Information on EC 3.4.22.B70 - SENP1 peptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B70
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
SENP1 peptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO-1, SUMO-2 and SUMO-3 to their mature forms and deconjugation of SUMO-1, SUMO-2 and SUMO-3 from targeted proteins. Deconjugates SUMO-1 from homeodomain-interacting protein kinase 2. Deconjugates SUMO-1 from histone deacetylase 1, which decreases its transcriptional repression activity. Cleavage of Gly97-/-His98 bond in the SUMO-1 precursor with release of the propeptide His-Ser-Thr-Val. Cleavage of Gly93-/-Val94 bond in the SUMO-2 precursor with release of the propeptide Val94-Thyr. Cleavage of the Gly92-/-Val93 in the SUMO-3 precursor with release of the propeptide Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe.
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Q9P0U3 {SwissProt}
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
show the reaction diagram
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
show the reaction diagram
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
show the reaction diagram
(SUMO-1)-K2P1 potassium channel + H2O
SUMO-1 + K2P1 potassium channel
show the reaction diagram
-
silent K2P1 channels in excised plasma membrane patches are activated by SENP1
-
-
?
(SUMO-1)-K2P1 subunit of potassium channel + H2O
SUMO-1 + K2P1 subunit of potassium channel
show the reaction diagram
-
SUMO1 is conjugated to the epsilon-amino group of Lys274 of the K2P1 potassium channel. When mutated to Gln, Arg, Glu, Asp, Cys, or Ala, the channels are constitutively active and insensitive to SUMO1 and SENP1. Wild-type channels in plasma membrane have two K2P1 subunits and assemble with two SUMO1 monomers. Although channels engineered with one Lys274 site carry just one SUMO1 they are activated and silenced by SENP1 and SUMO1 like wild-type channels
-
-
?
(SUMO-1)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-1 + Ran GTPase-activating protein 1
show the reaction diagram
-
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
-
-
?
(SUMO-1)-RanGAP1 conjugate + H2O
SUMO-1 + RanGAP1
show the reaction diagram
-
SENP1 binding is accompanied by a conformational change in the substrate
-
-
?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2 + Ran GTPase-activating protein 1
show the reaction diagram
-
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
-
-
?
(SUMO-2)-RanGAP1 conjugate + H2O
SUMO-2 + RanGAP1
show the reaction diagram
-
SENP1 binding is accompanied by a conformational change in the substrate
-
-
?
(SUMO-2)n-glutathione S-transferase-promyelocytic leukemia protein conjugate + H2O
?
show the reaction diagram
-
glutathione S-transferase-promyelocytic leukemia protein bearing a polymeric chain of SUMO-2
-
-
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
show the reaction diagram
-
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
-
-
?
CrSUMO148 precursor + H2O
CrSUMO148 + peptide
show the reaction diagram
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CrSUMO148 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids. SENP1 solely cleaves CrSUMO148 at the peptide bond after the first diglycine motif, although there are four putative cleavage sites in the primary amino acid sequence
-
-
?
CrSUMO148-conjugated protein + H2O
CrSUMO148 + protein
show the reaction diagram
-
CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids
-
-
?
CrSUMO96 precursor + H2O
CrSUMO96 + peptide
show the reaction diagram
-
CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
-
-
?
CrSUMO96-conjugated protein + H2O
CrSUMO96 + protein
show the reaction diagram
-
CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids
-
-
?
CrSUMO97 precursor + H2O
CrSUMO97 + peptide
show the reaction diagram
-
CrSUMO97 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
-
-
?
CrSUMO97-conjugated protein + H2O
CrSUMO97 + protein
show the reaction diagram
-
CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids
-
-
?
