Issue 43, 2010
From the journal:

Chemical Communications

Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase†‡

Bian Wu,a   Wiktor Szymański,ab   Hein J. Wijma,a   Ciprian G. Crismaru,a   Stefaan de Wildeman,c   Gerrit J. Poelarends,d   Ben L. Feringab  and  Dick B. Janssen*a  

* Corresponding authors

a Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, Groningen, The Netherlands
E-mail: D.B.Janssen@rug.nl
Fax: +31 50-3634165
Tel: +31 50-3634008

b Center for System Chemistry, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, Groningen, The Netherlands

c DSM Pharmaceutical Products, P.O. Box 18, Geleen, The Netherlands

d Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, Groningen, The Netherlands

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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Article information

DOI
https://doi.org/10.1039/C0CC02768E
Article type
Communication
Submitted
23 jul 2010
Accepted
14 sep 2010
First published
05 okt 2010

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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