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2.5.1.18: glutathione transferase

This is an abbreviated version!
For detailed information about glutathione transferase, go to the full flat file.

Word Map on EC 2.5.1.18

Reaction

RX
+
glutathione
=
HX
 +
R-S-glutathione

Synonyms

2-hydroxychromene-2-carboxylic acid isomerase, 26GST, adGSTD4-4, agGSTe2, allergen Der p 2, allergen Der p 8, alpha class glutathione transferase, Alpha class GST, alpha GST, alpha-class glutathione transferase, asGST5.5, AtGSTF2, AtuGSTH1-1, BaeAB, beta-etherase, bmGSTD, BphK, CgGSTM1, CgGSTM2, cGST, Chi class GST, Chi GST, class mu glutathione S-transferase, delta class glutathione transferase, delta-class glutathione S-transferase, Delta-class glutathione transferase, EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14, EC 4.4.1.7, EGST, epsilon class GST, Epsilon glutathione S-transferase, Epsilon glutathione transferase, Epsilon GST, epsilon-class glutathione S-transferase, epsilon-class glutathione transferase, GHR, glutathione S-alkyl transferase, glutathione S-aralkyltransferase, glutathione S-aryltransferase, glutathione S-transferase, glutathione S-transferase 2, glutathione S-transferase A1-1, glutathione S-transferase A3-3, glutathione S-transferase AdFSTD3-3, glutathione S-transferase I, glutathione S-transferase omega 1, glutathione S-transferase omega 2, glutathione S-transferase P1-1, glutathione S-transferase pi, glutathione S-transferase Pi-1, glutathione S-transferase X, glutathione transferase, glutathione transferase A1-1, glutathione transferase A4-4, glutathione transferase M1-1, glutathione transferase M2-2, glutathione transferase Omega 3S, glutathione transferase omega-1, glutathione transferase P1-1, glutathione transferase Pi, glutathione transferase T1-1, glutathione transferase zeta, glutathione transferase zeta 1, glutathione transferase Zeta 1-1, glutathione transferase zeta1-1, glutathione transferase-like protein, glutathione-S-transferas, glutathione-S-transferase, glutathione-S-transferase pi, glutathione-transferase, GmGSTU4-4, GSH S-transferase, GSH transferase, GSH transferase homologue, GSH-S transferase rho, GSHTase-P, GST, GST A1-1, GST A2-2, GST A3-3, GST A4-4, GST adgstD4-4, GST alpha, GST Delta 2, GST I, GST II, GST III, GST IV, GST M1-1, GST M2-2, GST M4-4, GST M5-5, GST mu, GST O1-1, GST P1-1, GST pi, GST T1-1, GST Tau, GST Tau19, GST