Bacterial glutathione transferase

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Beta class glutathione transferase structure from Proteus mirabilis (PDB: 1PMT).[1]

Bacterial glutathione transferases (GSTs; EC 2.5.1.18) are part of a superfamily of enzymes that play a crucial role in cellular detoxification.[2][3][4] The primary role of GSTs is to catalyse the conjugation of glutathione (GSH) with the electrophilic centers of a wide variety of molecules.[5]

GSTs are widely distributed in aerobic bacteria and are classified into several classes. GSTs are not detected in anaerobic bacteria or archaea.[6]

In bacteria, GSTs are involved in a variety of distinct processes such as biotransformation of toxic compounds, protection against several stresses and antibacterial drug resistance.[7][8][9][10][11]

See also

References

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External links


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  1. Rossjohn J, Polekhina G, Feil SC, Allocati N, Masulli M, Di Ilio C, Parker MW (1998) A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6 721–734.
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