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

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C0CC02768E
Article type
Communication
Submitted
23 Jul 2010
Accepted
14 Sep 2010
First published
05 Oct 2010

Chem. Commun., 2010,46, 8157-8159

Permissions

Request permissions

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements