BRENDA - Enzyme Database show
show all sequences of 2.1.1.11

S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase from Rhodobacter capsulatus: mechanistic insights and stimulation with phospholipids

Sawicki, A.; Willows, R.D.; Biochem. J. 406, 469-478 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Phospholipids
increase enzymatic activity 3-4fold
Rhodobacter capsulatus
Cloned(Commentary)
Commentary
Organism
derived from plasmid pRPS404, consisting of a 46 kb pair section of the photosynthetic gene cluster, overexpression of His6-tagged protein in Escherichia coli, strain BL21DE3, expression plasmid pHisBchM
Rhodobacter capsulatus
General Stability
General Stability
Organism
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms
Rhodobacter capsulatus
Inhibitors
Inhibitors
Commentary
Organism
Structure
cobalt II-protoporphyrin
non-substrate metalloporphyrin, competitive, assay described
Rhodobacter capsulatus
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition
Rhodobacter capsulatus
manganese III-protoporphyrin
non-substrate metalloporphyrin, non-competitive or un-competitive, assay described
Rhodobacter capsulatus
additional information
higher magnesium ion concentrations above 3.8 mM inhibit enzyme activity in presence or absence of magnesium-chelatase subunits or BSA
Rhodobacter capsulatus
S-adenosyl-L-homocysteine
non-competitive product inhibition
Rhodobacter capsulatus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
magnesium deuteroporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.0008
-
zinc protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.001
-
magnesium mesoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.045
-
S-adenosyl-L-methionine
previously determined constant
Rhodobacter capsulatus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
His6-tagged protein, gel filtration, SDS-PAGE
Rhodobacter capsulatus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + magnesium mesoporphyrin
Rhodobacter capsulatus
-
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter capsulatus
P26236
-
-
Purification (Commentary)
Commentary
Organism
from inclusion bodies, gel filtration and SDS-PAGE
Rhodobacter capsulatus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Rhodobacter capsulatus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
effect of detergents and alcohols on activity analyzed, no stimulatory effect by magnesium-chelatase subunits, heat-stable stimulatory component present in S-adenosyl-L-methionine synthetase found to be a phospholipid, kinetic analysis shows a random sequential reaction mechanism
Rhodobacter capsulatus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + magnesium deuteroporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
-
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + zinc protoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
disaggregation to lower molecular mass forms, monomeric to multimeric species, gel filtration
Rhodobacter capsulatus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodobacter capsulatus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.003
-
magnesium deuteroporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.018
-
zinc protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.04
-
magnesium protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
slight preference for Tris/HCl buffer over Tricine/NaOH
Rhodobacter capsulatus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.5
8.5
within activity range
Rhodobacter capsulatus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00045
-
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition, magnesium deuteroporphyrin as substrate
Rhodobacter capsulatus
0.00061
-
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition, S-adenosyl-L-methionine as substrate
Rhodobacter capsulatus
0.121
-
S-adenosyl-L-homocysteine
non-competitive, magnesium protoporphyrin as substrate
Rhodobacter capsulatus
0.141
-
S-adenosyl-L-homocysteine
non-competitive, S-adenosyl-L-methionine as substrate
Rhodobacter capsulatus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Phospholipids
increase enzymatic activity 3-4fold
Rhodobacter capsulatus
Cloned(Commentary) (protein specific)
Commentary
Organism
derived from plasmid pRPS404, consisting of a 46 kb pair section of the photosynthetic gene cluster, overexpression of His6-tagged protein in Escherichia coli, strain BL21DE3, expression plasmid pHisBchM
Rhodobacter capsulatus
General Stability (protein specific)
General Stability
Organism
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms
Rhodobacter capsulatus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
cobalt II-protoporphyrin
non-substrate metalloporphyrin, competitive, assay described
Rhodobacter capsulatus
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition
Rhodobacter capsulatus
manganese III-protoporphyrin
non-substrate metalloporphyrin, non-competitive or un-competitive, assay described
Rhodobacter capsulatus
additional information
higher magnesium ion concentrations above 3.8 mM inhibit enzyme activity in presence or absence of magnesium-chelatase subunits or BSA
Rhodobacter capsulatus
S-adenosyl-L-homocysteine
non-competitive product inhibition
Rhodobacter capsulatus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00045
-
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition, magnesium deuteroporphyrin as substrate
Rhodobacter capsulatus
0.00061
-
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition, S-adenosyl-L-methionine as substrate
Rhodobacter capsulatus
0.121
-
S-adenosyl-L-homocysteine
non-competitive, magnesium protoporphyrin as substrate
Rhodobacter capsulatus
0.141
-
S-adenosyl-L-homocysteine
non-competitive, S-adenosyl-L-methionine as substrate
Rhodobacter capsulatus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
magnesium deuteroporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.0008
-
zinc protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.001
-
magnesium mesoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.045
-
S-adenosyl-L-methionine
previously determined constant
Rhodobacter capsulatus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
29000
-
His6-tagged protein, gel filtration, SDS-PAGE
Rhodobacter capsulatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + magnesium mesoporphyrin
Rhodobacter capsulatus
-
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
from inclusion bodies, gel filtration and SDS-PAGE
Rhodobacter capsulatus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Rhodobacter capsulatus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
effect of detergents and alcohols on activity analyzed, no stimulatory effect by magnesium-chelatase subunits, heat-stable stimulatory component present in S-adenosyl-L-methionine synthetase found to be a phospholipid, kinetic analysis shows a random sequential reaction mechanism
Rhodobacter capsulatus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + magnesium deuteroporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
-
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + zinc protoporphyrin
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
684982
Rhodobacter capsulatus
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
disaggregation to lower molecular mass forms, monomeric to multimeric species, gel filtration
Rhodobacter capsulatus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Rhodobacter capsulatus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.003
-
magnesium deuteroporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.018
-
zinc protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
0.04
-
magnesium protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
Rhodobacter capsulatus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
slight preference for Tris/HCl buffer over Tricine/NaOH
Rhodobacter capsulatus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.5
8.5
within activity range
Rhodobacter capsulatus
Other publictions for EC 2.1.1.11
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)
734272
Chen
Structural insights into the c ...
