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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Sus scrofa and UniProt Accession P51781

for references in articles please use BRENDA:EC2.5.1.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Sus scrofa
UNIPROT: P51781
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: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
RX
+
glutathione
=
HX
+
R-S-glutathione
+
=
+
Synonyms
gst, glutathione s-transferase, gstm1, gstp1, gstt1, glutathione-s-transferase, glutathione transferase, gsta1, gst pi, gstm3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-class glutathione transferase
-
glutathione transferase A1-1
-
GST A1-1
-
glutathione S-alkyl transferase
-
-
-
-
glutathione S-aralkyltransferase
-
-
-
-
glutathione S-aryltransferase
-
-
-
-
glutathione S-transferase
glutathione S-transferase X
-
-
-
-
GSH S-transferase
-
-
-
-
GSHTase-P
-
-
-
-
GSTalpha1
-
-
S-(hydroxyalkyl)glutathione lyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryl group transfer
-
-
-
-
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 hide
50812-37-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
-
-
-
?
5-androstene-3,17-dione + glutathione
?
show the reaction diagram
-
-
-
?
5-pregnene-3,20-dione + glutathione
?
show the reaction diagram
-
-
-
?
phenethyl isothiocyanate + glutathione
?
show the reaction diagram
-
-
-
?
trans-2-nonenal + glutathione
?
show the reaction diagram
-
-
-
?
1-chloro-2,4-dinitrobenzene + glutathione
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
-
-
-
-
?
glutathione + 1,2-dinitrobenzene
?
show the reaction diagram
-
-
-
-
?
glutathione + 1-chloro-2,4-dinitrobenzene
S-2,4-dinitrophenylglutathione + HCl
show the reaction diagram
glutathione + 2,5-dinitrophenol
?
show the reaction diagram
-
-
-
-
?
glutathione + 3,4-dinitrobenzoic acid
?
show the reaction diagram
-
-
-
-
?
glutathione + 4-nitrobenzyl chloride
?
show the reaction diagram
-
-
-
-
?
glutathione + 5-nitrofurfural
?
show the reaction diagram
-
-
-
-
?
glutathione + 5-nitrofurfural diacetal
?
show the reaction diagram
-
-
-
-
?
glutathione + cumene hydroperoxide
?
show the reaction diagram
-
-
-
-
?
RX + glutathione
HX + R-S-glutathione
show the reaction diagram
-
RX: R: aliphatic, aromatic or heterocyclic, X: sulfate, nitrite or halide, enzyme also catalyzes: the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrite, certain isomerization reactions and disulfide interchange
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cantharidic acid
-
-
S-hexylglutathione
-
-
additional information
-
cantharidin has no effect on isoform SGSTalpha1 activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
0.237
5-androstene-3,17-dione
pH 7.8, 30°C
0.7
5-Pregnene-3,20-dione
pH 7.8, 30°C
0.121
phenethyl isothiocyanate
pH 7.8, 30°C
0.16
trans-2-nonenal
pH 7.8, 30°C
0.091
1-chloro-2,4-dinitrobenzene
-
at pH 7.5 and 30°C
0.79
glutathione
-
at pH 7.5 and 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
84
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
4.8
5-androstene-3,17-dione
pH 7.8, 30°C
0.01
5-Pregnene-3,20-dione
pH 7.8, 30°C
9.5
phenethyl isothiocyanate
pH 7.8, 30°C
0.155
trans-2-nonenal
pH 7.8, 30°C
99
1-chloro-2,4-dinitrobenzene
-
at pH 7.5 and 30°C
141.7
glutathione
-
at pH 7.5 and 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
420
1-chloro-2,4-dinitrobenzene
pH 7.8, 30°C
20
5-androstene-3,17-dione
pH 7.8, 30°C
16
5-Pregnene-3,20-dione
pH 7.8, 30°C
79
phenethyl isothiocyanate
pH 7.8, 30°C
1.1
trans-2-nonenal
pH 7.8, 30°C
109
1-chloro-2,4-dinitrobenzene
-
at pH 7.5 and 30°C
178
glutathione
-
at pH 7.5 and 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124
