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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Anopheles gambiae and UniProt Accession Q93113
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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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Word Map
- 2.5.1.18
- catalase
- dismutase
- sod
-
pull-down
- malondialdehyde
- carcinogenesis
-
detoxify
- hepatocytes
-
smoke
- isoenzymes
- cyp1a1
-
smoking
-
case-control
-
electrophilic
- epoxide
-
aquatic
- wistar
-
genotoxic
-
insecticide
-
chemopreventive
- gill
-
hepatocarcinogenesis
- acetylcholinesterase
-
polycyclic
-
pesticide
- hydroperoxide
-
thiobarbituric
-
hepatotoxicity
-
tbars
-
ache
-
albino
- metallothioneins
-
cigarette
-
benzoapyrene
- phenobarbital
-
drug-metabolizing
-
preneoplastic
-
alt
- aflatoxin
- gssg
-
hepatoprotective
- schistosoma
- comet
- carboxylesterase
- mussel
-
udp-glucuronosyltransferase
-
methylation-specific
- gsh-px
-
organophosphate
- drug development
- medicine
- cyp2d6
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Anopheles gambiae
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
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
1,1-dichloro-2,2-bis-(4-chlorophenyl)ethylene + ?
i.e. DDT, modeling of DDT into the putative DDT-binding pocket, catalytic mechanism of isozyme agGSTe2 that shows high activity through the inclination of the upper part of H4 helix, H4'' helix, which brings residues Arg112, Glu116, and Phe120 closer to the GSH-binding site resulting in a more efficient GS- stabilizing hydrogen-bond-network and higher DDT-binding affinity, overview
product formation through an elimination reaction triggered by the nucleophilic attack of the thiolate group of GS- on the beta-hydrogen of DDT
-
?
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
?
detoxification of the insecticide DDT, especially by isozyme agGSTe2
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
-
-
-
?
additional information
?
-
agGSTe2 has a long narrow cleft at the interface of the N- and C-domains, in which a GSH molecule tightly fits, binding of glutathione does not induce significant conformational changes in the isozyme agGSTe2 protein, structure, overview
-
-
?
additional information
?
-
-
agGSTe2 has a long narrow cleft at the interface of the N- and C-domains, in which a GSH molecule tightly fits, binding of glutathione does not induce significant conformational changes in the isozyme agGSTe2 protein, structure, overview
-
-
?
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
1,1,1-trichloro-2,2-bis-(4-chlorophenyl)ethane + glutathione
?
detoxification of the insecticide DDT, especially by isozyme agGSTe2
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-hexylglutathione
inhibitor binding does not induce significant conformational changes in the protein
2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,7-diol
85% inhibition at 0.1 mM
3-(3,4-dihydroxybenzoyl)-4-hydroxy-8-methyl-5,7-bis(3-methylbut-2-enyl)-8-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,9-dione
95% inhibition at 0.033 mM
4-[3-(5,5-dimethyl-4-oxo-4,5-dihydrofuran-2-yl)-3-hydroxybutoxy]-7H-furo[3,2-g]chromen-7-one
45% inhibition at 0.1 mM
5,8-dihydroxy-1-(hydroxymethyl)naphtho[2,3-c]furan-4,9-dione
98.5% inhibition at 0.1 mM
5,8-dihydroxy-1-methylnaphtho[2,3-c]furan-4,9-dione
85% inhibition at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0048
3-(3,4-dihydroxybenzoyl)-4-hydroxy-8-methyl-5,7-bis(3-methylbut-2-enyl)-8-(4-methylpent-3-enyl)bicyclo[3.3.1]nonane-2,9-dione
Anopheles gambiae
-
0.0043
5,8-dihydroxy-1-(hydroxymethyl)naphtho[2,3-c]furan-4,9-dione
Anopheles gambiae
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). GST1D_ANOGA
209
0
23445
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
agGSTe2 is a canonical GST fold with a highly conserved N-domain and a less conserved C-domain, isozyme agGSTe2 amino acid sequence and secondary structure comparisons, overview
additional information
-
agGSTe2 is a canonical GST fold with a highly conserved N-domain and a less conserved C-domain, isozyme agGSTe2 amino acid sequence and secondary structure comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three agGSTe2 crystal structures including one apo form and two binary complex forms with the co-factor glutathione or the inhibitor S-hexylglutathione, sitting-drop vapor diffusion, 20°C, protein solution is mixed with an equal volume of a reservoir solution, containing 0.1 M Bis-Tris buffer, pH 6.5, and 25% w/v PEG 3350 for the apoenzyme crystallization, or for the enzyme-glutathione complex containing 0.2 M ammonium acetate, 0.1 M sodium acetate buffer, pH 4.6, and 30% w/v PEG 4000, or for the enzyme-inhibitor complex containing 0.2 M sodium iodide and 20% w/v PEG 3350, pH 6.9, 3 weeks, X-ray diffraction structure determination and analysis at 1.4-2.2 A resolution, molecular replacement method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Muleya, V.; Hayeshi, R.; Ranson, H.; Abegaz, B.; Bezabih, M.T.; Robert, M.; Ngadjui, B.T.; Ngandeu, F.; Mukanganyama, S.
Modulation of Anopheles gambiae Epsilon glutathione transferase activity by plant natural products in vitro
J. Enzyme Inhib. Med. Chem.
23
391-399
2008
Anopheles gambiae (Q7PVS6), Anopheles gambiae
Wang, Y.; Qiu, L.; Ranson, H.; Lumjuan, N.; Hemingway, J.; Setzer, W.N.; Meehan, E.J.; Chen, L.
Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity
J. Struct. Biol.
164
228-235
2008
Anopheles gambiae (Q93113), Anopheles gambiae
EXTERNAL LINKS (specific for EC-Number 2.5.1.18)
Transporter Classification Database (TCDB): 1.A.12.2.1
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Release 2023.1 (January 2023)
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