The Mechanism of the Enzymatic Synthesis of 2,4-hydroxymethfufural phosphate

Abstract

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 some bacteria 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). Furan-containing compounds have been highlighted for their high potential in the production of biofuels and biomaterial compounds; thus, research efforts seek to create a more efficient synthesis process for furan compounds. The broad industrial applications of MfnB could usher in a new era for the synthesis of furan compounds to be used in the generation of liquid fuel or other valuable 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 the catalytic mechanism utilizing a site-directed mutagenesis, comprehensive kinetic evaluation, and structural study.