Z1-1, GST-1, GST-2, GST-26, GST-3, GST-Acr, GST-OCX-32, GST-T, GST-theta, GST1, GST1b, GST2, GST20, GST3, GST4, GST5, GST5118, GST7, GST83044, Gsta, GSTA1, GSTA1-1, GSTA2-2, GSTA3, GSTA3-3, GSTA4, GSTA4-4, GSTA4L, GSTA5, GSTA5-5, GSTalpha1, GSTD, GSTD1, GSTD10, GSTd14, GSTD2, GSTD4, GSTD4-4, GSTE1, GSTE2, GSTE3, GSTE4, GSTE5, GSTE6, GSTE7, GSTE8, GSTF12-1, GSTF12-2, GSTF3, GSTF5, GSTF9, GSTFuA1, GSTk, GSTK1, GSTL1, GSTL2, GSTL3, Gstm, GSTm09, GSTM1, GSTM1-1, GSTM2, GSTM2-2, GSTM3, GSTM3-3, GSTM4, GSTM4-4, GSTM5, GSTM5-5, GSTmu, GSTO, GSTO1, GSTO1-1, GSTO2, GSTO2-2, GstO2A, GstO2B, GSTO3, GSTO3S, GSTO4, GSTO7, GSTP, GSTP 1-1, GSTP-1, GSTP1, GSTP1-1, Gstr1, GSTrho, GSTS, GSTS1, GSTS1-1, GSTS2, GSTS3, GSTT, GSTT1, GSTT1-1, Gstt1a, GSTT2, GSTT2-2, GSTT2B-2B, GSTT4, GSTT4L, GSTU1, GSTU10, GSTU10-10, GSTU11, GSTU12, GSTU13, GSTU13-1, GSTU14, GSTU16, GSTU17, GSTU18, GSTU19, GSTU2, GSTU2-2, GSTU21, GSTU24, GSTU24-1, GSTU25, GSTU26, GSTU28, GSTU3, GSTU4, GSTU45, GSTU5, GSTU6, GSTU7, GSTU8, GSTU9, GSTZ, Gstz1, GSTZ1-1, GTT1.2, HCCA isomerase, Hematopoietic prostaglandin D synthase, hGSTA-3, hGSTA1-1, hGSTZ1-1, kappa class glutathione transferase, kappa class GSH transferase, Kappa class GST, KKSG9, lambda glutathione transferase, MAAI, MGST1, MGST2, MGST3, Mgst3a, Mgst3b, microsomal glutathione transferase 1, microsomal glutathione transferase-1, More, mtMGST1, mu class glutathione S-transferase, Mu class GST, mu glutathione transferase, Mu GST, mu-class glutathione S-transferase, mu-class glutathione S-transferase1, Mu-class GST, Mu-GST, nu-class glutathione transferase, Omega class GST, omega glutathione S-transferase, omega glutathione transferase, omega-class glutathione S-transferase, omega-class glutathione S-transferase 2, pGSTA1, phi class glutathione transferase, Pi class GST, pm-GSTR1, PmGST, PtGSTU1, PvGSTF1-1, PvGSTU2-2, PvGSTU3-3, rho class glutathione S-transferase, rho-GST, RX: glutathione R-transferase, RX:glutathione R-transferase, S-(hydroxyalkyl)glutathione lyase, Saro_2873/Saro_2872, selenium-containing glutathione transferase zeta1-1, seleno-hGSTZ1-1, SGST26.5, sigma class glutathione transferase, Sigma class GST, sigma glutathione S-transferase, sigma-class glutathione S-transferase, sigma-class GST, SIGST, Sj26GST, sjGST, sll1545, ssGST3, ssGST5, tau class glutathione S-transferase, tau class glutathione transferase, tau class GST, tau class GSTU4-4, TDR1, theta class glutathione S-transferase, theta class glutathione transferase T1-1, theta class GST, theta-class glutathione transferase, thiol-dependent reductase I, Ure2p mutant A122C, Ure2pB1, Xi class glutathione transferase, Ya-GST, YghU, zeta class glutathione S-transferase, Zeta class GST

