BRENDA - Enzyme Database
show all sequences of 1.8.3.7

Copper is a cofactor of the formylglycine-generating enzyme

Knop, M.; Dang, T.Q.; Jeschke, G.; Seebeck, F.P.; ChemBioChem 18, 161-165 (2017)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
C187A/C231A/C284S/C298A
the mutant shows increased activity compared to the wild type enzyme
Thermomonospora curvata
C274S
inactive
Thermomonospora curvata
C296S
inactive
Thermomonospora curvata
S266A
the mutant shows reduced activity compared to the wild type enzyme
Thermomonospora curvata
S290K
the mutant shows very low activity compared to the wild type enzyme
Thermomonospora curvata
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.23
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.52
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.58
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu+
required
Thermomonospora curvata
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermomonospora curvata
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol
-
742288
Thermomonospora curvata
?
-
-
-
?
additional information
low activity with Abz-SALSSPTRA-NH2
742288
Thermomonospora curvata
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0001
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.027
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.07
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C187A/C231A/C284S/C298A
the mutant shows increased activity compared to the wild type enzyme
Thermomonospora curvata
C274S
inactive
Thermomonospora curvata
C296S
inactive
Thermomonospora curvata
S266A
the mutant shows reduced activity compared to the wild type enzyme
Thermomonospora curvata
S290K
the mutant shows very low activity compared to the wild type enzyme
Thermomonospora curvata
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.23
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.52
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.58
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu+
required
Thermomonospora curvata
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol
-
742288
Thermomonospora curvata
?
-
-
-
?
additional information
low activity with Abz-SALSSPTRA-NH2
742288
Thermomonospora curvata
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0001
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.027
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.07
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00011
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S290K, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.00082
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.048
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.333
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00011
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S290K, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.00082
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant S266A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.048
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
wild type enzyme, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
0.333
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2
mutant C187A/C231A/C284S/C298A, at pH 8.0, temperature not specified in the publication
Thermomonospora curvata
Other publictions for EC 1.8.3.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740316
Knop M.; Dang
Copper is a Cofactor of the Fo ...
Thermomonospora curvata
ChemBioChem
18
161-165
2017
2
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4
4
741607
Meury
Structural basis for copper-o ...
Thermomonospora curvata
Angew. Chem. Int. Ed. Engl.
56
8115-8119
2017
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742288
Knop
Copper is a cofactor of the f ...
Thermomonospora curvata
ChemBioChem
18
161-165
2017
-
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5
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3
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1
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2
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3
-
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-
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4
4
742289
Knop
Mutation of conserved residue ...
Thermomonospora curvata
ChemBioChem
18
1755-1761
2017
-
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-
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6
-
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5
-
1
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1
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2
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2
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5
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6
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5
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1
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1
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2
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5
-
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-
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5
5
742923
Meshach Paul
Structural distortions due to ...
Homo sapiens
J. Biomol. Struct. Dyn.
FEHLT
1-11
2017
-
-
-
-
14
-
-
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1
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2
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1
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14
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1
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1
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-
-
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-
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1
1
-
-
-
740309
Knop
In Vitro Reconstitution of For ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis DSM 43465, Thermomonospora curvata, Thermomonospora curvata DSM 43183
ChemBioChem
16
2147-2150
2015
-
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2
1
1
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4
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6
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4
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2
3
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2
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1
1
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4
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4
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2
3
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-
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4
4
742496
Peng
Eukaryotic formylglycine-gene ...
Homo sapiens
FEBS J.
282
3262-3274
2015
1
-
1
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-
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1
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2
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1
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1
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1
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1
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1
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742873
Holder
Reconstitution of formylglyci ...
Homo sapiens, Streptomyces coelicolor
J. Biol. Chem.
290
15730-15745
2015
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2
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2
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2
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2
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2
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2
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2
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742435
Schlotawa
Rapid degradation of an activ ...
Homo sapiens
Eur. J. Hum. Genet.
21
1020-1023
2013
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1
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1
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1
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2
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1
1
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742852
Ennemann
Proprotein convertases proces ...
Homo sapiens
J. Biol. Chem.
288
5828-5839
2013
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3
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1
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740686
Carlson
Function and structure of a pr ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Streptomyces coelicolor, Streptomyces coelicolor M145
J. Biol. Chem.
283
20117-20125
2008
-
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2
1
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2
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8
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741881
Grove
In vitro characterization of ...
Klebsiella pneumoniae, Klebsiella pneumoniae ATCC 700721D
Biochemistry
47
7523-7538
2008
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1
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1
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742331
Bojarova
Sulfotransferases, sulfatases ...
Homo sapiens
Curr. Opin. Chem. Biol.
12
573-581
2008
-
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1
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1
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742481
Gande
Paralog of the formylglycine- ...
Homo sapiens
FEBS J.
275
1118-1130
2008
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742630
Schlotawa
Molecular analysis of SUMF1 m ...
Homo sapiens
Hum. Mutat.
29
205
2008
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2
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742833
Mariappan
The non-catalytic N-terminal ...
Homo sapiens
J. Biol. Chem.
283
11556-11564
2008
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742835
Carlson
Function and structure of a p ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471
J. Biol. Chem.
283
20117-20125
2008
-
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2
1
2
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2
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166
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2
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4
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2
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4
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742836
Mariappan
ERp44 mediates a thiol-indepe ...
Homo sapiens
J. Biol. Chem.
283
6375-6383
2008
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741508
Roeser
Probing the oxygen-binding si ...
Homo sapiens
Acta Crystallogr. Sect. D
63
621-627
2007
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1
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1
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2
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1
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743673
Roeser
A general binding mechanism f ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
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81-86
2006
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740284
Dierks
Molecular Basis or Multiple Su ...
Homo sapiens
Cell
121
541-552
2005
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742234
Dierks
Molecular basis for multiple ...
Homo sapiens
Cell
121
541-552
2005
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18
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742628
Takakusaki
Coexpression of formylglycine ...
Homo sapiens
Hum. Gene Ther.
16
929-936
2005
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Mariappan
Expression, localization, str ...
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15173-15179
2005
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742831
Dickmanns
Crystal structure of human pF ...
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280
15180-15187
2005
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740282
Dierks
Multiple sulfatase deficiency ...
Bos taurus
Cell
113
435-44
2003
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740283
Dierks
Multiple sulfatase deficiency ...
Homo sapiens
Cell
113
435-444
2003
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740770
Fey
Characterization of posttransl ...
Bos taurus
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276
47021-47028
2001
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