Literature summary for 2.5.1.18 extracted from

Tars, K.; Larsson, A.K.; Shokeer, A.; Olin, B.; Mannervik, B.; Kleywegt, G.J.
Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant (2006), J. Mol. Biol., 355, 96-105.

Search for more literature for 2.5.1.18

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant isozyme GST T1-1	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
W234R	site-directed mutagenesis, mutation of the residue from human isozyme GST T1-1 to the analogous residue of rat and mouse enzymes results in altered substrate binding site structure and improved catalytic activity compared to the wild-type enzyme	Homo sapiens

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
RX + glutathione = HX + R-S-glutathione	active site involving residue Trp234, and substrate binding structure, isozyme GST T1-1	Homo sapiens	a

Subunits

Subunits	Comment	Organism
dimer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
glutathione S-transferase	-	Homo sapiens
GST	-	Homo sapiens

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Release 2023.1 (January 2023)