Vinsamlegast notið þetta auðkenni þegar þið vitnið til verksins eða tengið í það: http://hdl.handle.net/1946/18761
Modern enzymes are known to be very efficient at catalysing one type of reaction. Recent studies have shown that despite their specialized function, some enzymes tend to retain very low levels of ancient activity. This has been referred to as promiscuous activity. Previously it has been shown that minor changes in enzymes can significantly increase the promiscuous activity of enzymes.
The hypothesis tested in this project is that by mutating a single amino acid it is possible induce β-lactamase activity in the Vibrio strain G15-21 alkaline phosphatase (VAP). Computational calculations were performed to predict the mutations needed in the active site of VAP to induce a electrostatic environment similar to that of a metallo-β-lactamase. The proposed mutations were D12E, D12A and D12W. Results indicated that β-lactamase activity was not present in the selected variants.
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