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GS63

Sigma-Aldrich

GST A3-3, Recombinant Human

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Synonym(s):
GTA3, glutathione S-transferase alpha 3
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

assay

>95% (SDS-PAGE)

form

frozen liquid

specific activity

61 U/mg (using spectrophotometric determination of 1-chloro-2,4-dinitrobenzene (CDNB) conjugation with reduced glutathione (1 mM) in 100 mM NaPO4 (pH 6.5) at room temperature.)

mol wt

25 kDa

concentration

1.0 mg/mL

storage temp.

−70°C

Gene Information

human ... GSTA3(2940)

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GST P1-1, Recombinant Human

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

concentration

1.0 mg/mL

concentration

2.95 mg/mL

concentration

3.1 mg/mL

concentration

-

assay

>95% (SDS-PAGE)

assay

>95% (SDS-PAGE)

assay

>95% (SDS-PAGE)

assay

>95% (SDS-PAGE)

mol wt

25 kDa

mol wt

-

mol wt

26 kDa

mol wt

23 kDa

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−70°C

Biochem/physiol Actions

Glutathione S-transferase alpha 3 (GSTA3) is an enzyme that in humans is encoded by the GSTA3 gene. Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTs are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
This gene encodes a glutathione S-tranferase belonging to the alpha class genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined.

Storage and Stability

The enzyme should be used by the end-user customer within 1 year of receipt.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Jonathan L Daka et al.
The Journal of biological chemistry, 289(46), 32243-32252 (2014-09-25)
The seemingly simple proton abstraction reactions underpin many chemical transformations, including isomerization reactions, and are thus of immense biological significance. Despite the energetic cost, enzyme-catalyzed proton abstraction reactions show remarkable rate enhancements. The pathways leading to these accelerated rates are
Ann-Sofie Johansson et al.
The Journal of biological chemistry, 277(19), 16648-16654 (2002-03-02)
Glutathione transferase (GST) A3-3 is the most efficient human steroid double-bond isomerase known. The activity with Delta(5)-androstene-3,17-dione is highly dependent on the phenolic hydroxyl group of Tyr-9 and the thiolate of glutathione. Removal of these groups caused an 1.1 x
Natasha Tetlow et al.
Pharmacogenetics, 14(10), 657-663 (2004-09-30)
The alpha class glutathione transferase GSTA3-3 is involved in steroid biosynthesis and the metabolism of some xenobiotics. A bioinformatics approach was utilized to identify novel coding region polymorphisms in the glutathione transferase A3 gene (GSTA3). We describe an I71L polymorphism
Yijun Gu et al.
Biochemistry, 43(50), 15673-15679 (2004-12-15)
The crystal structure of human class alpha glutathione (GSH) S-transferase A3-3 (hGSTA3-3) in complex with GSH was determined at 2.4 A. Despite considerable amino acid sequence identity with other human class alpha GSTs (e.g., hGSTA1-1), hGSTA3-3 is unique due to
Françoise Raffalli-Mathieu et al.
The Biochemical journal, 414(1), 103-109 (2008-04-23)
hGSTA3-3 (human Alpha-class glutathione transferase 3-3) efficiently catalyses steroid Delta(5)-Delta(4) double-bond isomerization in vitro, using glutathione as a cofactor. This chemical transformation is an obligatory reaction in the biosynthesis of steroid hormones and follows the oxidation of 3beta-hydroxysteroids catalysed by

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