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Literature summary for 2.5.1.18 extracted from

  • Josephy, P.D.; Kent, M.; Mannervik, B.
    Single-nucleotide polymorphic variants of human glutathione transferase T1-1 differ in stability and functional properties (2009), Arch. Biochem. Biophys., 490, 24-29.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D141N site-directed mutagenesis of isozyme GST T1-1, the mutant enzyme behaves similarly to the wild-type enzyme, in terms of expression level and specific activity. The mutant activity with ethidium bromide is highly reduced compared to the wild-type enzyme Homo sapiens
E173K site-directed mutagenesis of isozyme GST T1-1, the mutant shows reduced expression levels and enzyme activity with all substrates compared to the wild-type enzyme. The mutant is not active with ethidium bromide Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
S-hexyl glutathione
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P30711 isozyme GST T1-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1,2-epoxy-3-(p-nitrophenoxy)propane
-
Homo sapiens ?
-
?
glutathione + 4-nitrobenzyl chloride
-
Homo sapiens S-(4-nitrobenzyl)glutathione + HCl
-
?
glutathione + ethylene diiodide
-
Homo sapiens ?
-
?
additional information GST T1-1 displays both glutathione transferase and glutathione peroxidase enzyme activities, the latter with CuOOH Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
glutathione transferase T1-1
-
Homo sapiens
GST T1-1
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Homo sapiens