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

Chem Commun (Camb). 2014 Dec 11;50(95):14953-5. doi: 10.1039/c4cc06527a.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amination
  • Amines / chemistry
  • Amino Acid Oxidoreductases / chemistry*
  • Amino Acid Oxidoreductases / genetics
  • Ketones / chemistry
  • Leucine Dehydrogenase / chemistry*
  • Leucine Dehydrogenase / genetics
  • Recombinant Fusion Proteins / chemistry*
  • Substrate Specificity

Substances

  • Amines
  • Ketones
  • Recombinant Fusion Proteins
  • Amino Acid Oxidoreductases
  • Leucine Dehydrogenase
  • phenylalanine oxidase