4s13

Publication Abstract from PubMed

The non-oxidative decarboxylation of aromatic acids occurs in a range of microbes and is of interest for bioprocessing and metabolic engineering. Although phenolic acid decarboxylases provide useful tools for bioindustrial applications, the molecular basis of how these enzymes function are only beginning to be examined. Here we present the 2.35 A resolution x-ray crystal structure of the ferulic acid decarboxylase (FDC1; UbiD) from Saccharomyces cerevisiae. FDC1 shares structural similarlity with the UbiD family of enzymes that are involved in ubiquinone biosynthesis. The position of 4-vinylphenol, the product of p-coumaric acid decarboxylation, in the structure identifies a large hydrophobic cavity as the active site. Differences in the beta2e-alpha5 loop of chains in the crystal suggest that conformational flexibility of this loop allows access to the active site. The structure also implicates Glu285 as the general base in the non-oxidative decarboxylation reaction catalyzed by FDC1. Biochemical analysis shows a loss of enzymatic activity in the E285A mutant. Modeling of 3-methyoxy-4-hydroxy-5-decaprenylbenzoate, a partial stucture of the physiological UbiD substrate, in the binding site suggests that a approximately 30 A-long pocket adjacent to the catalytic site may accommodate the isoprenoid tale of the substrate needed for ubiquinone biosynthesis in yeast. The three-dimensional structure of yeast FDC1 provides a template for guiding protein engineering studies aimed at optimizing the efficiency of aromatic acid decarboxylation reactions in bioindustrial applications.

Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae.,Bhuiya MW, Lee SG, Jez JM, Yu O Appl Environ Microbiol. 2015 Apr 10. pii: AEM.00762-15. PMID:25862228^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.