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3.4.22.49: separase

This is an abbreviated version!
For detailed information about separase, go to the full flat file.

Word Map on EC 3.4.22.49

Reaction

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 =

Synonyms

AESP, AtESP, Cut1, Cut1/separase, ESP, Esp1, ESPL1, sep-1, separase, separin, SSE, TbSep

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.49 separase

Crystallization

Crystallization on EC 3.4.22.49 - separase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of full-length separase in complex with securin
crystal structures of the active protease segment of Chaetomium thermophilum separase in complex with a substrate-mimic inhibitor at up to 1.85 A resolution
Thermochaetoides thermophila
crystal structures of the separase protease domain from the thermophilic fungus Chaetomium thermophilum, alone or covalently bound to unphosphorylated and phosphorylated inhibitory peptides derived from a cohesin cleavage site
Thermochaetoides thermophila