EC Number |
Reaction |
Reference |
---|
3.4.22.49 | all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage |
- |
- |
3.4.22.49 | all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage |
unphosphorylatable form of cohesin subunit Rad21 is less efficiently cleaved by Separase |
697171 |
3.4.22.49 | all bonds known to be hydrolysed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by an hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage |
cohesin cleavage by human separase requires DNA in a sequence-nonspecific manner (in vitro). Autocleavage of separase is not stimulated by DNA. Cleavage of the chromosome-associated cohesins is sensitive to nuclease treatment. |
697240 |