Pin1 + H2O
?
show the reaction diagram
polyCrSUMO148 + H2O
?
show the reaction diagram
-
CrSUMO148 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids. polyCrSUMO148 chains aree completely deconjugated by SENP1
-
-
?
polyCrSUMO96 + H2O
?
show the reaction diagram
-
CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids. polyCrSUMO96 chains aree completely deconjugated by SENP1. SENP1 displays a similar efficiency to deconjugate either polymeric CrSUMO96 or CrSUMO97 chains
-
-
?
polyCrSUMO97 + H2O
?
show the reaction diagram
-
CrSUMO97 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids. polyCrSUMO97 chains aree completely deconjugated by SENP1. SENP1 displays a similar efficiency to deconjugate either polymeric CrSUMO96 or CrSUMO97 chains
-
-
?
pro-small ubiquitin-related modifier + H2O
small ubiquitin-related modifier + ?
show the reaction diagram
-
SENP1 processes the precursor SUMO to its mature form by catalyzing the cleavage of a scissile peptide bond
-
-
?
Sharp-1 protein + H2O
?
show the reaction diagram
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deSUMOylation by the enzyme
-
-
?
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
-
-
r
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
show the reaction diagram
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
show the reaction diagram
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
show the reaction diagram
SUMO-7-amido-4-methylcoumarin + H2O
SuMo + 7-amino-4-methylcoumarin
show the reaction diagram
SUMO-Elk-1 conjugate + H2O
SUMO + Elk-1
show the reaction diagram
SUMO-GATA 1 conjugate + H2O
SUMO + GATA1
show the reaction diagram
SUMO-homeodomain-interacting protein kinase 1 conjugate + H2O
SUMO + homeodomain-interacting protein kinase 1 conjugate
show the reaction diagram
-
-
-
-
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
show the reaction diagram
SUMO-STAT3 protein conjugate + H2O
SUMO + STAT3 protein
show the reaction diagram
-
-
-
-
?
SUMO1ylated protein + H2O
SUMO1 + protein
show the reaction diagram
SUMO2ylated protein + H2O
SUMO2 + protein
show the reaction diagram
-
-
-
-
?
SUMO3ylated protein + H2O
SUMO3 + protein
show the reaction diagram
-
-
-
-
?
SUMOylated androgen receptor + H2O
androgen receptor + SUMO1
show the reaction diagram
-
deconjugation
-
-
?
SUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + H2O
deSUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + SUMO1
show the reaction diagram
-
deSUMOylation
-
-
?
additional information
?
-
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
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
show the reaction diagram
-
SENP1 markedly contributes to the androgen-stimulated proliferation of prostate cancer cells
-
-
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
show the reaction diagram
-
SENP1 regulates that androgen receptor-dependent transcription through desumoylation of histone deacetylase 1 (HDAC1)
-
-
?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
show the reaction diagram
-
desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) may be regulated by the cytoplasmic-nuclear shuttling of SENP1. Desumoylation induces dissociation of homeodomain-interacting protein kinase 2 conjugate from nuclear bodies
-
-
?
(SUMO-1)-K2P1 potassium channel + H2O
SUMO-1 + K2P1 potassium channel
show the reaction diagram
-
silent K2P1 channels in excised plasma membrane patches are activated by SENP1
-
-
?
Pin1 + H2O
?
show the reaction diagram
-
Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain, deSUMOlation by SENP1
-
-
?
pro-small ubiquitin-related modifier + H2O
small ubiquitin-related modifier + ?
show the reaction diagram
-
SENP1 processes the precursor SUMO to its mature form by catalyzing the cleavage of a scissile peptide bond
-
-
?
Sharp-1 protein + H2O
?
show the reaction diagram
-
deSUMOylation by the enzyme
-
-
?
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
-
-
r
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
show the reaction diagram
-
cleavage of the -Gly-Gly-/-His-Ser-Thr-Val bond. The maturation reaction is the first committed step for subsequent sumoylation
-
-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
show the reaction diagram
-
cleavage of the -Gly-Gly-/-Val-Tyr. The maturation reaction is the first committed step for subsequent sumoylation
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
show the reaction diagram
-
cleavage of the -Gly-Gly-/-Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe bond. The maturation reaction is the first committed step for subsequent sumoylation
-
-
?
