Glutathione transferases in bacteria.
Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.
Allocati
Nerino
N
Dipartimento di Scienze Biomediche, Università G. d'Annunzio, Chieti, Italy. allocati@unich.it
Federici
Luca
L
Masulli
Michele
M
Di Ilio
Carmine
C
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000627:therapeutic use; D001419:Bacteria / Q000145:classification / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D002384:Catalysis; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology; D019143:Evolution, Molecular; D005982:Glutathione Transferase / Q000737:chemistry / Q000378:metabolism*; D008658:Inactivation, Metabolic; D008031:Lignin / Q000378:metabolism; D008958:Models, Molecular; D009281:Naphthalenes / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D012988:Soil Microbiology
D000900:Anti-Bacterial Agents; D009281:Naphthalenes; C031721:naphthalene; D008031:Lignin; D005982:Glutathione Transferase