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.18 glutathione transferase

Crystallization

Crystallization on EC 2.5.1.18 - glutathione transferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtuGSTH1-1 in complex with inhibitor S-(4-nitrobenzyl)-glutathione, hanging drop vapor diffusion method, mixing of 0.002 ml of 4.85 mg/ml protein in 15 mM Tris-HCl, pH 7.0, and 10 mM S-(4-nitrobenzyl)-glutathione, with 0.002 ml of well solution 1.4 M Na/K phosphate, pH 8.3, equilibration against 0.8 ml well solution, 16°C, X-ray diffraction structure determination and analysis at 1.4 A resolution
-
purified recombinant GST adgstD4-4 mutant V107A, hanging drop vapour diffusion method, 0.002 ml of 9 mg/ml protein in 50 mM Tris–HCl, pH 7.5, 10 mM DTT, and 10 mM glutathione, are mixed with 0.002 ml of reservoir solution containing 0.1 M imidazole, pH 7.0, 0.35 M ammonium acetate, and 32% PEG 4000, 1 week, 22°C, X-ray diffraction structure determination and analysis at
-
purified recombinant wild-type and mutant enzymes F123A and Y119E in complex with S-hexyl glutathione, hanging drop vapour diffusion method at 16°C and 23°C, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-Cl, pH 7.5, and 5 mM S-hexyl glutathione, with 0.002 ml of precipitant solution containing 0.1 M cacodylate, pH 6.6, 29-34% of PEG4000, and 0.13-0.16 M of sodium 32 acetate, equilibration against 0.5 ml reservoir, 1-2 days, X-ray diffraction structure determination and analysis at 2.6-3.0 A resolution, molecular replacement
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
purified bmGSTD, sitting-drop vapor diffusion method, 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, and 0.2 M NaCl, is mixed with with 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate trihydrate, pH 6.5, and 30% w/v PEG 8000, 20°C, 1 month, three-dimensional structure of bmGSTD by the molecular replacement method to a resolution of 2.0 A resolution
-
in the presence of glutathione, hanging drop vapour diffusion method, using 2 M ammonium sulfate as a precipitating agent
in complex with glutathione, vapor diffusion method, using 0.1 M MES pH 6.5, 5 mM zinc sulfate, and 10% (w/v) PEG MME 550, or 0.1 M Tris pH 8.5, 5 mM zinc sulfate, and 2.0 M ammonium sulfate
dmGSTD10 in apo- and glutathione-bound form, and dmGSTD1, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, with 0.002 ml of reservoir solution16 and 23°C, X-ray diffraction structure determination and analysis, attempts to crystallize dmGSTD1 apo-form are unsuccessful due to its affinity toward glutathione ligand
-
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 20% (w/v) PEG 4000, 10% (v/v) 2-propanol, 2 mM GSH, 10 mM dithiothreitol
hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 7.5, 25% (w/v) PEG 4000, 2 mM GSH, and 10 mM dithiothreitol
hanging drop vapor diffusion method, using 0.1M succinic acid-phosphate-glycine buffer with 25% (w/v) PEG 1500 at pH 4.0
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
-
enzyme in GSH-free and -bound forms, using 20% (w/v) PEG8000, 100 mM HEPES-HCl (pH 7.5), 200 mM ammonium sulfate, and 20% (v/v) 2-propanol at 4°C
hanging drop vapor diffusion method, using 0.2 M MgCl2, 0.1 M Bis-Tris, pH 5.6, 22% (w/v) PEG 3350
crystals belong to the triclinic space group P1, with unit-cell parameters a = 72.7, b = 74.0, c = 88.6 A, alpha = 79.1°, beta = 80.1°, gamma = 81.5°, likely contains four homodimers per asymmetric unit
-
isozyme GST Nu2-2, X-ray diffraction structure determination and analysis at 1.71 A resolution, molecular replacement method
-
enzyme in complex with GSH is determined at 2.4 A
-
hanging drop vapor diffusion method, using 1.7-2.2 M (NH4)2SO4, 0.2 M sodium potassium tartrate, 0.75 mM ZnSO4, 17 mM citric acid
-
hanging drop vapour diffusion method
in complex with chlorambucil, hanging drop vapour diffusion method
purified isozyme GST A1-1 in complex with substrate glutathione, hanging drop vapour diffusion method, room temperature, 10 mg/ml protein in 0.1 M Tris-HCl, pH 8.5, with 19% methyl PEG 2000, 0.03 M sodium acetate, pH 4.6, and 1% 2-mercaptoethanol for the apoenzyme, or in 0.1 M Tris–HCl, pH 7.8, with 24% PEG 4000, and 1% 2-mercaptoethanol, with glutathione for wild-type and mutant enzyme complexed with the substrate, the mutant apoenzyme is crystallized from 0.1 M Tris–HCl, pH 7.8, with 24% PEG 4000, 2 mM DTT and 30% MPD, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
