title: Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily.
abstract: Three similar but mechanistically distinct fosfomycin resistance proteins that catalyze the opening of the oxirane ring of the antibiotic are known. FosA is a Mn(II) and K(+)-dependent glutathione transferase. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. The expression, purification, kinetic, and physical characteristics of six fosfomycin resistance proteins including the FosA proteins from transposon TN2921 and Pseudomonas aeruginosa, the FosB proteins from Bacillus subtilis and Staphylococcus aureus, and the FosX proteins from Mesorhizobium loti and Listeria monocytogenes are reported.
authors.affiliation: Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, USA.
authors.forename: Rachel E
authors.initials: RE
authors.lastname: Rigsby
authors.forename: Kerry L
authors.initials: KL
authors.lastname: Fillgrove
authors.forename: Lauren A
authors.initials: LA
authors.lastname: Beihoffer
authors.forename: Richard N
authors.initials: RN
authors.lastname: Armstrong
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004352:Drug Resistance, Microbial; D005578:Fosfomycin / Q000378:metabolism; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism*; D006867:Hydrolases / Q000235:genetics / Q000378:metabolism; D008667:Metalloproteins / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure
chemical_list: D001426:Bacterial Proteins; D008667:Metalloproteins; D005578:Fosfomycin; D005982:Glutathione Transferase; D006867:Hydrolases