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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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Supplementary files

Article information


Submitted
23 Jul 2010
Accepted
14 Sep 2010
First published
05 Oct 2010

Chem. Commun., 2010,46, 8157-8159
Article type
Communication

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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