A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes.

نویسندگان

  • Bettina R Bommarius
  • Martin Schürmann
  • Andreas S Bommarius
چکیده

We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs ('L- and F-AmDH'), which in turn had been generated from leucine and phenylalanine DH, respectively. Unlike the parent proteins, the chimeric AmDH ('cFL-AmDH') catalyzes the amination of acetophenone to (R)-methylbenzylamine and adamantylmethylketone to adamantylethylamine.

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عنوان ژورنال:
  • Chemical communications

دوره 50 95  شماره 

صفحات  -

تاریخ انتشار 2014