purified recombinant hGSTk in apo-form and in complex with S-hexylglutathione, hanging drop vapour diffusion method, apo-form of hGSTk in 20 mM NaH2PO4, pH 7.4, 20 mM NaCl, 1 mM EDTA and 7.2 mM 2-mercaptoethanol, hGSTk in complex in 20 mM HEPES, pH 7.0, 50 mM NaCl, 1 mM EDTA and 1 mM DTT, supplemented with S-hexylglutathione at a molar ratio of 1:2, is mixed with an equal volume of reservoir solution containing 0.2 M NaSCN and 20% PEG3350, 20°C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution
-
purified recombinant wild-type and mutant isozyme GST T1-1 complexed with S-hexyl-glutathione and the 1-iodohexane-glutathione conjugate, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution
-
purified recombinant wild-type isozyme GSTA4-4 and recombinant mutant GSTA1-1 GIMFhelix in complex with reaction product 4-hydroxynonenal-3S-glutathione, 0.002 ml of protein solution containing 10 mg/ml protein in 10 mM HEPES, pH 7.0, with a 10fold molar excess of ligand are mixed with 0.002 ml of reservoir solution containing containing 24% PEG 4000, 0.1 M sodium acetate trihydrate, pH 4.6, and 0.2 M ammonium sulfate, or mixing of 0.002 ml protein solution with 500 nl of EtOH and 0.003 ml of reservoir solution containing 16% PEG monomethyl ester 5000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, X-ray diffraction structure determination and analysis at 1.90-2.10 A resolution, molecular replacement
-
recombinant I71A and I71V hGSTA1-1, hanging drop vapour diffusion method, protein solution, containing 10 mg/ml I71A hGSTA1-1 or 15 mg/ml I71V hGSTA1-1 in 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 2.5 mM S-hexylglutathione and 0.02% sodium azide is mixed with an equal volume of reservoir solution containing 19%w/v PEG 4000, 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, and 0.02% sodium azide, 20°C, X-ray diffraction structure determmination and analysis at 1.75-2.51 A resolution
recombinant mutant R15L isozyme GSTA1-1 complexed with inhibitor S-hexylglutathione, hanging drop vapor diffusion method, 0.002 ml of 14 mg/ml R15L GSTA1-1 in 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 0.02% sodium azide solution are mixed with 0.002 ml of reservoir buffer containing 5 mM S-hexylglutathione, 0.1 M Tris-HCl, pH 7.5, 10 mM DTT, 5-30% PEG 2000 or 4000, equilibration against 1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 1.80 A resolution, molecular replacement method
sitting drop vapor diffusion method, using 100 mM MES pH 6.5, 25% (w/v) poly(ethylene glycol) 3350, and 3% (v/v) methanol
enzyme in complex with substrates glutathione or 1-chloro-2,4-dinitrobenzene, sitting-drop vapour-diffusion method, 0.004 ml of protein solution, containing 20 mM Tris-HCl, pH 7.9, 200 mM NaCl, 2 mM DTT, is mixed with 0.004 ml of reservoir solution containing 6% Tacsimate, pH 8.0, and 26% w/v PEG 3350, for cocrystallization, the protein solution is mixed with glutathione at a molar ratio of 1:1 and with 1-chloro-2,4-dinitrobenzene at a molar ratio of 1:5. The glutathionecomplex crystals from 7% Tacsimate, pH 8.0, 24% w/v PEG 3350 and the CDNB-complex crystals from 8.5% Tacsimate, pH 8.0, 25% w/v PEG 335. Equilibration over 0.5 ml reservoir solution, 22°C, 3 days, X-ray diffraction structure determination and analysis at 2.2 A and 2.0 A resolution, respectively
-
SeMet TDR1 in complex with glutathione, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.3 a resolution, single-wavelength anomalous diffraction, modeling
-
complexed with glutathione or its analogues
-
purified recombinant GSTP1-1 C47A mutant, hanging drop vapour diffusion method, mixing of 0.002 ml of 7 mg/ml protein in 10 mM MES, pH 6.0, with 0.0006 ml of 30 mM S-(p-nitrobenzyl)glutathione in 50 mM MES, pH 6.0, and 0.003 ml of reservoir solution containing 20% PEG 6000 and 0.1 M sodium citrate, pH 4.0, several weeks, 20°C, X-ray diffraction structure determmintion and analysis at 1.77 A resolution
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
using 25% (w/v) polyethylene glycol 3350, 0.1 M Tris-HCl pH 8.5 and 0.2 M lithium sulfate
in complex with glutathione, sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.0) containing 1 M LiCl and 30% (w/v) PEG-6000
