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Literature summary for 2.5.1.18 extracted from

  • Zeng, Q.Y.; Wang, X.R.
    Catalytic properties of glutathione-binding residues in a tau class glutathione transferase (PtGSTU1) from Pinus tabulaeformis (2005), FEBS Lett., 579, 2657-2662.
    View publication on PubMed
Search for more literature for 2.5.1.18

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pinus tabuliformis

Protein Variants

Protein Variants Comment Organism
E66A activity with 1-chloro-2,4-dinitrobenzene is 18.4fold lower than wild-type activity, activity with ethacrynic acid is 1.25fold higher than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 3fold lower than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is higher than the refolding of the wild-type enzyme Pinus tabuliformis
I54A activity with 1-chloro-2,4-dinitrobenzene is 2fold lower than wild-type activity, activity with ethacrynic acid is 3.5fold higher than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 2.8fold higher than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is lower than the refolding of the wild-type enzyme Pinus tabuliformis
K40A activity with 1-chloro-2,4-dinitrobenzene is 18fold lower than wild-type activity, activity with ethacrynic acid is 1.2fold lower than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is nearly identical to wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is lower than the refolding of the wild-type enzyme Pinus tabuliformis
S67A activity with 1-chloro-2,4-dinitrobenzene is fold 21.6fold lower than wild-type activity, activity with ethacrynic acid is 1.13fold lower than wild-type activity, activity with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole is 3.9fold lower than wild-type activity, no activity with 4-nitrophenyl acetate. More thermolabile than wild-type enzyme. Refolding after denaturation is higher than the refolding of the wild-type enzyme Pinus tabuliformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.47
-
 GSH 25°C, wild-type enzyme Pinus tabuliformis
0.48
-
 GSH 25°C, mutant enzyme S67A Pinus tabuliformis
0.57
-
 GSH 25°C, mutant enzyme K40A Pinus tabuliformis
0.76
-
 1-chloro-2,4-dinitrobenzene 25°C, wild-type enzyme Pinus tabuliformis
0.89
-
 GSH 25°C, mutant enzyme E66A Pinus tabuliformis
1.42
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme S67A Pinus tabuliformis
1.89
-
 GSH 25°C, mutant enzyme I54A Pinus tabuliformis
3.13
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme I54A Pinus tabuliformis
4.23
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme E66A Pinus tabuliformis
4.96
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme K40A Pinus tabuliformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pinus tabuliformis the enzyme plays an importent role in stress tolerance and detoxification in plants ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pinus tabuliformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pinus tabuliformis

Renatured (Commentary)

Renatured (Comment) Organism
wild-type enzyme shows 25.42% of the initial activity after denaturation and refolding, mutant K40A 20.51%, mutant I54A 8.51%, mutant E66A 51.68% and mutant S67A 34.33% Pinus tabuliformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-chloro-2,4-dinitrobenzene + GSH
-
 Pinus tabuliformis S-(2,4-dinitrophenyl)glutathione + HCl
-
 ?
4-nitrophenyl acetate + GSH at 0.2% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme Pinus tabuliformis ?
-
 ?
7-chloro-4-nitrobenzo-2-oxa-1,3-diazole + GSH at 23% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme Pinus tabuliformis ?
-
 ?
ethacrynic acid + GSH at 8% of the activity with 1-chloro-2,4-dinitrobenzene, wild-type enzyme Pinus tabuliformis ?
-
 ?
additional information the enzyme plays an importent role in stress tolerance and detoxification in plants Pinus tabuliformis ?
-
 ?

Synonyms

Synonyms Comment Organism
PtGSTU1
-
 Pinus tabuliformis
tau class glutathione transferase
-
 Pinus tabuliformis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 15 min, mutant enzymes E66A and S67A retain about 15% of its initial activity, K40A and I54A retain 62% of their initial activity, wild-type enzyme retains 95% of its initial activity Pinus tabuliformis
60
-
 15 min, complete inactivation of the mutant enzymes K40A, I54A, E66A and S67A, wild-type enzyme retains 41% of its initial activity Pinus tabuliformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
 GSH 25°C, mutant enzyme E66A Pinus tabuliformis
0.35
-
 GSH 25°C, mutant enzyme S67A Pinus tabuliformis
0.5
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme S67A Pinus tabuliformis
0.52
-
 GSH 25°C, mutant enzyme K40A Pinus tabuliformis
1.08
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme E66A Pinus tabuliformis
1.7
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme K40A Pinus tabuliformis
3.4
-
 GSH 25°C, mutant enzyme I54A Pinus tabuliformis
4.75
-
 1-chloro-2,4-dinitrobenzene 25°C, mutant enzyme I54A Pinus tabuliformis
6.48
-
 GSH 25°C, wild-type enzyme Pinus tabuliformis
6.74
-
 1-chloro-2,4-dinitrobenzene 25°C, wild-type enzyme Pinus tabuliformis