SUMO-Elk-1 conjugate + H2O
SUMO + Elk-1
show the reaction diagram
-
SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
-
-
?
SUMO-GATA 1 conjugate + H2O
SUMO + GATA1
show the reaction diagram
-
SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1
-
-
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
show the reaction diagram
SUMO-STAT3 protein conjugate + H2O
SUMO + STAT3 protein
show the reaction diagram
-
-
-
-
?
SUMO1ylated protein + H2O
SUMO1 + protein
show the reaction diagram
-
main substrate
-
-
?
SUMO2ylated protein + H2O
SUMO2 + protein
show the reaction diagram
-
-
-
-
?
SUMO3ylated protein + H2O
SUMO3 + protein
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
the enzyme effectively removes SUMO-1 moiety, in the presence of Ca2+ rather than Mn2+, from the sumoylated homeodomain-interacting protein kinase 2 conjugate
Mn2+
-
the enzyme effectively removes SUMO-1 moiety, in the presence of Ca2+ rather than Mn2+, from the sumoylated homeodomain-interacting protein kinase 2 conjugate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2Z)-3-(naphthalen-2-yl)-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]prop-2-enamide
-
-
1-(1H-indol-3-ylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
3% inhibition at 0.02 mM
1-(3-hydroxy-4-methylphenyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
5% inhibition at 0.02 mM
1-(5-aminopentyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
43% inhibition at 0.02 mM
1-(cyclohexylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
5% inhibition at 0.02 mM
1-(naphthalen-2-ylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
26% inhibition at 0.02 mM
1-naphthalen-1-yl-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
7% inhibition at 0.02 mM
1-naphthalen-2-yl-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
30% inhibition at 0.02 mM
1-[2-(1H-indol-3-yl)ethyl]-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
24% inhibition at 0.02 mM
1-[2-(naphthalen-2-yl)ethyl]-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
45% inhibition at 0.02 mM
2-(4-chlorophenyl)-2-oxoethyl 4-(benzoylamino)benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-diethoxybenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-dimethoxybenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-aminobenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-fluorobenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-hydroxybenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-methoxybenzoyl)amino]benzoate
-
-
2-(4-chlorophenyl)-2-oxoethyl 4-[[3-(benzyloxy)benzoyl]amino]benzoate
-
-
3-[(acetyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
3-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
4-methyl-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzenesulfonamide
-
17% inhibition at 0.02 mM
4-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
benzyl (3-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
-
-
benzyl (4-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
-
-
benzyl [4-(2-oxo-2-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]amino]ethoxy)phenyl]carbamate
-
23% inhibition at 0.02 mM
haemagglutinin-SUMO-vinylmethylester
-
iodoacetamide
-
inhibits desumoylation
N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]pyridine-2-carboxamide
-
7% inhibition at 0.02 mM
naphthalen-2-yl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]sulfamate
-
-
phenyl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamate
-
-
phenyl [[1-(2-hydroxyethyl)-2-oxo-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
phenyl [[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
phenyl [[2-oxo-1-(4-oxobutyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
SUMO-1-GG
-
product inhibition, competitive, inhibits cleavage of the SUMO-1 precursor, SUMO-2 precursor, (SUMO-1)-RanGAP1 conjugate and (SUMO-2)-RanGAP1 conjugate
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SUMO-2-GG
-
product inhibition, competitive, inhibits cleavage of the SUMO-1 precursor, SUMO-2 precursor, (SUMO-1)-RanGAP1 conjugate and (SUMO-2)-RanGAP1 conjugate
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tert-butyl [3-([[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]amino)propyl]carbamate
-
4% inhibition at 0.02 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
desumoylation is enhanced either by the forced translocation of SENP1 into the nucleus or by the SENP1 NES (nuclear export sequence) mutant
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000224
(SUMO-1)-RanGAP1 conjugate
-
pH 7.5, 30°C
-
0.00000275
(SUMO-2)-RanGAP1 conjugate
-
pH 7.5, 30°C
-
0.0000018
SUMO-1 precursor
-
pH 7.5, 30°C
-
0.00000198
SUMO-2 precursor
-
pH 7.5, 30°C
-
additional information
additional information
-
enzyme-substrate complex formation kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.3
(SUMO-1)-RanGAP1 conjugate
Homo sapiens
-
pH 7.5, 30°C
-
18.2
(SUMO-2)-RanGAP1 conjugate
Homo sapiens
-
pH 7.5, 30°C
-
3.7
SUMO-1 precursor
Homo sapiens
-
pH 7.5, 30°C
-
0.075
SUMO-2 precursor
Homo sapiens
-
pH 7.5, 30°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0218
(2Z)-3-(naphthalen-2-yl)-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]prop-2-enamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00118 - 0.00354
2-(4-chlorophenyl)-2-oxoethyl 4-(benzoylamino)benzoate
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-diethoxybenzoyl)amino]benzoate
Homo sapiens
Q5W0Q7
above, pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-dimethoxybenzoyl)amino]benzoate
Homo sapiens
Q5W0Q7
above, pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-aminobenzoyl)amino]benzoate
Homo sapiens
Q5W0Q7
above, pH and temperature not specified in the publication
0.00174
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-fluorobenzoyl)amino]benzoate
Homo sapiens
Q5W0Q7
pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-hydroxybenzoyl)amino]benzoate
Homo sapiens
Q5W0Q7
above, pH and temperature not specified in the publication
0.00186 - 0.00239
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-methoxybenzoyl)amino]benzoate
0.00108
2-(4-chlorophenyl)-2-oxoethyl 4-[[3-(benzyloxy)benzoyl]amino]benzoate
Homo sapiens
Q5W0Q7
pH and temperature not specified in the publication
0.1
3-[(acetyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1
3-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1
4-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0092
benzyl (3-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0155
benzyl (4-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0212
naphthalen-2-yl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]sulfamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [[1-(2-hydroxyethyl)-2-oxo-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0272
phenyl [[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [[2-oxo-1-(4-oxobutyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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enzyme SENP1 levels are positively correlated with substrate Pin1 levels in human breast cancer specimens
Manually annotated by BRENDA team
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the enzyme expression is deregulated in cancers
Manually annotated by BRENDA team
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metastatic neuroblastoma tissue
Manually annotated by BRENDA team
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enzyme SENP1 is upregulated in pancreatic ductal adenocarcinoma tissues compared with adjacent normal tissues
Manually annotated by BRENDA team
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SENP1 modulates prostate epithelial cell proliferation
Manually annotated by BRENDA team
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elevation of SENP1 mRNA in prostate cancer cells as compared with normal prostate epithelial cells
Manually annotated by BRENDA team
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highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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in the crystal structure of human SENP1 complexed with unprocessed SUMO1, PDB: 2IY1, the catalytic Cys603 is located in a cleft which, upon substrate binding, closes to form a channel-like structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sumoylation
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SENP1 is itself a target for SUMO-1 modification but that this modification is normally rapidly reversed by an autocatalytic activity removing the SUMO-1, with little of the modified form accumulating. In the mutant SENP1 (C603S), the absence of proteolytic activity resulted in the detection of the conjugated form
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of the human SENP1 catalytic domain are obtained at room temperature by hanging-drop vapour diffusion. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation is noted. This is assigned as Co2+, an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggest that Co2+ has been overlooked and rerefinement support this conclusion. Highthroughput automated re-refinement protocols also failed to mark the Co2+ position
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SENP1 crystallization is performed at 20°C using a sitting drop vapour-diffusion method. Single diamond-shaped crystals are grown after 2 days from equal volumes of protein solution (20 mg/ml in 20 mM Tris/HCl, pH 8.0, and 50 mM NaCl) and reservoir solution containing 100 mM CoCl2, 0.1 M Mes, pH 6.5, and 1.8 M (NH4)2SO4. The structure of SENP1 is determined to 2.45 A. NaBH4 is used to trap a stable thiohemiacetal transition-state analogue between Cys602 of SENP1 and Gly92 of SUMO-2, determination of the structure of this complex to 3.2 A. Crystallization and structure determination of the SENP1-SUMO-2 complex
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X-ray structure of SENP1CC603S-SUMO-1 complex at 2.8 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged catalytic domain SENP1c, aa419-aa643 from Escherichia coli strain BL21 by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the His-tagged catalytic domain of SENP1, SENP1c, aa419-aa643, from PC-3 cell cDNA library, cloned into pET28a(+) vector, and expressed in Escherichia coli strain BL21
