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

Bian Wu, Wiktor Szymański, Hein J. Wijma, Ciprian G. Crismaru, Stefaan de Wildeman, Gerrit J. Poelarends, Ben L. Feringa, Dick B. Janssen*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

22 Citaten (Scopus)

Samenvatting

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.
Originele taal-2English
Pagina's (van-tot)8157-8159
Aantal pagina's3
TijdschriftChemical Communications
Volume46
Nummer van het tijdschrift43
DOI's
StatusPublished - 2010

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