What does glutathione S-transferase do?
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).
What does the GSTM1 gene do?
GSTM1 is a glutathione S-transferase (GST) which play a role in the detoxification of metabolites of environmental carcinogens including tobacco smoke. There is some evidence to suggest that people with common polymorphisms of these genes may have an increased susceptibility to a range of different cancers.
Where is glutathione S-transferase found?
cytosol
The glutathione transferases (GSTs; also known as glutathione S-transferases) are major phase II detoxification enzymes found mainly in the cytosol. In addition to their role in catalysing the conjugation of electrophilic substrates to glutathione (GSH), these enzymes also carry out a range of other functions.
Which cells are expressing glutathione S-transferase?
Six families of glutathione S-transferases (GSTs), which play an important role in cellular detoxification, are identified in human cells. We report that human keratinocytes and melanocytes express significant levels of GST activity, for which GSTP1-1 is mainly responsible.
What is the function of glutathione peroxidase?
Glutathione Peroxidase (GPx) is a cytosolic enzyme that catalyzes the reduction of hydrogen peroxide to water and oxygen as well as catalyzing the reduction of peroxide radicals to alcohols and oxygen.
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.
What is GSTT1 gene?
Glutathione S-transferase theta-1 is an enzyme that in humans is encoded by the GSTT1 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.
What is the difference between glutathione and glutathione peroxidase?
Glutathione, which is involved in the transport of amino acids, acts as a coenzyme for enzymes and it protects against oxygen radicals and toxic compounds [5]. Se- dependent GSH peroxidase is capable of utilizing hydrogen peroxide (H2O2) and a variety of organic hydroperoxides as substrates.
What foods contain glutathione peroxidase?
4. Eat Foods Naturally Rich in Glutathione. The human body produces glutathione, but there are also dietary sources. Spinach, avocados, asparagus and okra are some of the richest dietary sources ( 13 ).
What are the examples of transferases?
Classification
| EC number | Examples |
|---|---|
| EC 2.2 | transketolase and transaldolase |
| EC 2.3 | acyltransferase |
| EC 2.4 | glycosyltransferase, hexosyltransferase, and pentosyltransferase |
| EC 2.5 | riboflavin synthase and chlorophyll synthase |
Which is the human Glutathione S-transferase Mu 1?
“Stereoselective conjugation of prostaglandin A2 and prostaglandin J2 with glutathione, catalyzed by the human glutathione S-transferases A1-1, A2-2, M1a-1a, and P1-1.” Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
How is glutathione S-transferase 1 inactivated in prostate cancer?
Glutathione S-transferase 1 (GSTP1) expression is inactivated in >90% of all prostate cancers in association with aberrant DNA methylation.
How does glutathione S-transferase affect the risk of systemic sclerosis?
Glutathione S-transferase genetic polymorphisms affect the risk of systemic sclerosis in the Polish population. GSTM1 and GSTT1 null genotypes are not a risk features for nephrolithiasis. The GSTT1 and GSTM1 null polymorphisms are associated with chronic myeloid leukemia among Sudanese patients, independently of their age and gender.
Where does glutathione bind in the GST dimer?
The glutathione molecule binds in a cleft between N – and C -terminal domains – the catalytically important residues are proposed to reside in the N -terminal domain. [21] Both subunits of the GST dimer, whether hetero- or homodimeric in nature, contain a single nonsubstrate binding site, as well as a GSH-binding site.