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crystallization of a complex of SENP1 C603A bound to full-length SUMO-1 and determination of the structure by X-ray crystallography. Two structures of SENP1 C603A in complex with the SUMO-1 precursor and RanGAP1-SUMO-1
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expression as N-terminally His-tagged enzyme in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli BL21
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expression of GFP-tagged SENP2 in HeLa cells
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expression of wild-type and mutant enzymes in MEF, 293T, and 3T3-L1 cells, real-time quantitative PCR expression analysis
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gene SP1, recombinant expression of GFP-tagged or untagged SENP1 and the catalytically dead enzyme mutant transiently in HeLa cells
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overexpression of a catalytically inactive/dominant negative Cys-to-Ser SENP1 mutant
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quantitative real-time PCR expression analysis
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recombinant expression of wild-type Flag-tagged C13orf22l and C13orf22lcat mutant comprising amino acid residues 312-649 in HeLa cells
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recombinant expression of YFP-tagged enzyme USPL1 in HeLa cell nucleoplasm, and of HA-tagged enzyme in Cajal bodies, co-expression with suicide inhibitor Strep-TEV-HA-SUMO-vinylmethylester, recombinant expression of truncated enzyme variant USPL1cat as His-GST-TEV-USPL1cat
SENP1, recombinant expression of wild-type and mutant enzymes
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the catalytic core domain of SENP1 (amino acids 415-643) and mutants are cloned into the vector pEHISTEV and expressed as a N-terminally His-tagged protein. The recombinant proteins are expressed in Escherichia coli Bl21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cadmium induces SENP1 expression in LNCaP cells
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enzyme SENP1 silencing by expression of siRNA
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human prostate cancer patients show elevated mRNA levels of SENP1
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IL-6 induces SENP1 mRNA expression in Hep3B cells
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SENP1 expression can be induced by hypoxia. Induction of SENP1 expression is mediated by hypoxia-inducible factor HIF-1alpha
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SENP1 levels are influenced by the presence of nucleoporin Nup153
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C236S
site-directed mutagenesis, the mutant is not inhibited by suicide inhibitor Strep-TEV-HA-SUMO-vinylmethylester in contrast to the wild-type enzyme
C602A
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completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
C603A
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the mutant is unable to desumoylate the (SUMO-1)-homeodomain-interacting protein kinase 2 conjugate
D441A
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mutant protein is indistinguishable from that of the wild-type protein in both processing and deconjugation
D468A
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mutated protein is only slightly impaired in processing and not at all in deconjugation
D550A
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completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
F496A
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altered protein retains significant levels of deconjugation activity
H529A
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altered protein retains significant levels of deconjugation activity
H533A
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completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
Q596A
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mutant of SENP1 is severely impaired in both deconjugation and processing
R511A
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mutant has reduced activity, but is unaffected in deconjugation
V532A
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mutation has no effect on either deconjugation or processing
W229L
site-directed mutagenesis, mutation to the residue found in USP2 and other ubiquitin-specific USPs dramatically impairs SUMO binding and cleavage
W237F
site-directed mutagenesis, mutation to the residue found in USP2 and other ubiquitin-specific USPs dramatically impairs SUMO binding and cleavage
W512A
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mutant has a reduced deconjugation activity in vitro, its deconjugation activity in vivo is only impaired to a small extent
C599S
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site-directed mutagenesis, the active site mutant precipitates SUMO1ylated proteins but not SUMO2/3-modified substrate
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
drug development
medicine