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

作者：Wu Bian; Szymanski Wiktor; Wijma Hein J; Crismaru Ciprian G; de Wildeman Stefaan; Poelarends Gerrit J; Feringa Ben L; Janssen Dick B^*

来源：Chemical communications, 2010, 46(43): 8157-8159.

DOI：10.1039/c0cc02768e

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 beta-tyrosine from p-coumaric acid and may prove to be useful for the synthesis of enantiopure beta-tyrosine and its derivatives.

• 出版日期2010