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Information on EC 3.1.2.12 - S-formylglutathione hydrolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40363
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3.1.2.12 S-formylglutathione hydrolaseIUBMB Comments
Also hydrolyses S-acetylglutathione, but more slowly.
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Word Map
- 3.1.2.12
- lymphocyte
- esterases
- retinoblastoma
- ctl
- granule
- phosphoglucomutase
-
cytolytic
-
killer
-
francisco
- glyoxalase
- perforin
- carboxylesterase
-
granzyme
- 6-phosphogluconate
- haptoglobin
- fluorophosphate
- pmsf
- dfp
-
diisopropyl
-
bloodstain
-
organophosphate
-
thiobenzyl
- cutinase
- lymphokine
- phenylalanyl-trna
-
3.1.1.1
- diisopropylfluorophosphate
-
g-x-s-x-g
- paraoxon
-
perforin-mediated
-
lymphokine-activated
- analysis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Deubiquitinating enzyme 12
-
-
-
-
FGH
-
-
-
-
hydrolase, S-formylglutathione
-
-
-
-
Ubiquitin thiolesterase 12
-
-
-
-
Ubiquitin-specific processing protease 12
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
S-formylglutathione hydrolase
Also hydrolyses S-acetylglutathione, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY
50812-21-0
-
83380-83-0
the former number 50812-21-0 has been deleted
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-methylumbelliferyl acetate + H2O
4-methylumbelliferone + acetate
-
very low activity
-
?
carboxyfluorescein diacetate + H2O
carboxyfluorescein + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
very low activity
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.054
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.1
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.14
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.15
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.19
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.23
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.34
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.4
4-nitrophenyl acetate
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.9
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
2.6
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.012
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.018
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.019
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.03
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.04
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.09
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.12
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.13
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.14
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.19
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.2
4-nitrophenyl butyrate
Km less than 0.2 mM, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.25
S-Lactoylglutathione
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
2.6
4-nitrophenyl acetate
-
mutant H160I oxidized form with catalase, pH 7.4, 22°C
3.5
4-nitrophenyl acetate
-
mutant H160I oxidized form, pH 7.4, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0055
4-nitrophenyl acetate
mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.028
4-nitrophenyl acetate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.1
4-nitrophenyl acetate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.32
4-nitrophenyl acetate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.525
4-nitrophenyl acetate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.76
4-nitrophenyl acetate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.97
4-nitrophenyl acetate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.05
4-nitrophenyl acetate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.5
4-nitrophenyl acetate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.53
4-nitrophenyl acetate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.8
4-nitrophenyl acetate
Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.003
4-nitrophenyl butyrate
mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.0165
4-nitrophenyl butyrate
kcat less than 0.0165 s-1, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.04
4-nitrophenyl butyrate
mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.078
4-nitrophenyl butyrate
mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.2
4-nitrophenyl butyrate
wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
0.43
4-nitrophenyl butyrate
mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.23
4-nitrophenyl butyrate
mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.65
4-nitrophenyl butyrate
mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.92
4-nitrophenyl butyrate
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
1.97
4-nitrophenyl butyrate
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
3.63
4-nitrophenyl butyrate
mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
50
S-Lactoylglutathione
mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
116.7
S-Lactoylglutathione
mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C
2.8
4-nitrophenyl acetate
-
mutant H160I oxidized form with catalase, pH 7.4, 22°C
3.1
4-nitrophenyl acetate
-
mutant H160I oxidized form, pH 7.4, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
4-nitrophenyl acetate
-
mutant H160I oxidized form, pH 7.4, 22°C
1.16
4-nitrophenyl acetate
-
mutant H160I oxidized form with catalase, pH 7.4, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8
peroxide
-
wild-type, 22°C, pH 7.4, in the presence of substrate, inactivation is 10fold faster
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
the wild type enzyme crystallizes as a dimer of dimers with four molecules in the asymmetric unit, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
M162H/C60S/W197I
mutant shows significantly decreased activity
W197I
the substitution enhances SFGH reactivity with paraoxon by more than 1000fold thereby overcoming natural organophosphate resistance, the mutant increases the rate of organophosphate inhibition under pseudo-first-order conditions but does not accelerate organophosphate hydrolysis
C60A
-
Km and kcat(4-nitrophenyl acetate) slightly decreased compared to wild-type
C60S
-
Km and kcat(4-nitrophenyl acetate) slightly decreased compared to wild-type. mutant is not inactivated by peroxide
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
N64A
-
Km (4-nitrophenyl acetate) slightly increased and kcat (4-nitrophenyl acetate) slightly decreased compared to wild-type
W197I
-
Km (4-nitrophenyl acetate) decreased and kcat (4-nitrophenyl acetate) 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
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Degrassi, G.; Uotila, L.; Klima, R.; Venturi, V.
Purification and properties of an esterase from the yeast Saccharomyces cerevisiae and identification of the encoding gene
Appl. Environ. Microbiol.
65
3470-3472
1999
Saccharomyces cerevisiae
Legler, P.M.; Kumaran, D.; Swaminathan, S.; Studier, F.W.; Millard, C.B.
Structural characterization and reversal of the natural organophosphate resistance of a D-type esterase, Saccharomyces cerevisiae S-formylglutathione hydrolase
Biochemistry
47
9592-9601
2008
Saccharomyces cerevisiae (P40363), Saccharomyces cerevisiae
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