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Issue 43, 2010
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Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase

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Abstract

By replacing a single active-site residue Cys107 with Ser in phenylalanine aminomutase (PAM), the enzyme gained tyrosine aminomutase (TAM) activity while retaining PAM activity and high enantioselectivity. This engineered enantioselective TAM also catalyzed formation of β-tyrosine from p-coumaric acid and may prove to be useful for the synthesis of enantiopure β-tyrosine and its derivatives.

Graphical abstract: Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase

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Publication details

The article was received on 23 Jul 2010, accepted on 14 Sep 2010 and first published on 05 Oct 2010


Article type: Communication
DOI: 10.1039/C0CC02768E
Citation: Chem. Commun., 2010,46, 8157-8159
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    Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase

    B. Wu, W. Szymański, H. J. Wijma, C. G. Crismaru, S. de Wildeman, G. J. Poelarends, B. L. Feringa and D. B. Janssen, Chem. Commun., 2010, 46, 8157
    DOI: 10.1039/C0CC02768E

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