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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Escherichia coli and UniProt Accession P0A9D2
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2.5.1.18 glutathione transferaseIUBMB Comments
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
-
-
-
-
glutathione S-transferase X
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aryl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
RX:glutathione R-transferase
A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY
50812-37-8
-
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
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)-glutathione + HCl
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
1-chloro-2,4-dinitrobenzene + GSH
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
-
?
additional information
?
-
-
bacterial enzyme represents a defence against the effects of antibiotics
-
-
?
additional information
?
-
-
YghU from Escherichia coli binds two molecules of GSH in each active site. YghU exhibits little or no GSH transferase activity with most typical electrophilic substrates but does possess a modest catalytic activity toward several organic hydroperoxides. The enzyme also exhibits disulfide-bond reductase activity towards 2-hydroxyethyl disulfide
-
-
?
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
additional information
?
-
-
bacterial enzyme represents a defence against the effects of antibiotics
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
1-chloro-2,4-dinitrobenzene
mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
1.9
1-chloro-2,4-dinitrobenzene
wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)
2.1
1-chloro-2,4-dinitrobenzene
mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)
4.3
1-chloro-2,4-dinitrobenzene
mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
4.4
1-chloro-2,4-dinitrobenzene
mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)
0.05
glutathione
mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)
0.3
glutathione
wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)
1.4
glutathione
mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
1.9
glutathione
mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)
2.5
glutathione
mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
1-chloro-2,4-dinitrobenzene
mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
1.6
1-chloro-2,4-dinitrobenzene
mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)
4.8
1-chloro-2,4-dinitrobenzene
mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)
9.1
1-chloro-2,4-dinitrobenzene
wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)
55.8
1-chloro-2,4-dinitrobenzene
mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
0.3
glutathione
mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)
1.1
glutathione
mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
6.8
glutathione
mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)
7.7
glutathione
wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)
41
glutathione
mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
structures and properties of YghU and YfcG indicate that they are members of the same distinct subfamily of GSH transferase homologues, proposed to be called the Nu-class GSH transferases. Cytoscape cluster analysis of the GSH transferase superfamily, overvew
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant YghU, hanging-drop vapor diffusion method, YghU at 20 mg/ml in 30 mM NaH2PO4, pH 7.0, 1 mM DTT, and 20 mM GSH, is mixed with an equal volume of reservoir solution containing 0.1 M Bis-Tris, 0.2 M NaCl, pH 5.5, 25% w/v PEG 3350, 25°C, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C10A
shows a 5 or 6fold higher kcat than wild type for both glutathione and 1-chloro-2,4-dinitrobenzene, accompanied by an 8fold increase in the Km for glutathione
C10S
shows a 25fold lower kcat for glutathione H and 5fold lower kcat for 1-chloro-2,4-dinitrobenzene than wild type accompanied by a 6fold decrease in the Km for glutathione
H106A
shows clearly decreased activity compared to the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant YghU from strain BL21(DE3) by anion and cation exchange chromatography and dialysis
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene yghU, expression in Escherichia coli strain BL21(DE3), expression of the selenomethionine YghU derivative in Escherichia coli strain B834 DE3
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Piccolomini, R.; Di Ilio, C.; Aceto, A.; Allocati, N.; Faraone, A.; Cellini, L.; Ravagnan, G.; Federici, G.
Glutathione transferase in bacteria: subunit composition and antigenic characterization
J. Gen. Microbiol.
135
3119-3125
1989
Enterobacter cloacae, Escherichia coli, Klebsiella oxytoca, Proteus mirabilis, Proteus vulgaris, Pseudomonas aeruginosa, Serratia marcescens, Proteus vulgaris ATCC 8427, Serratia marcescens CIP 6755, Enterobacter cloacae CIP 6085, Proteus mirabilis AF 2924
Wang, X.Y.; Zhang, Z.R.; Perrett, S.
Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys10 and His106
Biochem. J.
417
55-64
2008
Escherichia coli (P0A9D2), Escherichia coli
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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