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ENZYME entry: EC

Accepted Name
Reaction catalysed
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.
PRIAM enzyme-specific profiles3.4.21.106
KEGG Ligand Database for Enzyme Nomenclature3.4.21.106
IUBMB Enzyme Nomenclature3.4.21.106
MEDLINEFind literature relating to
Rhea expert-curated reactions3.4.21.106
Q05511, HEPS_RAT;  

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