Information on EC 3.4.22.B75 - SENP7 peptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B75
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
SENP7 peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms. SENP67 prefers the LRGG-/- sequence versus the QTGG-/- sequence.
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the SENP/ULP protease family
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(di-SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
?
show the reaction diagram
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SENP7 displays isopeptidase activity against di-SUMO-2- and SUMO-2-modified Ran GTPase-activating protein 1 but has limited activity against SUMO-1-modified Ran GTPase-activating protein 1
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?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
?
show the reaction diagram
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SENP7 displays isopeptidase activity against di-SUMO-2- and SUMO-2-modified Ran GTPase-activating protein 1 but has limited activity against SUMO-1-modified Ran GTPase-activating protein 1
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?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
show the reaction diagram
SENP6 and SENP7 prefer SUMO2 or SUMO3 in deconjugation reactions with rates comparable with those catalyzed by SENP2. In contrast to SENP2, SENP6 and SENP7 are less able to deconjugate SUMO1-RanGAP1, and products are only detected at enzyme concentrations 100 x higher than that observed for reactions containing SENP2
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?
acetyl-LRGG-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-LRGG + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
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SENP7 prefers the LRGG sequence, residues typical of Nedd8 or ubiquitin in the P3 and P4 positions
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?
acetyl-QTGG-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-QTGG + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
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very low activity
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?
di-SUMO-2 + H2O
2 SUMO-2
show the reaction diagram
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?
di-SUMO-3 + H2O
2 SUMO-3
show the reaction diagram
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?
poly-SUMO-2 + H2O
?
show the reaction diagram
poly-SUMO-3 + H2O
?
show the reaction diagram
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?
polySUMO2 KRAB-associated protein 1 + H2O
KRAB-associated protein 1 + SUMO 2 + SUMO3
show the reaction diagram
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enzyme SENP7 promotes the removal of SUMO2 from KRAB-associated protein 1
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?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
show the reaction diagram
SENP7 exhibits lower rates for processing pre-SUMO-1, pre-SUMO-2, or pre-SUMO-3 in comparison with SENP2
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?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
show the reaction diagram
SENP7 exhibits lower rates for processing pre-SUMO1, pre-SUMO-2, or pre-SUMO-3 in comparison with SENP2
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?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
show the reaction diagram
SENP7 exhibits lower rates for processing pre-SUMO1, pre-SUMO-2, or pre-SUMO-3 in comparison with SENP2
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SUMO1-HP1 + H2O
HP1 + SUMO1
show the reaction diagram
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deSUMOylation
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SUMO2/3ylated HP1alpha + H2O
HP1alpha + SUMO3 + SUMO2
show the reaction diagram
SUMOylated c-Myc + H2O
deSUMOylated c-Myc + SUMO
show the reaction diagram
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?
SUMOylated HP1alpha + H2O
HP1alpha + SUMO
show the reaction diagram
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SUMO deconjugation by enzyme SENP7
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SUMOylated KRAB-associated protein 1 + H2O
KRAB-associated protein 1 + SUMO 2 + SUMO3
show the reaction diagram
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enzyme SENP7 promotes the removal of SUMO2/3 from KRAB-associated protein 1
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
poly-SUMO-2 + H2O
?
show the reaction diagram
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the C-terminal catalytic domain of SENP7 efficiently depolymerized poly-SUMO-2 chains but has undetectable activity against poly-SUMO-1 chains
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?
SUMO1-HP1 + H2O
HP1 + SUMO1
show the reaction diagram
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deSUMOylation
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SUMO2/3ylated HP1alpha + H2O
HP1alpha + SUMO3 + SUMO2
show the reaction diagram
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HP1alpha localizes at the pericentric heterochromatin, importance of SUMOylation in directing HP1alpha’s subnuclear localization, SUMO deconjugation by enzyme SENP7
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?
SUMOylated c-Myc + H2O
deSUMOylated c-Myc + SUMO
show the reaction diagram
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SUMOylated HP1alpha + H2O
HP1alpha + SUMO
show the reaction diagram
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SUMO deconjugation by enzyme SENP7
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?
SUMOylated KRAB-associated protein 1 + H2O
KRAB-associated protein 1 + SUMO 2 + SUMO3
show the reaction diagram
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enzyme SENP7 promotes the removal of SUMO2/3 from KRAB-associated protein 1
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?
additional information
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
truncated SUMO-2
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whereas truncated SUMO-2 and -3 can substantially enhance SENP6 activity, neither truncated SUMO-1 nor truncated Nedd8 nor ubiquitin has this ability
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truncated SUMO-3
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whereas truncated SUMO-2 and -3 can substantially enhance SENP6 activity, neither truncated SUMO-1 nor truncated Nedd8 nor ubiquitin has this ability
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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two splicing variants, a short SENP7 splice variant SENP7S and a long transcript SENP7L
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of the SENP7 catalytic domain are obtained at 18°C by sitting drop vapor diffusion methods crystal structure of the SENP7 catalytic domain at a resolution of 2.4 A
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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recombinant expression of GFP-tagged wild-type and mutant enzyme SENP7
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recombinant expression of N-terminally FLAG-tagged wild-type and mutant enzymes in HEK-293 cells
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recombinant exxpression of GFP-tagged SENP7 constructs in NIH-3T3 cell nuclei
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C745K
mutation does not alter deconjugation rates in comparison with wild-type SENP7
C992A
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site-directed mutagenesis, inactive catalytic mutant
F709W
end point deconjugation reactions using di-SUMO2/3 or poly-SUMO2/3 reveales rates equivalent to or slightly greater than wild-type SENP7. Mutation results in a 2fold higher activity when di-SUMO2 deconjugation rates are measured
V713E
mutation elicits 65-fold reduction in deconjugation rate compared to wild-type activity
V713E/C745K
C745K substitution partially rescues defects observed for SENP7-V713E when present as a double point substitution (SENP7-V713E/C745K)
C979S
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site-directed mutagenesis
additional information