Glutathione transferases

Published on October 1, 2007 Reviewed on October 1, 2015   31 min

Other Talks in the Series: Drug Metabolizing Enzymes

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Glutathione transferases constitute an important part of the phase two by a transformation reactions. The enzymes are made up of members of three superfamilies with different locations in the cell. In the rodent liver, glutathione transferases make up an impressive five percent of the protein content. The unique aspect of these enzymes is their specificity towards reactive compounds. The substrates being lipophilic and electrophilic. In this lecture, I will describe the enzymes and enzyme families, the structure and mechanism of glutathione transferases, their regulation and highly versatile functions. I will refer to glutathione transferases also by their common abbreviation GSTs.
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There are three superfamilies of glutathione transferases. The soluble diameric enzymes, the membrane bound trimeric enzymes and the fosfomycin resistance protein. Soluble also called cytosolic and membrane bound glutathione transferases have been found in all aerobic organisms, whereas fosfomycin resistance protein is found in bacteria. All of the enzymes involved in xenobiotic metabolism display very broad substrate specificity, whereas the fosfomycin resistance protein is clearly different since it is specific for one substrate only.