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

BRENDA support

Literature summary for 2.5.1.18 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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.042
-
alachlor pH 6.5, 30°C, recombinant mutant I118F Zea mays
0.18
-
alachlor pH 6.5, 30°C, recombinant wild-type enzyme Zea mays
0.73
-
glutathione pH 6.5, 30°C, recombinant mutant W12I Zea mays
0.76
-
glutathione pH 6.5, 30°C, recombinant mutant I118F Zea mays
0.82
-
alachlor pH 6.5, 30°C, recombinant mutant W12I Zea mays
0.83
-
glutathione pH 6.5, 30°C, recombinant wild-type enzyme Zea mays
3.92
-
glutathione pH 6.5, 30°C, recombinant mutant F35L Zea mays
7.23
-
alachlor pH 6.5, 30°C, recombinant mutant F35L Zea mays

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Zea mays
-
isozyme GST I
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glutathione S-transferase
-
Zea mays
GST
-
Zea mays

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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