recombinant GST2, hanging-drop vapour-diffusion method. Two different crystal forms are grown under identical conditions. They belong to space groups P2(1)2(1)2 and P2(1), respectively. The unit-cell parameters obtained are a = 112.6, b = 84.3, c = 45.1 A from the P2(1)2(1)2 crystal and a = 51.6, b = 82.3, c = 56.7 A, beta = 95.89 degrees from the P2(1) form
-
purified recombinant selenomethionine-apoGST5118 and native holoGST5118 with bound glutathione, microbatch under oil, paraffin, method at 4°C, 4 Selenomethionine-apoGST5118 crystals appear after 4-5 days from droplets containing 0.002 ml of 15-20 mg/ml protein in TE buffer, and 0.002 ml of precipitating solution containing 30% PEG 8000, 200 mM sodium acetate,and 100 mM sodium cacodylate, pH 6.5. The best crystals of GST5118 in complex with GSH grow after 2 months in droplets containing a mixture of 14 mg/ml protein and 6 mM GSH in TE buffer and precipitating solution containing 30% PEG 8000, 200 mM sodium acetate, and 100 mM HEPES, pH 7.0. X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution, single-wavelength anomalous dispersion, the molecular replacement method fails to solve the protein structure
purified recombinant wild-type GST in complex with inhibitor S-hexylglutathione, 22°C, hanging drop vapour diffusion method, from 60 mM CaCl2, 30 mM HEPES, pH 7.5, 8.4% PEG 400, 3.4 mg GST/ml, and 1.4 mM S-hexylglutathione, the reservoir solution contains 150 mM CaCl2, 75 mM HEPES, pH 7.5, and 21% PEG 400, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
recombinant enzyme expressed in bacterial cells, hanging-drop vapour diffusion. X-ray intensity data to 2.8 A resolution are collected from an orthorhombic crystal form with unit-cell parameters a = 62.2, b = 88.3, c = 75.3 A
-
purified enzyme complexed with glutathione, 2-hydroxychromene-2-carboxylic acid, and trans-o-hydroxybenzylidene pyruvic acid, 10 mg/ml protein in storage buffer, with 1 mM GSH, and 1 mM HCCA at 21°C, all crystals are grown under 7 ml of Al’s oil in a microbatch plate, X-ray diffraction structure determination and analysis at 1.7 A resolution, structure modeling
-
structures of the GSH-free enzyme, as well as the partially (approximately 40%) and almost fully (approximately 80%) GSH-saturated enzyme
purified recombinant GST-IRK, 10 mg/ml protein in 20 mM Tris–HCl, pH 7.5, 150 mM NaCl, and 2 mM TCEP, 21°C, against 0.1 M Bis-Tris, pH 5.5, and 25% w/v PEG 3350, or 0.1 M sodium acetate pH 5.5, and 36% w/v PEG MME 5000 as precipitant solutions, 7 days, orthorhombic crystals, X-ray diffraction structure determination and analysis, at 3.0-3.14 A resolution, molecular-replacement
hanging drop vapor diffusion method
-
purified recombinant isozymes SoGST3 and SoGST6, hanging drop vapour diffusion method, 7 mg/ml protein, isozyme SoGST3 gives two crystal forms: SoGST3-A crystals grow from 22% w/v PEG 4000, 0.1 M CHES, pH 9, 0.25 M calcium chloride, 4 mM GSH, and SoGST3-B crystals grow from 22% w/v PEG 4000, 0.1 M CHES, pH 9, 0.25 M calcium chloride, 2 mM GSH and 0.5 mM DTT, isozyme SoGST6 crystals grow within 3 d at 21°C, from 15% w/v PEG 3350, 50 mM MES, pH 6.3, 0.2 M sodium chloride and 0-0.3 mM GSH, X-ray diffraction structure determination and analysis at 2.6-4.0 A resolution
-
purified recombinant enzyme, sitting-drop vapour-diffusion method, 100 nl of 3 mg/ml protein solution is mixed with 100 nl of reservoir solution containing 20% w/v PEG 6000, 0.2 M CaCl2 and 100 mM HEPES buffer, pH 7.5 or 100 mM MES buffer, pH 6.5, 5 days, second variant by hanging-drop vapour-diffusion method, 0.002 ml protein solution are mixed with an equal volume of reservoir solution containing 13-18% w/v PEG 6000, 0.2 M CaCl2 and 100 mM MES buffer, pH 6.5, equilibration against 1 ml reservoir solution, 3 weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
purified recombinant enzyme, hanging-drop vapour-diffusion method, 22°C, 0.002 ml of 6 mg/ml protein in 10 mM Tris-HCl buffer, pH 7.8, and 1 mM EDTA, is mixed with 0.002 ml of reservoir solution containing 25-35% v/v pentaerythritol propoxylate, 0.2 M potassium chloride and 50 mM HEPES buffer, pH 7.5, 3 days, X-ray diffraction structure determination and analysis at 1.45 A resolution, molecular replacement
Thermosynechococcus vestitus
-
in complex with glutathionyl-phenethylthiocarbamate, microbatch under oil method, using 30% (w/v) PEG 400, 0.2 M calcium acetate in 0.1 M pH 4.5 acetate buffer (pH of 5.8)
hanging drop vapour diffusion method with 28% PEG 6000, 100 mM HEPES pH 7.6
-