Separase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.49 separase
Separase is a large cysteine endopeptidase required for sister-chromatid separation at anaphase, the type example of peptidase family C50. In budding yeast and human cells it cleaves the cohesin subunit Scc1 to trigger anaphase; budding yeast separase also cleaves the meiotic cohesin Rec8 subunit and the kinetochore protein Slk19. All bonds hydrolyzed by separase have Arg at P1 and an acidic residue at P4, with P6 often an acidic or hydroxy amino acid whose phosphorylation enhances cleavage. In eukaryotes it triggers the metaphase-to-anaphase transition. It features a caspase-related protease domain regulated by securin and Cdk1 phosphorylation.
Separase is a large cysteine endopeptidase required for sister-chromatid separation at anaphase, the type example of peptidase family C50. In budding yeast and human cells it cleaves the cohesin subunit Scc1 to trigger anaphase; budding yeast separase also cleaves the meiotic cohesin Rec8 subunit and the kinetochore protein Slk19. All bonds hydrolyzed by separase have Arg at P1 and an acidic residue at P4, with P6 often an acidic or hydroxy amino acid whose phosphorylation enhances cleavage. In eukaryotes it triggers the metaphase-to-anaphase transition. It features a caspase-related protease domain regulated by securin and Cdk1 phosphorylation.
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