polyserase-2 (polyserine protease 2, serine protease 36, PRSS36)
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Function
- serine protease
- hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC & N-t-Boc-Gln-Gly-Arg-AMC > N-t-Boc-Ala-Phe-Lys-AMC & N-t-Boc-Val-Leu-Lys-AMC
- preference for substrates with Arg instead of Lys residue in position P1
Inhibition:
- inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride (AEBSF), but not by EDTA or E-64
Structure
- 1st serine protease domain is catalytically active, 2nd domain lacks the essential His of catalytic triad at position 363, thus inactive 3rd domain lacks essential Asp of catalytic triad at position 679, thus inactive
- the 3 protease domains are not proteolytically cleaved
- N-glycosylated
- belongs to the peptidase S1 family
Compartment
Expression
- expressed in fetal kidney, skeletal muscle, liver, placenta, heart
Pathology
- expressed in tumor cell lines derived from lung & colon adenocarcinomas