Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Protein engineering

Check nature first, then evolve

Nature Chemical Biology volume 6, pages 793–794 (2010)Cite this article

Subjects

Ten significantly active new (R)-transaminases, still very rare enzymes, were found among 21 designed variants obtained from nothing more than existing transaminase structures and alignment of pertinent fingerprints of annotated sequences.

Biocatalysis—that is, performing chemical transformations with biological catalysts—has made great inroads over the last few years. Owing in large part to their superior chemo-, regio- and enantioselectivity and specificity, enzymes are increasingly used in low– and high–value-added transformations ranging from hydrolysis of cellulose to the generation of chiral alcohols and amines for pharma applications1. A significant fraction of new chemical entities under development in pharma feature chiral centers of amines, but the enzymes needed to access these molecules are currently rare. To address this problem, new (R)-transaminases, rarer than their (S)-specific counterparts, were developed by applying a sequence-based algorithm to exclude sequences leading to known (S)-amine and (R)- or (S)-amino acid specificity2.

This is a preview of subscription content, access via your institution

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Learn more

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Evaluation of active site environment and of fingerprints in multiple sequence alignments of transaminases.

Katherine Vicari

References

  1. Pollard, D.J. & Woodley, J.M. Trends Biotechnol. 25, 66–73 (2007).

    Article  CAS  Google Scholar 

  2. Höhne, M., Schätzle, S., Jochens, H., Robins, K. & Bornscheuer, U.T. Nat. Chem. Biol. 6, 807–813 (2010).

    Article  Google Scholar 

  3. Bornscheuer, U.T. & Pohl, M. Curr. Opin. Chem. Biol. 5, 137–143 (2001).

    Article  CAS  Google Scholar 

  4. Chaparro-Riggers, J.F. et al. BMC Biotechnol. 7, 77 (2007).

    Article  Google Scholar 

  5. Kazlauskas, R.J. & Bornscheuer, U.T. Nat. Chem. Biol. 5, 526–529 (2009).

    Article  CAS  Google Scholar 

  6. Reetz, M.T., Wang, L.-W. & Bocola, M. Angew. Chem. Int. Edn Engl. 45, 1236–1241 (2006).

    Article  CAS  Google Scholar 

  7. Reetz, M.T. & Carballeira, J.D. Nat. Protoc. 2, 891–903 (2007).

    Article  CAS  Google Scholar 

  8. Vázquez-Figueroa, E., Chaparro-Riggers, J. & Bommarius, A.S. ChemBioChem 8, 2295–2301 (2007).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Andreas S. Bommarius is in the School of Chemical and Biomolecular Engineering and the School of Chemistry and Biochemistry, Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta.,

    Andreas S Bommarius

Authors
  1. Andreas S Bommarius
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Andreas S Bommarius.

Ethics declarations

Competing interests

The author declares no competing financial interests.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Bommarius, A. Check nature first, then evolve. Nat Chem Biol 6, 793–794 (2010). https://doi.org/10.1038/nchembio.461

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nchembio.461

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing