<br/>This 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 and creates a furan-containing compound 4-(hydroxymethyl)-2-furan-carboxaldehyde-phosphate (4-HMF-P). The US. Department of Energy (DOE) 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 biomaterial compounds. As one can imagine, 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 biomaterial 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. Uncovering the molecular basis of this catalytic mystery will help us in applying the knowledge to enzyme engineering. The engineered catalytic machinery could then be used for generating platform compounds to meet the needs of industrial biofuel and other biomaterial products.<br/>

Mechanism of the enzymatic synthesis of furan-containing compound, hydroxymethylfurfural

2019 Spring National Meeting

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