Pyrolysin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.B55 pyrolysin
Pyrolysin is a hyperthermophilic serine endopeptidase produced by the archaeon Pyrococcus furiosus, named for its extreme thermophilicity. It hydrolyzes alphaS1-casein at two preferential sites, the Gln9-Gly10 bond and the Leu16-Asn17 bond, and is active under near-boiling conditions. In the host it participates in extracellular protein degradation at temperatures above 90 °C. It belongs to the subtilisin-related S53 family and carries an elaborate propeptide and surface loops adapted for thermostability.
Pyrolysin is a hyperthermophilic serine endopeptidase produced by the archaeon Pyrococcus furiosus, named for its extreme thermophilicity. It hydrolyzes alphaS1-casein at two preferential sites, the Gln9-Gly10 bond and the Leu16-Asn17 bond, and is active under near-boiling conditions. In the host it participates in extracellular protein degradation at temperatures above 90 °C. It belongs to the subtilisin-related S53 family and carries an elaborate propeptide and surface loops adapted for thermostability.
References:
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