Pernilase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.B58 pernilase
Pernilase is a thiol-dependent serine peptidase from Archaea and Bacteria with broad trypsin-like substrate specificity. It hydrolyzes azocasein and synthetic arginine-containing amide substrates including benzoyl-Arg-AMC, Boc-Gly-Lys-Arg-AMC, Boc-Leu-Gly-Arg-AMC and Boc-Phe-Ser-Arg-AMC in the presence of water, with a strong preference for basic P1 residues. In organisms it contributes to intracellular protein turnover. It features a catalytic serine activated in a thiol-dependent manner, distinct from classical trypsin.
Pernilase is a thiol-dependent serine peptidase from Archaea and Bacteria with broad trypsin-like substrate specificity. It hydrolyzes azocasein and synthetic arginine-containing amide substrates including benzoyl-Arg-AMC, Boc-Gly-Lys-Arg-AMC, Boc-Leu-Gly-Arg-AMC and Boc-Phe-Ser-Arg-AMC in the presence of water, with a strong preference for basic P1 residues. In organisms it contributes to intracellular protein turnover. It features a catalytic serine activated in a thiol-dependent manner, distinct from classical trypsin.
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