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Information on EC 3.4.22.49 - separase and Organism(s) Arabidopsis thaliana and UniProt Accession Q5IBC5

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.49 separase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q5IBC5 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
separase, sep-1, espl1, separin, atesp, cut1/separase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
separin
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
351527-77-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cohesin + H2O
?
show the reaction diagram
-
-
-
?
SYN1 + H2O
?
show the reaction diagram
the enzyme plays an essential role in embryo development. The enzyme is required for the removal of cohesin from meiotic chromosomes. The cleavage of SYN1 by separase is responsible for the release of sister chromatid cohesion during meiosis
-
-
?
cohesin + H2O
cleaved cohesin
show the reaction diagram
-
-
-
-
?
cohesin + H2O
fragments of cohesin
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cohesin + H2O
?
show the reaction diagram
-
-
-
?
SYN1 + H2O
?
show the reaction diagram
the enzyme plays an essential role in embryo development. The enzyme is required for the removal of cohesin from meiotic chromosomes. The cleavage of SYN1 by separase is responsible for the release of sister chromatid cohesion during meiosis
-
-
?
cohesin + H2O
cleaved cohesin
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the enzyme contains a Ca2+-binding EF-hand motif, which can possibly affect separase interaction with the spindle, similar to the budding yeast Esp1, or alternatively Ca2+ might be a critical component for (auto-)catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
securin
in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
knocking down AtESP in meiocytes using RNAi unexpectedly converts the symmetric radial microtubule systems that form after telophase II into asymmetric structures partially resembling phragmoplasts
physiological function
malfunction
physiological function
additional information
securin, in addition to its inhibitory role, can act as a molecular chaperone of separase, essential for its proper folding
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ESP1_ARATH
2180
0
244847
Swiss-Prot
other Location (Reliability: 5)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
during metaphase, separase is kept inactive through its binding to the chaperone securin. During anaphase, APCcdc20 cleaves securin releasing separase. Active separase cleaves itself, and the resulting N- and C-terminal fragments associate, mechanism of separase maturation during metaphase to anaphase transition
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, Z.; Makaroff, C.A.
Arabidopsis separase AESP is essential for embryo development and the release of cohesin during meiosis
Plant Cell
18
1213-1225
2006
Arabidopsis thaliana (Q5IBC5), Arabidopsis thaliana
Manually annotated by BRENDA team
Wu, S.; Scheible, W.R.; Schindelasch, D.; Van Den Daele, H.; De Veylder, L.; Baskin, T.I.
A conditional mutation in Arabidopsis thaliana separase induces chromosome non-disjunction, aberrant morphogenesis and cyclin B1,1 stability
Development
137
953-961
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Yang, X.; Boateng, K.A.; Strittmatter, L.; Burgess, R.; Makaroff, C.A.
Arabidopsis separase functions beyond the removal of sister chromatid cohesion during meiosis
Plant Physiol.
151
323-333
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Moschou, P.N.; Bozhkov, P.V.
Separases: biochemistry and function
Physiol. Plant.
145
67-76
2012
Saccharomyces cerevisiae, Caenorhabditis elegans, Ricinus communis, Chlamydomonas reinhardtii, Drosophila melanogaster, Homo sapiens, Oryza sativa, Schizosaccharomyces pombe, Sorghum bicolor, Vitis vinifera, Cryptosporidium muris, Arabidopsis thaliana (Q5IBC5)
Manually annotated by BRENDA team
Kumar, R.
Separase Function beyond cohesion cleavage and an emerging oncogene
J. Cell. Biochem.
118
1283-1299
2017
Caenorhabditis elegans, Arabidopsis thaliana (A0A1P8B3N4), Schizosaccharomyces pombe (P18296), Saccharomyces cerevisiae (Q03018), Drosophila melanogaster (Q9VRN6), Picea abies (R4XPW1), Schizosaccharomyces pombe ATCC 24843 (P18296)
Manually annotated by BRENDA team
Winter, A.; Schmid, R.; Bayliss, R.
Structural insights into separase architecture and substrate recognition through computational modelling of caspase-like and death domains
PLoS Comput. Biol.
11
e1004548
2015
Arabidopsis thaliana (Q5IBC5), Caenorhabditis elegans (G5ED39), Caenorhabditis elegans, Homo sapiens (Q14674), Saccharomyces cerevisiae (Q03018), Saccharomyces cerevisiae ATCC 204508 (Q03018)
Manually annotated by BRENDA team