4 years ago

Characterization of a (R)-selective amine transaminase from Fusarium oxysporum

Characterization of a (R)-selective amine transaminase from Fusarium oxysporum
Amine transaminases are prominent biocatalysts in the production of chiral amines which are indispensable building blocks in asymmetric synthesis. In this study, a new (R)-enantioselective amine transaminase from Fusarium oxysporum (ATFo) was identified by genome mining. ATFo possibly evolved from a branched chain amino acid aminotransferase (BCAT) with key amino acids being changed, which belong to one of the three groups of pyridoxal 5′-phosphate dependent enzymes class IV (PLPDE_IV). The gene of the amine transaminase was functionally expressed and the protein was then purified with a molecular mass of approximately 36kDa. The purified ATFo demonstrated high stereoselectivity towards (R)-enantiomer of α-phenethylamine and other analogues, which clearly indicated its (R)-selectivity. The optimal temperature and pH for the activities of ATFo were 25°C and 7.0, respectively. Addition of Mn2+ and Zn2+ could greatly enhance the enzyme activity. In addition, the specific activities and stereoselectivities of these ATFo toward various amino donors and amino acceptors were determined. Compared to (S)-selective amine transaminase, the (R)-selective counterpart has been less studied. Given their pivotal role in asymmetric biocatalysis, it is of great importance to find more (R)-selective amine transaminases with ability or potential for synthesis of the target compounds. Thus, the discovery of the (R)-selective amine transaminase ATFo is a valuable contribution to the currently small toolbox of these enzymes.

Publisher URL: www.sciencedirect.com/science

DOI: S1359511317306712

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.