GSS
GSS (glutathione synthetase) is an ATP-dependent ligase that catalyses the final step in making glutathione, the most abundant intracellular thiol in aerobic cells. It belongs to the eukaryotic GSH synthase family and functions as a homodimer. Browse Assay Genie's current range of GSS research reagents below, or read on for the biology behind the target.
GSS catalyses the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. According to the NCBI Gene summary, it carries out the second step of glutathione biosynthesis, the conversion of gamma-L-glutamyl-L-cysteine to glutathione, and the active protein functions as a homodimer. UniProt also records a role for the enzyme in ophthalmate biosynthesis in hepatocytes.
Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells. It is required for protection of cells against oxidative damage, amino acid transport, detoxification of foreign compounds and maintenance of protein sulfhydryl groups in a reduced state. It also acts as a cofactor for a number of enzymes. Because GSS supplies the final step of this pathway, it is a natural focus for studies of redox balance and xenobiotic handling.
The human GSS gene encodes a protein of the eukaryotic GSH synthase family and is classed by HGNC within the ligases. Defects in the gene are a cause of glutathione synthetase deficiency. Mouse and rat each have a Gss ortholog, which allows the enzyme to be studied in common rodent models. Researchers working with GSS antibody, GSS ELISA kit or GSS protein reagents typically do so in the context of glutathione metabolism and oxidative stress biology.
Glutathione protects cells against oxidative damage and free radicals, so GSS is relevant to studies of how cells maintain redox balance.
Glutathione contributes to the detoxification of foreign compounds, making GSS a point of interest in xenobiotic handling.
GSS catalyses the second, ATP-dependent step of glutathione synthesis, making it central to analysis of pathway flux and regulation.
Defects in the GSS gene cause glutathione synthetase deficiency, so the enzyme is studied in inherited disorders of glutathione metabolism.
GSS catalyses the ATP-dependent formation of glutathione from gamma-glutamylcysteine and glycine, the second step of glutathione biosynthesis. It works as a homodimer. UniProt also lists a role in ophthalmate biosynthesis in hepatocytes. Check the datasheet of any product for its validated reactivity.
GSS is the HGNC symbol for glutathione synthetase, also named GSH synthase. No alternative symbols or previous names are recorded by HGNC. The protein belongs to the eukaryotic GSH synthase family, and HGNC places the gene in the ligases group, with EC number 6.3.2.3.
Mouse and rat both have a Gss ortholog, so the enzyme can be studied in rodent systems. In humans, defects in the GSS gene are a cause of glutathione synthetase deficiency, a disorder of glutathione biosynthesis described in the NCBI Gene summary.
Other glutathione pathway enzymes and oxidative stress markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P48637; product specifications from Assay Genie datasheets.