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ENZYME entry: EC 188.8.131.52
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|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
- 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 profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
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entries corresponding to 3.4.21.-
entries corresponding to 3.4.-.-
entries corresponding to 3.-.-.-