Literature summary for 2.5.1.18 extracted from

Balogh, L.M.; Le Trong, I.; Kripps, K.A.; Shireman, L.M.; Stenkamp, R.E.; Zhang, W.; Mannervik, B.; Atkins, W.M.
Substrate specificity combined with stereopromiscuity in glutathione transferase A4-4-dependent metabolism of 4-hydroxynonenal (2010), Biochemistry, 49, 1541-1548.

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant isozyme GSTA4-4, and of isozyme GSTA1-1GIMFhelix mutant in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type isozyme GSTA4-4 and recombinant mutant GSTA1-1 GIMFhelix in complex with reaction product 4-hydroxynonenal-3S-glutathione, 0.002 ml of protein solution containing 10 mg/ml protein in 10 mM HEPES, pH 7.0, with a 10fold molar excess of ligand are mixed with 0.002 ml of reservoir solution containing containing 24% PEG 4000, 0.1 M sodium acetate trihydrate, pH 4.6, and 0.2 M ammonium sulfate, or mixing of 0.002 ml protein solution with 500 nl of EtOH and 0.003 ml of reservoir solution containing 16% PEG monomethyl ester 5000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, X-ray diffraction structure determination and analysis at 1.90-2.10 A resolution, molecular replacement	Homo sapiens

Crystallization (Comment)

Organism

purified recombinant wild-type isozyme GSTA4-4 and recombinant mutant GSTA1-1 GIMFhelix in complex with reaction product 4-hydroxynonenal-3S-glutathione, 0.002 ml of protein solution containing 10 mg/ml protein in 10 mM HEPES, pH 7.0, with a 10fold molar excess of ligand are mixed with 0.002 ml of reservoir solution containing containing 24% PEG 4000, 0.1 M sodium acetate trihydrate, pH 4.6, and 0.2 M ammonium sulfate, or mixing of 0.002 ml protein solution with 500 nl of EtOH and 0.003 ml of reservoir solution containing 16% PEG monomethyl ester 5000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, X-ray diffraction structure determination and analysis at 1.90-2.10 A resolution, molecular replacement

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of mutant GSTA1-1GIMFhelix	Homo sapiens
Y9F	site-directed mutagenesis of isozyme GSTA4-4	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
rac-4-hydroxynonenal + glutathione	Homo sapiens	elimination of the lipid peroxidation product 4-hydroxynonenal, a toxic compound that contributes to numerous diseases	S-(4-hydroxy-1-oxononan-3-yl)glutathione	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isozyme GSTA4-4	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant isozyme GSTA4-4, and recombinant isozyme GSTA1-1GIMFhelix mutant from Escherichia coli by glutathione affinity chromatography and gel filtration	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	isozyme GSTA4-4 shows high catalytic chemospecificity for alkenals, but negligible stereoselectivity, GSTA4-4 undergoes no enantiospecific induced fit, mechanism of the combination of high substrate chemoselectivity and low substrate stereoselectivity, overview	Homo sapiens	?	-	?
rac-4-hydroxynonenal + glutathione	elimination of the lipid peroxidation product 4-hydroxynonenal, a toxic compound that contributes to numerous diseases	Homo sapiens	S-(4-hydroxy-1-oxononan-3-yl)glutathione	-	?
rac-4-hydroxynonenal + glutathione	GSTA1-1 isoform has poor catalytic efficiency with 4-hydroxynonenal, GSTA4-4 has negligible stereoselectivity towards the two 4-hydroxynonenal enantiomers, despite its high catalytic chemospecificity for alkenals	Homo sapiens	S-[(2S)-3-hydoxy-2-(2-oxoethyl)octyl]glutathione	product binding, overview	?

Synonyms

Synonyms	Comment	Organism
glutathione transferase A4-4	-	Homo sapiens
GSTA4-4	-	Homo sapiens