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Information on EC 2.5.1.18 - glutathione transferase and Organism(s) Brucella anthropi and UniProt Accession P81065

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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.
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This record set is specific for:
Brucella anthropi
UNIPROT: P81065
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Word Map
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The taxonomic range for the selected organisms is: Brucella anthropi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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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
glutathione S-transferase
-
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 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
glutathione + 1-chloro-2,4-dinitrobenzene
S-(2,4-dinitrophenyl)glutathione + HCl
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
guanidine hydrochloride
retains 30% of its functionality at 0.5 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46 - 3.933
1-chloro-2,4-dinitrobenzene
0.132 - 13.96
glutathione
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85 - 10.78
1-chloro-2,4-dinitrobenzene
0.45 - 16.51
glutathione
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
mutant enzyme C10A/S11A, at 30°C
3.1
mutant enzyme C10A, at 30°C
5.9
wild type enzyme, at 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GST_BRUAN
201
0
21739
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the presence of glutathione, hanging drop vapour diffusion method, using 2 M ammonium sulfate as a precipitating agent
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C10A
the mutation causes the preferential binding of glutathione to the H-site, the mutant shows a decrease in activity of about 50%, drastic increase in Km value for glutathione of 105fold, and 23fold lower catalytic efficiency compared to the wild type enzyme
C10A/S11A
mutant shows dramatic decrease in specific activity of about 98%, the double mutation exhibits loss of affinity for glutathione, a Km value 10-fold higher than in the wild type, and a 291fold decrease of the catalytic efficiency compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
wild type enzyme retains 80% of initial activity at about 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography and glutathione-affinity Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain XL1-Blue
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in 0.1 M potassium phosphate buffer (pH 6.5) containing 1 mM EDTA and 5 mM dithiothreitol, with 4 M guanidine hydrochloride
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allocati, N.; Federici, L.; Masulli, M.; Favaloro, B.; Di Ilio, C.
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site
Proteins
71
16-23
2008
Brucella anthropi (P81065), Brucella anthropi
Manually annotated by BRENDA team