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A Single Residue Influences the Reaction Mechanism of Ammonia Lyases and Mutases
Authors:Sebastian Bartsch Dipl.‐Biochem.  Uwe T. Bornscheuer Prof.
Affiliation:Institute of Biochemistry, Dept. of Biotechnology & Enzyme Catalysis, Greifswald University, Felix‐Hausdorff‐Strasse 4, 17487 Greifswald (Germany), Fax: (+49)?3834‐86‐80066, http://www.chemie.uni‐greifswald.de/~biotech
Abstract:All ways lead to Rome? Computer modeling and kinetic measurements identified a distinct residue in Phe/Tyr ammonia lyases (PAL/TAL) which controls whether the Friedel–Crafts or an E1cB reaction mechanism takes place. Hence, Glu484 in pcPAL favors the Friedel–Crafts reaction (see picture, MIO=4‐methylidene imidazol‐5‐one) whereas an Asn in TAL gives an elimination reaction. These mechanistic investigations also reveal activity of a PAL mutant and a TAL towards an amino alcohol.
image

Keywords:enzyme catalysis  Friedel–  Crafts mechanism  lyases  molecular modeling  substrate specificity
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