Selection of allosteric β‐lactamase mutants featuring an activity regulation by transition metal ions

• Published in: Protein science Vol. 15; no. 10; pp. 2335 - 2343
• Main Authors: Mathonet, Pascale, Barrios, Humberto, Soumillion, Patrice, Fastrez, Jacques
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.10.2006
• Subjects: Allosteric Regulation - genetics; Allosteric Site - genetics; beta-Lactamases - chemistry; beta-Lactamases - genetics; beta-Lactamases - metabolism; Copper - pharmacology; engineered allosteric site; Kinetics; metal binding; Mutation; Nickel - pharmacology; Peptide Library; Protein Engineering; regulation; Transition Elements - pharmacology; Zinc - pharmacology; β‐lactamase

Libraries of phage‐displayed β‐lactamase mutants in which up to three loops have been engineered by genetic introduction of random peptide sequences or by randomization of the wild‐type sequence have been submitted to selection protocols designed to find mutants in which binding of transition metal...