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Literature summary extracted from

  • Labrou, N.E.; Karavangeli, M.; Tsaftaris, A.; Clonis, Y.D.
    Kinetic analysis of maize glutathione S-transferase I catalysing the detoxification from chloroacetanilide herbicides (2005), Planta, 222, 91-97.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.18 F35L site-directed mutagenesis, the mutant shows highly reduced activity with alachlor compared to the wild-type enzyme Zea mays
2.5.1.18 I118F site-directed mutagenesis, the mutant shows increased activity with alachlor compared to the wild-type enzyme Zea mays
2.5.1.18 W12I site-directed mutagenesis, the mutant shows reduced activity with alachlor compared to the wild-type enzyme Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.18 additional information
-
 additional information thermodynamics and kinetics of recombinant wild-type and mutant enzymes, the rate-limiting step of the reaction is viscosity-dependent product release Zea mays
2.5.1.18 0.042
-
 alachlor pH 6.5, 30°C, recombinant mutant I118F Zea mays
2.5.1.18 0.18
-
 alachlor pH 6.5, 30°C, recombinant wild-type enzyme Zea mays
2.5.1.18 0.73
-
 glutathione pH 6.5, 30°C, recombinant mutant W12I Zea mays
2.5.1.18 0.76
-
 glutathione pH 6.5, 30°C, recombinant mutant I118F Zea mays
2.5.1.18 0.82
-
 alachlor pH 6.5, 30°C, recombinant mutant W12I Zea mays
2.5.1.18 0.83
-
 glutathione pH 6.5, 30°C, recombinant wild-type enzyme Zea mays
2.5.1.18 3.92
-
 glutathione pH 6.5, 30°C, recombinant mutant F35L Zea mays
2.5.1.18 7.23
-
 alachlor pH 6.5, 30°C, recombinant mutant F35L Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.18 glutathione + alachlor Zea mays isozyme GSTI ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.18 Zea mays
-
 isozyme GST I
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.18 RX + glutathione = HX + R-S-glutathione the enzyme uses a rapid equilibrium random sequential bi-bi mechanism with intrasubunit modulation between GSH binding site, the G-site, and electrophile binding site, the H-site, Trp12, Phe35 and Ile118 are involved in substrate binding, Phe35 is important for catalytic activity Zea mays
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.18 glutathione + 1-chloro-2,4-dinitrobenzene
-
 Zea mays chloride + 2,4-dinitrophenyl-glutathione
-
 ?
2.5.1.18 glutathione + alachlor isozyme GSTI Zea mays ?
-
 ?
2.5.1.18 glutathione + alachlor i.e. 2-chloro-N-[2,6-diethylphenyl]-N-[methoxymethyl]acetamide, isozyme GSTI Zea mays ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.18 glutathione S-transferase
-
 Zea mays
2.5.1.18 GST
-
 Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.5.1.18 30
-
 assay at Zea mays

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.18 0.00011
-
 alachlor pH 6.5, 30°C, recombinant mutant W12I Zea mays
2.5.1.18 0.00019
-
 alachlor pH 6.5, 30°C, recombinant mutant F35L Zea mays
2.5.1.18 0.00046
-
 alachlor pH 6.5, 30°C, recombinant mutant I118F Zea mays
2.5.1.18 0.00048
-
 alachlor pH 6.5, 30°C, recombinant wild-type enzyme Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.18 6.5
-
 assay at Zea mays