Information on EC 3.1.2.12 - S-formylglutathione hydrolase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.2.12
-
RECOMMENDED NAME
GeneOntology No.
S-formylglutathione hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-formylglutathione + H2O = glutathione + formate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
formaldehyde oxidation II (glutathione-dependent)
-
-
formaldehyde oxidation
-
-
Methane metabolism
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
S-formylglutathione hydrolase
Also hydrolyses S-acetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-21-0
-
83380-83-0
the former number 50812-21-0 has been deleted
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 enzymes FrmB and YeiG, encoded by genes frmB or yaiM, and yeiG
-
-
Manually annotated by BRENDA team
grown in presence of formaldehyde
-
-
Manually annotated by BRENDA team
Kloeckera sp.
No.2201, grown in presence of methanol
-
-
Manually annotated by BRENDA team
IFP 206
-
-
Manually annotated by BRENDA team
Lota maculosa
burbot
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
the enzyme is bifunctional with the formaldehyde dehydrogenase activity downstream of the S-formylglutathione hydrolase activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
grown in presence of formaldehyde
-
-
Manually annotated by BRENDA team
i.e. Sterkiella histriomuscorum, gene FSF1, the enzyme is bifunctional with the formaldehyde dehydrogenase activity upstream of the S-formylglutathione hydrolase activity
SwissProt
Manually annotated by BRENDA team
the enzyme is bifunctional with the formaldehyde dehydrogenase activity and the S-formylglutathione hydrolase activity located at different sites
-
-
Manually annotated by BRENDA team
the enzyme is bifunctional with the formaldehyde dehydrogenase activity downstream of the S-formylglutathione hydrolase activity
-
-
Manually annotated by BRENDA team
Torulopsis pinus
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
4-methyl-2-oxo-2H-chromen-7-yl (2E)-but-2-enoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3,3-dimethylbutanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-cyclopentylpropanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbut-2-enoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbutanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl 3-phenoxybutanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl acetate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl butyrate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl cyclopentanecarboxylate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl heptanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl hexanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl pentanoate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl pivalate + H2O
?
show the reaction diagram
-
-
-
?
4-methyl-2-oxo-2H-chromen-7-yl propionate + H2O
?
show the reaction diagram
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferol + acetate
show the reaction diagram
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
show the reaction diagram
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
4-nitrophenyl acetate + H2O
4-nitrophenol + formate
show the reaction diagram
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
show the reaction diagram
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
4-nitrophenyl thioacetate + H2O
4-nitrophenol + thioacetate
show the reaction diagram
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
show the reaction diagram
alpha-naphthyl butyrate + H2O
alpha-naphthol + butyrate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl propionate + H2O
alpha-naphthol + propionate
show the reaction diagram
-
-
-
-
?
beta-naphthyl acetate + H2O
beta-naphthol + acetate
show the reaction diagram
-
-
-
?
carboxyfluorescein diacetate + H2O
carboxyfluorescein + acetate
show the reaction diagram
-
-
-
?
fluorescein diacetate + H2O
?
show the reaction diagram
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
paraoxon + H2O
?
show the reaction diagram
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
show the reaction diagram
S-formylglutathione + H2O
?
show the reaction diagram
S-formylglutathione + H2O
glutathione + formate
show the reaction diagram
S-lactoylglutathione + H2O
glutathione + lactate
show the reaction diagram
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
S-formylglutathione + H2O
?
show the reaction diagram
S-formylglutathione + H2O
glutathione + formate
show the reaction diagram
additional information
?
-
-
esterase D/S-formylglutathione hydrolase plays a key role in glutathione-dependent detoxification of endogenously formed formaldehyde as well as in hydrolysis of various xenobiotics
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11-([5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl]amino)undecyl methylphosphonofluoridoate
-
-
2,4,6-Trinitrobenzene sulfonate
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-
5,5'-dithiobis(2-nitrobenzoate)
arsenite
ascorbate
-
-
CaCl2
-
-
Co2+
-
-
CuSO4
DTNB
-
48% inhibition at 0.001 mM
FeSO4
Kloeckera sp.
-
-
folate
-
-
glutathione
Hg2+
susceptible to inhibition by Hg2+
HgCl2
iodoacetamide
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-
iodoacetate
N-ethylmaleimide
p-chloromercuribenzoate
Kloeckera sp.
-
-
p-hydroxymercuribenzoate
PMSF
-
inhibition of wild-type YeiG and YeiG mutants C54A and C26A
sarin
-
strong inhibition at 0.0008 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
4-methyl-2-oxo-2H-chromen-7-yl (2E)-but-2-enoate
-
0.09
4-methyl-2-oxo-2H-chromen-7-yl 3,3-dimethylbutanoate
-
0.05
4-methyl-2-oxo-2H-chromen-7-yl 3-cyclopentylpropanoate
-
0.06
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbut-2-enoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl 3-methylbutanoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl 3-phenoxybutanoate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl acetate
-
0.07
4-methyl-2-oxo-2H-chromen-7-yl butyrate
-
0.04
4-methyl-2-oxo-2H-chromen-7-yl cyclopentanecarboxylate
-
0.04
4-methyl-2-oxo-2H-chromen-7-yl heptanoate
-
0.09
4-methyl-2-oxo-2H-chromen-7-yl hexanoate
-
0.05
4-methyl-2-oxo-2H-chromen-7-yl pentanoate
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0.1
4-methyl-2-oxo-2H-chromen-7-yl pivalate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl propionate
-
0.013 - 3.5
4-nitrophenyl acetate
0.012 - 0.7
4-nitrophenyl butyrate
0.02 - 0.95
4-nitrophenyl caproate
0.05 - 0.83
4-nitrophenyl propionate
0.019 - 0.12
4-yethylumbelliferyl acetate
0.54 - 1.3
Alpha-naphthyl acetate
0.35
alpha-naphthyl propionate
-
in Tris-HCl buffer, pH 8.0
0.54
beta-naphthyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.03
fluorescein diacetate
-
recombinant enzyme, pH 7.2, 37°C
0.44
naphthalen-1-yl n-butanoate
-
in Tris-HCl buffer, pH 8.0
0.49
p-nitrophenyl acetate
-
-
0.12 - 0.15
S-acetylglutathione
0.077 - 0.43
S-formylglutathione
0.58 - 3
S-Lactoylglutathione
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0055 - 3.1
4-nitrophenyl acetate
0.003 - 4.48
4-nitrophenyl butyrate
0.49 - 0.67
4-nitrophenyl caproate
0.14 - 1.84
4-nitrophenyl propionate
2.17 - 5.12
Alpha-naphthyl acetate
1.9
alpha-naphthyl propionate
-
in Tris-HCl buffer, pH 8.0
1.73
naphthalen-1-yl n-butanoate
-
in Tris-HCl buffer, pH 8.0
6.51 - 28.5
S-formylglutathione
0.05 - 116.7
S-Lactoylglutathione
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 20
4-nitrophenyl acetate
40.8
4-nitrophenyl butyrate
-
in Tris-HCl buffer, pH 8.0
39.6
4-nitrophenyl caproate
-
in Tris-HCl buffer, pH 8.0
38.5
4-nitrophenyl propionate
-
in Tris-HCl buffer, pH 8.0
5.54
alpha-naphthyl propionate
-
in Tris-HCl buffer, pH 8.0
3.93
naphthalen-1-yl n-butanoate
-
in Tris-HCl buffer, pH 8.0
0.13 - 33.3
S-Lactoylglutathione
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
Cu2+
-
wild-type, 22°C, pH 7.4
8 - 12
peroxide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
-
recombinant enzyme, substrate fluorescein diacetate
0.14
-
-
0.32
-
skin
0.44
-
testis
0.49
-
rectum and lung
0.53
-
esophagus
0.54
-
white adipose tissue
0.9
-
brown adipose tissue
0.92
-
spleen
0.94
-
muscle
0.99
-
brain
1.15
-
small intestine
1.25
-
heart
1.3
-
recombinant enzyme, substrate beta-naphthyl acetate
1.6
-
colon
1.61
-
stomach
3.35
-
liver
4.02
-
kidney
4.86
-
recombinant enzyme, crude enzyme extract
5.7
-
recombinant enzyme, substrate 4-nitrophenyl acetate
10.4
-
recombinant enzyme, substrate S-formylglutathione
14.5
-
recombinant enzyme, substrate S-acetylglutathione
15.2
-
recombinant enzyme, substrate alpha-naphthyl acetate
26.9
Lota maculosa
-
-
36.3
-
recombinant enzyme, substrate 4-methylumbelliferyl acetate
38.2
-
-
3390
-
-
5800
-
-
additional information
-
substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
assay at
6.4 - 6.6
Kloeckera sp.
-
-
6.9 - 7.1
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-
7.6 - 8
-
optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
additional information
-
activation energy 4.5 cal/mol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
SFGH activity is increased during Botrytis infection
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
detection of recombinant GFP-fusion protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neisseria meningitidis serogroup B (strain MC58)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
1 * 25000 + 1 * 35000, SDS-PAGE
31000
Kloeckera sp.
-
2 * 31000 SDS-PAGE
31700
-
2 * 31700, recombinant enzyme, amino acid sequence calculation without His-tag
32000
-
2 * 32000, SDS-PAGE
32586
-
x * 32586, recombinant His-tagged wild-type enzyme, mass spectrometry
33930
calculated from amino acid sequence
33934
1 * 33934, calculated from amino acid sequence
35000
-
1 * 25000 + 1 * 35000, SDS-PAGE
40000
-
gel filtration
52000
-
gel filtration
53000
-
gel filtration
58000
Kloeckera sp.
-
gel filtration
58200
-
calculation from sedimentation and diffusion coefficients
60000
-
gel filtration
61000 - 64000
-
gel filtration, sedimentation equilibrium centrifugation
66000
-
recombinant enzyme, gel filtration
67800
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the sitting drop-vapor diffusion technique, at 2 A resolution. Crystals belong to space group P1 with unit cell dimensions a = 66.43 A, b = 68.95 A, c = 95.65 A, alpha = 92.41, beta = 99.79, gamma = 98.43. Contacts between the two monomers in the dimer are formed both by hydrogen bonds and salt bridges
-
selenomethionine labelled recombinant enzyme, 30 mg/ml, hanging-drop vapor-diffusion method, 293K, precipitant solution: 16% PEG 4000, 0.2 M magnesium acetate, 0.2 M imidazole-malate, pH 6.5, 3% methanol, optimal crystals by microseeding, 1-5 d, production of selenomethionine-enzyme crystals is similar with 10% PEG 4000 and additional presence of 10 mM DTT, X-ray diffraction structure determination and analysis at 1.84 A resolution
-
by the hanging drop vapor diffusion technique, to 2.2 A resolution. Crystals belong to space group P212121 with unit cell dimensions of a = 49.49 A, b = 129.75 A, c = 152.67 A, with 4 molecules per asymmetric unit
-
sitting drop vapour diffusion method, using 0.17 M ammonium acetate, 0.085 M sodium acetate trihydrate (pH 4.6), 25.5% (w/v) PEG 4000, and 15% (v/v) glycerol
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
70 min, 30% loss
80981
4.6 - 8.6
-
stable for 30 min at 20°C
80982
5 - 8
-
-
80987
7.2 - 7.6
Kloeckera sp.
-
5°C, stable for 4 d
80985
10.4
-
unstable at
80981
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
unstable
45
Kloeckera sp.
-
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stabilization by 2-mercaptoethanol or dithiothreitol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the wild type enzyme is sensitive to oxidation
691005
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
Kloeckera sp.
-
-20°C, 50% glycerol, 6 months
-
-70°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
recombinant from overexpressing Escherichia coli BL21(DE3) as His-tagged enzyme
-
recombinant His-tagged enzyme from Escherichia coli
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel chelate affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography
-
to homogeneity by a single-step Ni2+ affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, alignment of sequences and domains of several species
DNA and amino acid sequence determinationand analysis, expression in Escherichia coli as C-terminally His-tagged enzyme
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expression as His-tagged enzyme in Escherichia coli BL21(DE3), production of a selenomethionine labelled enzyme in a methionine auxotrophic strain
-
expression in Escherichia coli
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli and in Arabidopsis thaliana protoplasts
-
gene fgh1, DNA and amino acid sequence determination and analysis, expression in DH5alpha, expression as GFP-fusion protein in Candida boidinii
-
genes frmB or yaiM, and yeiG, subcloning in strain DH5alpha, overexpression in strain BL21(DE3) of His-tagged wild-type and mutant enzymes
-
N-terminus His6-S-tagged protein from pET28a construct overexpressed in Escherichia coli strain BL21(DE3) under the control of the T7 RNA polymerase transcription system
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C54S
-
shows a 4fold decrease in alpha-naphthyl butyrate activity. Is insensitive to the inhibitor N-ethylmaleimide
S147A
-
is unable to hydrolyse alpha-naphthyl butyrate
S152A
-
site-directed mutagenesis, completely inactive mutant
C26A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
C54A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
D199A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
D218A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
D223A
-
site-directed mutagenesis, the YeiG mutant shows no esterase activity
D255A
-
site-directed mutagenesis, the YeiG mutant shows 2fold reduced activity compared to the wild-type enzyme
D80A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
S154A
-
site-directed mutagenesis, the YeiG mutant shows no esterase activity
C26A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
-
C54A
-
site-directed mutagenesis, the YeiG mutant shows wild-type activity
-
D199A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
-
D218A
-
site-directed mutagenesis, the YeiG mutant shows reduced activity compared to the wild-type enzyme
-
C60A
-
Km and kcat(4-nitrophenyl acetate) slightly decreased compared to wild-type
C60H/W197I
mutant shows significantly decreased activity
C60K/W197I
the mutation results in a further enhancement of the rates of phosphorylation with paraoxon but does not affect the dephosphorylation of the enzyme
C60Q/W197I
mutant shows significantly decreased activity
C60R/W197I
the mutation results in a further enhancement of the rates of phosphorylation with paraoxon but does not affect the dephosphorylation of the enzyme
C60S/W197I
mutant shows significantly decreased activity
G57H
mutant shows significantly decreased activity
H160I
-
Oxidation leads to activation of mutant enzyme. Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Oxidized form (with or without catalase): Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) increased compared to wild-type
H160S
-
Km (4-nitrophenyl acetate) slightly decreased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
L58H/W197I
mutant shows significantly decreased activity
M162H
mutant shows significantly decreased activity
M162H/C60S/W197I
mutant shows significantly decreased activity
N64A
-
Km (4-nitrophenyl acetate) slightly increased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
W197I/C60S
-
Km (4-nitrophenyl acetate) decreased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Km (S-lactolylglutathione) increased and kcat (4-nitrophenyl acetate) highly decreased compared to wild-type
W197I/H160I
-
Km (4-nitrophenyl acetate) increased and kcat (4-nitrophenyl acetate) decreased compared to wild-type. Km (S-lactolylglutathione) decreased and kcat (4-nitrophenyl acetate) highly decreased compared to wild-type
Y278F
-
Km (4-nitrophenyl acetate) slightly decreased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
identification of a carboxylesterase expressed in protoplasts using fluorescence-activated cell sorting
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