Synechocystis sp.
J. Biol. Chem.
289
25690-25698
2014
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1
1
5
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1
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734560
Tomiyama
Mg-chelatase I subunit 1 and M ...
Arabidopsis thaliana
J. Plant Res.
127
553-563
2014
-
-
-
-
-
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2
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1
1
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720712
Meinecke
Chlorophyll-deficient mutants ...
Chlamydomonas reinhardtii
Plant Mol. Biol.
72
643-658
2010
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1
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1
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3
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695554
McLean
An enzyme-coupled continuous s ...
Synechocystis sp. PCC 6803
Anal. Biochem.
394
223-228
2009
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1
1
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2
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1
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2
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1
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1
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700486
Van Wilder
C1 metabolism and chlorophyll ...
Arabidopsis thaliana, Pisum sativum
New Phytol.
182
137-145
2009
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1
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2
2
2
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4
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687761
Johnson
Characterization of three homo ...
Chlorobaculum tepidum
J. Biol. Chem.
283
27776-27784
2008
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674841
Pontier
Knock-out of the magnesium pro ...
Arabidopsis thaliana
J. Biol. Chem.
282
2297-2304
2007
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684982
Sawicki
S-adenosyl-L-methionine:magnes ...
Rhodobacter capsulatus
Biochem. J.
406
469-478
2007
1
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1
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1
5
4
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1
1
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1
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660178
Alawady
Tobacco Mg protoporphyrin IX m ...
Nicotiana tabacum
Plant J.
41
282-290
2005
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660202
Alawady
Cloning and expression of the ...
Nicotiana tabacum
Plant Mol. Biol.
57
679-691
2005
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661705
Shepherd
Kinetic basis for linking the ...
Synechocystis sp.
FEBS J.
272
4532-4539
2005
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657843
Shepherd
Transient kinetics of the reac ...
Synechocystis sp. PCC 6803
Biochem. J.
382
1009-1013
2004
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485113
Shepherd
Purification and kinetic chara ...
Synechocystis sp., Synechocystis sp. PCC 6803
Biochem. J.
371
351-360
2003
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485108
Block
The plant S-adenosyl-L-methion ...
Arabidopsis thaliana, Spinacia oleracea
Eur. J. Biochem.
269
240-248
2002
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485111
Averina
Native state, energetic intera ...
Hordeum vulgare
Indian J. Exp. Biol.
40
192-201
2002
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485112
Vothknecht
-
Sinefungin inhibits chlorophyl ...
Hordeum vulgare
Plant Physiol. Biochem.
33
759-763
1995
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485109
Gibson
The bacteriochlorophyll biosyn ...
Rhodobacter sphaeroides
FEBS Lett.
352
127-130
1994
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485110
Bollivar
Heterologous expression of the ...
Rhodobacter capsulatus
J. Bacteriol.
176
5290-5296
1994
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485102
Yee
Confirmation of a ping-pong me ...
Triticum aestivum
Biochem. Biophys. Res. Commun.
162
483-490
1989
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485104
Hinchigeri
-
The reaction mechanism of S-ad ...
Euglena gracilis
Photosynthetica
18
168-178
1984
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485103
Hinchigeri
-
The purification and reaction ...
Rhodobacter sphaeroides
Photosynthetica
16
554-560
1982
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485106
Hinchigeri
-
Purification of S-adenosyl-L-m ...
Hordeum vulgare
Photosynthetica
15
351-359
1981
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485107
Ellsworth
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Biosynthesis and inhibition of ...
Triticum aestivum
Photosynthetica
10
291-301
1976
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485105
Ellsworth
Activity and properties of (-) ...
Triticum aestivum
Biochim. Biophys. Acta
268
327-333
1972
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485101
Gibson
Studies on the biosynthesis of ...
Rhodobacter sphaeroides
Biochem. J.
88
325-334
1963
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