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- W2145429771 abstract "In nature, the activity of many enzymes involved in important biochemical pathways is controlled by binding a ligand in a site remote from the active site. The allosteric sites are frequently located in hinge regulatory subunits, in which a conformational change can occur and propagate to the active site. The enzymatic activity is then enhanced or decreased depending on the type of effectors. Many artificial binding sites have been created to engineer an allosteric regulation. Generally, these sites were engineered near the active site in loops or at the surface of contiguous helices or strands but rarely in hinge regions. This work aims at exploring the possibility of regulating a monomeric enzyme whose active site is located at the interface between two domains. We anticipated that binding of a ligand in the hinge region linking the domains would modify their positioning and, consequently, modulate the activity. Here, we describe the design of two mutants in a circularly permuted TEM-1 (cpTEM-1) β-lactamase. The first one, cpTEM-1-His3 was created by a rational design. It shows little regulation upon metal ion binding except for a weak activation with Zn2+. The second one, cpTEM-1-3M-His2, was selected by a directed evolution strategy. It is allosterically down-regulated by Zn2+, Ni2+ and Co2+ with binding affinities around 300 µM." @default.
- W2145429771 created "2016-06-24" @default.
- W2145429771 creator A5003175044 @default.
- W2145429771 creator A5011014068 @default.
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- W2145429771 date "2010-06-30" @default.
- W2145429771 modified "2023-09-26" @default.
- W2145429771 title "Engineering allosteric regulation into the hinge region of a circularly permuted TEM-1 β-lactamase" @default.
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- W2145429771 doi "https://doi.org/10.1093/protein/gzq041" @default.
- W2145429771 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20591901" @default.
- W2145429771 hasPublicationYear "2010" @default.
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