Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase

Chemical modification of the RTEM-1 thio

Chemical modification of the RTEM-1 thiol β-lactamase by thiol-selective reagents: Evidence for activation of the primary nucleophile of the β-lactamase active site by adjacent functional groups

✍ Anna K. Knap; R. F. Pratt 📂 Article 📅 1989 🏛 John Wiley and Sons 🌐 English ⚖ 806 KB

The RTEM-1 thiol beta-lactamase (Sigal, I.S., Harwood, B.G., Arentzen, R., Proc. Natl. Acad. Sci. U.S.A. 79:7157-7160, 1982) is inactivated by thiol-selective reagents such as iodoacetamide, methyl methanethiosulfonate, and 4,4'-dipyridyldisulfide, which modify the active site thiol group. The pH-ra