Inhibition of the metallo-beta-lactamase produced from Serratia marcescens by thiol compounds.
Low molecular weight thiol compounds have been found to be strong inhibitors of metallo-beta-lactamase (IMP-1) produced by Serratia marcescens TN9106, which was expressed by Echerichia coli JM109 cells. Mercaptoacetic acid and 2-mercaptopropionic acid strongly and competitively inhibited IMP-1 with Ki of 0.23 and 0.19 microM, respectively. 2-Mercaptoethanol reversibly inhibited IMP-1 but did not show simple competitive inhibition.
Goto
M
M
Faculty of Pharmaceutical Sciences, Kumamoto University, Japan.
Takahashi
T
T
Yamashita
F
F
Koreeda
A
A
Mori
H
H
Ohta
M
M
Arakawa
Y
Y
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000235:genetics; D012706:Serratia marcescens / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000235:genetics
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D013438:Sulfhydryl Compounds; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases