Skip to main content


This research project stems from the desire to explore and eventually harness the enzymatic mechanism of 4-(hydroxymethyl)-2-furan-carboxaldehyde-phosphate synthase (MfnB). The enzyme of interest, MfnB, is found most prominently in methanogens and can catalyze five or more separate chemical transformations in a single active site. This singular enzyme takes two molecules of glyceraldehyde-3-phosphate to create a furan-containing compound 4-(hydroxymethyl)-2-furan-carboxaldehyde-phosphate. The US. Department of Energy has published a list of the “Top 10 + 4” bio-based chemicals, with furan-containing compounds highlighted for their high potential in the production of biofuels and biomaterials. Industrial applications of MfnB might usher in a new era for the synthesis of furan compounds to be used in the generation of liquid fuel or other biomaterials via enzyme-catalyzed reactions. Despite the initial characterization of MfnB and the identification of Schiff base-forming lysine, the detailed mechanism of MfnB remains speculative. Our team seeks to understand the details of catalytic mechanism through site-directed mutagenesis, comprehensive kinetic evaluation, and structural study. At this point, a total of 13 mutant enzymes have been generated and the activity of 8 mutants has been measured with four resulting in no activity, three having limited activity and one mutant with increased activity. The remaining five mutants are currently undergoing kinetic evaluation with hopes of establishing activity of all mutant enzymes before the end of the semester. The next step is a collaboration with a protein crystallographer to generate a detailed mechanism of MfnB.


This is a metadata-only record.



  • Subject
    • Chemistry & Biochemistry

  • Institution
    • Dahlonega

  • Event location
    • Nesbitt 3110

  • Event date
    • 23 March 2018

  • Date submitted

    19 July 2022

  • Additional information
    • Acknowledgements:

      Dr. Yu Wang