Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.2.12 - S-formylglutathione hydrolase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8LAS8

for references in articles please use BRENDA:EC3.1.2.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.12 S-formylglutathione hydrolase
IUBMB Comments
Also hydrolyses S-acetylglutathione, but more slowly.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8LAS8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
serine esterase, esterase d, fgh, sfgh, phest, s-formylglutathione hydrolase, atsfgh, s-formyl-glutathione hydrolase, atu1476, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-formyl-glutathione hydrolase
-
Deubiquitinating enzyme 12
-
-
-
-
esterase D
-
-
hydrolase, S-formylglutathione
-
-
-
-
serine esterase
-
-
Ubiquitin thiolesterase 12
-
-
-
-
Ubiquitin-specific processing protease 12
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-formylglutathione + H2O = glutathione + formate
show the reaction diagram
Cys59 and Ser152 are involved in catalysis
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
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
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
show the reaction diagram
-
-
-
?
beta-naphthyl acetate + H2O
beta-naphthol + acetate
show the reaction diagram
-
-
-
?
fluorescein diacetate + H2O
?
show the reaction diagram
-
-
-
?
S-acetylglutathione + H2O
glutathione + acetate
show the reaction diagram
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-formylglutathione + H2O
glutathione + formate
show the reaction diagram
-
-
-
?
S-formylglutathione + H2O
glutathione + formate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
90% reduced activity at 0.01 mM
DTNB
-
48% inhibition at 0.001 mM
glutathione
-
reversible disulfide formation at Cys59, regulatory function
iodoacetamide
-
-
N-ethylmaleimide
-
complete inhibition at 1 mM
p-hydroxymercuribenzoate
-
59% inhibition at 0.001 mM
Zn2+
-
50% reduced activity at 0.01 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
-
0.1
4-methyl-2-oxo-2H-chromen-7-yl pivalate
-
0.08
4-methyl-2-oxo-2H-chromen-7-yl propionate
-
1.02
4-nitrophenyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.087 - 0.12
4-yethylumbelliferyl acetate
0.57
Alpha-naphthyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.54
beta-naphthyl acetate
-
recombinant enzyme, pH 7.2, 37°C
0.03
fluorescein diacetate
-
recombinant enzyme, pH 7.2, 37°C
0.15
S-acetylglutathione
-
recombinant enzyme, pH 7.2, 37°C
0.13 - 0.318
S-formylglutathione
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
-
recombinant enzyme, substrate fluorescein diacetate
1.3
-
recombinant enzyme, substrate beta-naphthyl acetate
10.4
-
recombinant enzyme, substrate S-formylglutathione
14.5
-
recombinant enzyme, substrate S-acetylglutathione
15.2
-
recombinant enzyme, substrate alpha-naphthyl acetate
36.3
-
recombinant enzyme, substrate 4-methylumbelliferyl acetate
4.86
-
recombinant enzyme, crude enzyme extract
5.7
-
recombinant enzyme, substrate 4-nitrophenyl acetate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6 - 8
-
optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
SFGH activity is increased during Botrytis infection
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SFGH_ARATH
284
0
31656
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, about, recombinant enzyme, SDS-PAGE
31700
-
2 * 31700, recombinant enzyme, amino acid sequence calculation without His-tag
32586
-
x * 32586, recombinant His-tagged wild-type enzyme, mass spectrometry
66000
-
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S152A
-
site-directed mutagenesis, completely inactive mutant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
fully stable up to, rapid inactivation at higher temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determinationand analysis, expression in Escherichia coli as C-terminally His-tagged enzyme
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is upregulated at nematode infection
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
identification of a carboxylesterase expressed in protoplasts using fluorescence-activated cell sorting
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McAuley, K.E.; Cummins, I.; Papiz, M.; Edwards, R.; Fordham-Skelton, A.P.
Purification, crystallization and preliminary X-ray diffraction analysis of S-formylglutathione hydrolase from Arabidopsis thaliana: effects of pressure and selenomethionine substitution on space-group changes
Acta Crystallogr. Sect. D
59
2272-2274
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Kordic, S.; Cummins, I.; Edwards, R.
Cloning and characterization of an S-formylglutathione hydrolase from Arabidopsis thaliana
Arch. Biochem. Biophys.
399
232-238
2002
Arabidopsis thaliana
Manually annotated by BRENDA team
Haslam, R.; Rust, S.; Pallett, K.; Cole, D.; Coleman, J.
Cloning and characterisation of S-formylglutathione hydrolase from Arabidopsis thaliana: a pathway for formaldehyde detoxification
Plant Physiol. Biochem.
40
281-288
2002
Arabidopsis thaliana
-
Manually annotated by BRENDA team
Cummins, I.; McAuley, K.; Fordham-Skelton, A.; Schwoerer, R.; Steel, P.G.; Davis, B.G.; Edwards, R.
Unique regulation of the active site of the serine esterase S-formylglutathione hydrolase
J. Mol. Biol.
359
422-432
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Cummins, I.; Landrum, M.; Steel, P.G.; Edwards, R.
Structure activity studies with xenobiotic substrates using carboxylesterases isolated from Arabidopsis thaliana
Phytochemistry
68
811-818
2007
Arabidopsis thaliana (Q8LAS8), Arabidopsis thaliana
Manually annotated by BRENDA team
Cummins, I.; Steel, P.G.; Edwards, R.
Identification of a carboxylesterase expressed in protoplasts using fluorescence-activated cell sorting
Plant Biotechnol. J.
5
354-359
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Kaschani, F.; Gu, C.; Niessen, S.; Hoover, H.; Cravatt, B.F.; Van der Hoorn, R.A.
Diversity of serine hydrolase activities of unchallenged and Botrytis-infected Arabidopsis thaliana
Mol. Cell. Proteomics
8
1082-1093
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Huetten, M.; Geukes, M.; Misas-Villamil, J.C.; van der Hoorn, R.A.; Grundler, F.M.; Siddique, S.
Activity profiling reveals changes in the diversity and activity of proteins in Arabidopsis roots in response to nematode infection
Plant Physiol. Biochem.
97
36-43
2015
Arabidopsis thaliana (Q8LAS8)
Manually annotated by BRENDA team