Mechanistic imperatives for the evolution of glutathione transferases.
Several significant advances in the understanding of the catalytic mechanisms, structures and evolution of glutathione transferases have occurred in the past year. These advances include new mechanistic information concerning the canonical soluble enzymes, the finding that the fosfomycin-specific enzyme, FosA, is a metalloglutathione transferase and a higher resolution projection structure of the microsomal enzyme.
Armstrong
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RN
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA. armstrong@toxicology.mc.vanderbilt.edu
D001426:Bacterial Proteins; D005075:Biological Evolution; D002384:Catalysis; D000697:Central Nervous System Stimulants / Q000737:chemistry; D004352:Drug Resistance, Microbial / Q000235:genetics; D005578:Fosfomycin / Q000737:chemistry; D005978:Glutathione / Q000378:metabolism*; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006873:Hydroquinones / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry; D010084:Oxidation-Reduction; D014443:Tyrosine / Q000031:analogs & derivatives / Q000737:chemistry
D001426:Bacterial Proteins; D000697:Central Nervous System Stimulants; D006873:Hydroquinones; D008667:Metalloproteins; C001245:3-fluorotyrosine; D005578:Fosfomycin; D014443:Tyrosine; C044578:2,3,5,6-tetrachlorohydroquinone; D005982:Glutathione Transferase; C041116:leukotriene-C4 synthase; D005978:Glutathione