath, M.E.