Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily.
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.
Rigsby
Rachel E
RE
Department of Biochemistry, Vanderbilt University, Nashville, Tennessee, USA.
Fillgrove
Kerry L
KL
Beihoffer
Lauren A
LA
Armstrong
Richard N
RN
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
D001426:Bacterial Proteins; D008667:Metalloproteins; D005578:Fosfomycin; D005982:Glutathione Transferase; D006867:Hydrolases