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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

Subunits

Subunits on EC 3.4.22.49 - separase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the human separase is composed of three domains: the tail, the trunk, and the head, structure modeling. The first two domains are spanned by Armadillo, ARM, repeats, which are composed of multiple 42 amino acid repeats and are present in the proteomes of all eukaryotic organisms. The ARM repeat domain is highly conserved right-handed super helix of ?-helices, which serves as molecular scaffold for protein-protein interactions. Phosphorylation and potential autocleavage sites span the region of the last ARM repeats and the central unstructured region. Human separase has an N-terminal region spanned by 26 ARM repeats and separated from the