-
-
3.6 - 11.8
-
with cumene hydroperoxide as substrate
7.9 - 41.1
-
with 1-chloro-2,4-dinitrobenzene as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay at
6.5 - 7.5
-
-
7 - 7.5
-
at 30°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
more than 50% activity between pH 6.0 and 8.0
6 - 8.1
-
at pH 6.0 and 8.1 about 50% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
more than 50% activity between 20 and 40°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
GST A1-1
8.9
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene GSTA1
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
distribution in brain
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSTA1_PIG
222
0
25281
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
2 * 22000, SDS-PAGE
25280
-
-
26000
26400
-
2 * 26400, isoenzyme VI, SDS-PAGE
26800
27100
27328
2 * 27328, electrospray ionization MS
28700
-
1 * 27100 + 1 * 28700, isoenzyme I, SDS-PAGE
43000
-
gel filtration
50000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25280, calculated from amino acid sequence
dimer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity during dialysis
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme GST A1-1 from Escherichia coli by ammonium sulfate fractionation, gel filtration, S-hexylglutathione affinity chromatography, ultrafiltration, and again gel filtration
5 major: I, IV, V, VI, VII and 3 minor forms
-
homogeneity, 4 enzyme fractions
-
Ni2+-NTA agarose column chromatography
-
omega isoenzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GSTA1, from ovary and testis, DNA and amino acid sequence determination and analysis, expression of isozyme GST A1-1 in Escherichia coli strain Rosetta(DE3)
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Williamson, G.; Ball, S.K.M.; Chan, H.W.C.
The purification of multiple forms of glutathione S-transferase from pig liver and their reaction with individual methyl linoleate hydroperoxides
Biochem. Soc. Trans.
14
1278-1279
1986
Sus scrofa
-
Manually annotated by BRENDA team
Asaoka, K.; Takahashi, K.
Purification and properties of porcine brain glutathione S-transferases
J. Biochem.
94
1191-1199
1983
Sus scrofa
Manually annotated by BRENDA team
Rouimi, P.; Anglade, P.; Benzekri, A.; Costet, P.; Debrauwer, L.; Pineau, T.; Tulliez, J.
Purification and characterization of a glutathione S-transferase omega in pig: evidence for two distinct organ-specific transcripts
Biochem. J.
358
257-262
2001
Sus scrofa (Q9N1F5), Sus scrofa
Manually annotated by BRENDA team
Torres-Rivera, A.; Landa, A.
Glutathione transferases from parasites: a biochemical view
Acta Trop.
105
99-112
2008
Homo sapiens, Echinococcus granulosus (O16058), Rattus norvegicus (P04905), Schistosoma mansoni (P15964), Mus musculus (P24472), Schistosoma japonicum (P26624), Onchocerca volvulus (P46427), Ascaris suum (P46436), Fasciola hepatica (P56598), Sus scrofa (P80031), Clonorchis sinensis (Q1L2C7), Taenia solium (Q3ZJN3), Ancylostoma caninum (Q6J1M5), Plasmodium yoelii (Q7REH6), Wuchereria bancrofti (Q86LL8), Plasmodium falciparum (Q8MU52)
Manually annotated by BRENDA team
Fedulova, N.; Raffalli-Mathieu, F.; Mannervik, B.
Characterization of porcine alpha-class glutathione transferase A1-1
Arch. Biochem. Biophys.
507
205-211
2011
Sus scrofa (P51781), Sus scrofa, Sus scrofa Yorkshire pig (P51781)
Manually annotated by BRENDA team
Yang, X.Q.; Zhang, Y.L.
Characterization of glutathione S-transferases from Sus scrofa, Cydia pomonella and Triticum aestivum: their responses to cantharidin
Enzyme Microb. Technol.
69
1-9
2015
Sus scrofa, Triticum aestivum, Cydia pomonella
Manually annotated by BRENDA team