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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Musca domestica and UniProt Accession Q9U795
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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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udp-glucuronosyltransferase
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methylation-specific
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organophosphate
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The taxonomic range for the selected organisms is: Musca domestica
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
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0067
1-chloro-2,4-dinitrobenzene
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
0.0084
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant R113A, pH and temperature not specified in the publication
0.0088
1-chloro-2,4-dinitrobenzene
recombinant detagged wild-type enzyme, pH and temperature not specified in the publication
0.0728
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant F108G, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.99
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant F108G, pH and temperature not specified in the publication
8
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant R113A, pH and temperature not specified in the publication
11.7
1-chloro-2,4-dinitrobenzene
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
25.1
1-chloro-2,4-dinitrobenzene
recombinant detagged wild-type enzyme, pH and temperature not specified in the publication
1.13
glutathione
mutant F108G, pH and temperature not specified in the publication
11
glutathione
mutant R113A, pH and temperature not specified in the publication
14
glutathione
wild-type enzyme, pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant F108G, pH and temperature not specified in the publication
0.95
1-chloro-2,4-dinitrobenzene
recombinant His-tagged mutant R113A, pH and temperature not specified in the publication
1.73
1-chloro-2,4-dinitrobenzene
recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mutation at Phe108, located just below Arg113 in the binding pocket, reduces the affinity and catalytic activity to both GSH and the electrophilic co-substrate, 1-chloro-2,4-dinitrobenzene
additional information
additional information
the substrate binding pocket of MdGST6B, involving Arg113 and Phe121 on helix 4, is narrower compared to other delta- and epsilon-class GSTs, structure, overview. The Arg113 hydrogen bond does not play a crucial role in catalysis
additional information
-
the substrate binding pocket of MdGST6B, involving Arg113 and Phe121 on helix 4, is narrower compared to other delta- and epsilon-class GSTs, structure, overview. The Arg113 hydrogen bond does not play a crucial role in catalysis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9U795_MUSDO
222
0
25025
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isozyme MdGST6B shows typical GST folding comprised of N-terminal and C-terminal domains
additional information
-
isozyme MdGST6B shows typical GST folding comprised of N-terminal and C-terminal domains
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged isozyme MdGST6B complexed with reduced glutathione, hanging drop vapor diffusion method, 10 mg/ml protein in 10 mM Tris-HCl, pH 8.0, and 10 mM GSH is mixed in a 1:1 ratio with a reservoir solution containing 0.1 M HEPES-NaOH, pH 7.0, and 1.2 M Na citrate, 20°C, several days, X-ray diffraction structure determination and analysis at 1.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F108G
site-directed mutagenesis, the mutant shows reduced affinity and catalytic activity to both GSH and the electrophilic co-substrate, 1-chloro-2,4-dinitrobenzene, compared to the wild-type enzyme
R113A
site-directed mutagensis, the mutant shows activity slightly reduced affinity and catalytic activity to both GSH and the electrophilic co-substrate, 1-chloro-2,4-dinitrobenzene, compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged isozyme MdGST6B from Escherichia coli strain BL21 CodonPlus (DE3)-RIL by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged isozyme MdGST6B in Escherichia coli strain BL21 CodonPlus (DE3)-RIL
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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