ArticleACS chemical biology2015
Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 99 citations in OpenAlex.
- Exploration of Genomic Features and Volatile Flavor Production of Yeasts Isolated from Commercial Korean Rice Wine Makgeolli.Journal of microbiology and biotechnology · 2026Article
- High-Gravity Brewing, Yeast Strain Selection, and Glucose Oxidase Effects on the Quality of Nonalcoholic Beer.ACS omega · 2026Article
- Anaerobic degradation of polycyclic aromatic hydrocarbons.Applied and environmental microbiology · 2025Review
- Genome-based exploration of volatile flavor diversity from food yeast species.FEMS yeast research · 2025Review
- Enzymatic Conversion of COChemical reviews · 2023Review
- Article
- Naphthalene Carboxylation in the Sulfate-Reducing Enrichment Culture N47 Is Proposed to Proceed via 1,3-Dipolar Cycloaddition to the Cofactor Prenylated Flavin Mononucleotide.Applied and environmental microbiology · 2023Article
- Toolbox for the structure-guided evolution of ferulic acid decarboxylase (FDC).Scientific reports · 2022Article
- One-Pot Biocatalytic In Vivo Methylation-Hydroamination of Bioderived Lignin Monomers to Generate a Key Precursor to L-DOPA.Angewandte Chemie (International ed. in English) · 2022Article
- One-Pot Biocatalytic In Vivo Methylation-Hydroamination of Bioderived Lignin Monomers to Generate a Key Precursor to L-DOPA.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Screening low-methanol and high-aroma produced yeasts for cider fermentation by transcriptive characterization.Frontiers in microbiology · 2022Article
- Stress modulation as a means to improve yeasts for lignocellulose bioconversion.Applied microbiology and biotechnology · 2021Review
- Fluorescent enzyme-coupled activity assay for phenylalanine ammonia-lyases.Scientific reports · 2020Article
- Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Non-Oxidative Enzymatic (De)Carboxylation of (Hetero)Aromatics and Acrylic Acid Derivatives.Advanced synthesis & catalysis · 2019Review
- The UbiX flavin prenyltransferase reaction mechanism resembles class I terpene cyclase chemistry.Nature communications · 2019Article
- Anaerobic degradation of xenobiotic isophthalate by the fermenting bacterium Syntrophorhabdus aromaticivorans.The ISME journal · 2019Article
- Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae.Scientific reports · 2019Article
- Corynebacterium Cell Factory Design and Culture Process Optimization for Muconic Acid Biosynthesis.Scientific reports · 2018Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
The decarboxylation of antimicrobial aromatic acids such as phenylacrylic acid (cinnamic acid) and ferulic acid by yeast requires two enzymes described as phenylacrylic acid decarboxylase (PAD1) and ferulic acid decarboxylase (FDC). These enzymes are of interest for various biotechnological applications, such as the production of chemical feedstocks from lignin under mild conditions. However, the specific role of each protein in catalyzing the decarboxylation reaction remains unknown. To examine this, we have overexpressed and purified both PAD1 and FDC from E. coli. We demonstrate that PAD1 is a flavin mononucleotide (FMN)-containing protein. However, it does not function as a decarboxylase. Rather, PAD1 catalyzes the formation of a novel, diffusible cofactor required by FDC for decarboxylase activity. Coexpression of FDC and PAD1 results in the production of FDC with high levels cofactor bound. Holo-FDC catalyzes the decarboxylation of phenylacrylic acid, coumaric acid and ferulic acid with apparent kcat ranging from 1.4-4.6 s(-1). The UV-visible and mass spectra of the cofactor indicate that it appears to be a novel, modified form of reduced FMN; however, its instability precluded determination of its structure. The E. coli enzymes UbiX and UbiD are related by sequence to PAD1 and FDC respectively and are involved in the decarboxylation of 4-hydroxy-3-octaprenylbenzoic acid, an intermediate in ubiquinone biosynthesis. We found that endogenous UbiX can also activate FDC. This implies that the same cofactor is required for decarboxylation of 4-hydroxy-3-polyprenylbenzoic acid by UbiD and suggests a wider role for this cofactor in metabolism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.