Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase
- Wu, Bian
- Szymański, Wiktor
- Wijma, Hein J.
- Crismaru, Ciprian G.
- Wildeman, Stefaan de
- Poelarends, Gerrit J.
- Feringa, Ben L.
- Janssen, Dick B.
Publication date
January 2010
DOIAbstract
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
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