How many amino acids are in glutathione S-transferase?
The tag is 220 amino acids (roughly 26 kDa) in size, which, compared to tags such as the Myc-tag or the FLAG-tag, is quite large.
What is the structure of glutathione S-transferase?
Domain I consists of a central four-stranded beta-sheet flanked on one side by two alpha-helices and on the other side by an irregular segment containing three short 3(10)-helices, while domain II is entirely helical. The dimeric molecule is globular with a prominent large cavity formed between the two subunits.
What is GSTT1 gene?
MyGenes for gene The protein encoded by this gene, glutathione S-transferase (GST) theta 1 (GSTT1), is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds.
Which vector has glutathione S-transferase tag?
Glutathione S-transferase (GST) is a naturally occurring 26 KDa protein found in eukaryotic cells. The gene from the parasitic helminth Schistosoma japonicum was used in the development of the pGEX vectors (1). This unit describes the use of a GST affinity tag to aid in the purification of recombinant proteins.
What are the three amino acids in glutathione?
A tripeptide comprised of three amino acids (cysteine, glutamic acid, and glycine) present in most mammalian tissue. Glutathione acts as an antioxidant, a free radical scavenger and a detoxifying agent.
How many amino acids are in GST?
GST is a 211 amino acid protein (26 kDa) whose DNA sequence is frequently integrated into expression vectors for production of recombinant proteins.
What does a GST tag do?
The GST tag Protein purification with affinity tags such as glutathione S-transferase (GST), histidine (HIS), and other affinity tags, enables purification of proteins with both known and unknown biochemical properties.
What is the role of glutathione S transferase?
Glutathione S-transferases (GSTs) are a family of Phase II detoxification enzymes that function to protect cellular macromolecules from attack by reactive electrophiles. Specifically, GSTs catalyse the conjugation of glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds (Figure 1).
Which amino acids are precursors of glutathione?
Abstract. Purpose: To correlate the distribution of glutathione (GSH) and its precursor amino acids (cysteine, glycine, and glutamate) with the expression of their respective amino acid transporters in the rat lens.
What are the functional groups in glutathione?
It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine. The carboxyl group of the cysteine residue is attached by normal peptide linkage to glycine….CHEBI:16856.
| Synonyms | Sources |
|---|---|
| N-(N-gamma-L-Glutamyl-L-cysteinyl)glycine | KEGG COMPOUND |
| Reduced glutathione | KEGG COMPOUND |
Is glutathione S transferase a protein?
The glutathione S-transferases (GSTs) are an abundant family of dimeric proteins that have the capacity to conjugate glutathione (GSH) with a variety of compounds containing electrophilic centers.
Is glutathione an essential amino acid?
The highest concentration of glutathione is in the liver, making it critical in the body’s detoxification process. Glutathione is also an essential component to the body’s natural defense system.
Does glutathione contain methionine?
Abstract. Methionine and cysteine are constituents of glutathione.
What amino acids are in glutathione?
Is glutathione acidic or alkaline?
acidic
Glutathione (GSH) can be used as a marker for such reactive species by covalently binding to electrophilic sites via the thiol sulphur. Glutathione is known to be acidic so we have investigated the effect of GSH concentration and pH on the formation of GSH adducts and metabolic activity of human liver microsomes.
Is GST a gene?
The glutathione S-transferase (GST) gene family encodes genes that are critical for certain life processes, as well as for detoxication and toxification mechanisms, via conjugation of reduced glutathione (GSH) with numerous substrates such as pharmaceuticals and environmental pollutants.
What is the function of glutathione transferase?
What 3 amino acids make up glutathione?
Glutathione Conjugation Glutathione is made up of three amino acids—cysteine, glutamic acid, and glycine. Glutathione is found in the diet and is also synthesized in the body.