Isofunctional Enzymes PAD1 and UbiX Catalyze Formation of a Novel Cofactor Required by Ferulic Acid Decarboxylase and 4-Hydroxy-3-polyprenylbenzoic Acid Decarboxylase

2015 ◽  
Vol 10 (4) ◽  
pp. 1137-1144 ◽  
Author(s):  
Fengming Lin ◽  
Kyle L. Ferguson ◽  
David R. Boyer ◽  
Xiaoxia Nina Lin ◽  
E. Neil G. Marsh
Keyword(s):  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

Chemoenzymatic cascade for stilbene production from cinnamic acid catalyzed by ferulic acid decarboxylase and an artificial metathease

2019 ◽  
Vol 9 (20) ◽  
pp. 5572-5576 ◽  
Author(s):  
M. A. Stephanie Mertens ◽  
Daniel F. Sauer ◽  
Ulrich Markel ◽  
Johannes Schiffels ◽  
Jun Okuda ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Cinnamic Acid ◽  
Olefin Metathesis ◽  
Metal Contamination ◽  
Cascade Reaction ◽  
Acid Decarboxylase ◽  
Efficient Removal ◽  
Ferulic Acid Decarboxylase ◽  
Acid Catalyzed ◽  
Removal Of Metal

We report a chemoenzymatic cascade reaction for stilbene production combining decarboxylation and olefin metathesis with efficient removal of metal contamination.

Mechanistic insights into the catalytic reaction of ferulic acid decarboxylase from Aspergillus niger: a QM/MM study

2017 ◽  
Vol 19 (11) ◽  
pp. 7733-7742 ◽  
Author(s):  
Ge Tian ◽  
Yongjun Liu
Keyword(s):  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Catalytic Reaction ◽  
Acid Decarboxylase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Ferulic Acid Decarboxylase ◽  
Rate Limiting

QM/MM calculations reveal the cofactor prFMNiminiumto be the catalytically relevant species compared with prFMNketamine. The protonation of the intermediate is the rate-limiting step, and the prolonged leaving of the generated CO2can facilitate this process.

scholarly journals Structural Basis of Enzymatic Activity for the Ferulic Acid Decarboxylase (FADase) from Enterobacter sp. Px6-4

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16262 ◽  
Author(s):  
Wen Gu ◽  
Jinkui Yang ◽  
Zhiyong Lou ◽  
Lianming Liang ◽  
Yuna Sun ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Ferulic Acid ◽  
Structural Basis ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase

2010 ◽  
Vol 89 (6) ◽  
pp. 1797-1805 ◽  
Author(s):  
Wen Gu ◽  
Xuemei Li ◽  
Jingwen Huang ◽  
Yanqing Duan ◽  
Zhaohui Meng ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

scholarly journals Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Emma Zsófia Aletta Nagy ◽  
Csaba Levente Nagy ◽  
Alina Filip ◽  
Katalin Nagy ◽  
Emese Gál ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

scholarly journals Direct 1,3-butadiene biosynthesis in Escherichia coli via a tailored ferulic acid decarboxylase mutant

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yutaro Mori ◽  
Shuhei Noda ◽  
Tomokazu Shirai ◽  
Akihiko Kondo
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Ferulic Acid ◽  
Rational Design ◽  
Acid Decarboxylase ◽  
Enzyme Design ◽  
Muconic Acid ◽  
Synthetic Rubber ◽  
Ferulic Acid Decarboxylase ◽  
Fed Batch Fermentation

AbstractThe C4 unsaturated compound 1,3-butadiene is an important monomer in synthetic rubber and engineering plastic production. However, microorganisms cannot directly produce 1,3-butadiene when glucose is used as a renewable carbon source via biological processes. In this study, we construct an artificial metabolic pathway for 1,3-butadiene production from glucose in Escherichia coli by combining the cis,cis-muconic acid (ccMA)-producing pathway together with tailored ferulic acid decarboxylase mutations. The rational design of the substrate-binding site of the enzyme by computational simulations improves ccMA decarboxylation and thus 1,3-butadiene production. We find that changing dissolved oxygen (DO) levels and controlling the pH are important factors for 1,3-butadiene production. Using DO–stat fed-batch fermentation, we produce 2.13 ± 0.17 g L−1 1,3-butadiene. The results indicate that we can produce unnatural/nonbiological compounds from glucose as a renewable carbon source via a rational enzyme design strategy.

scholarly journals Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae

2015 ◽  
Vol 81 (12) ◽  
pp. 4216-4223 ◽  
Author(s):  
Mohammad Wadud Bhuiya ◽  
Soon Goo Lee ◽  
Joseph M. Jez ◽  
Oliver Yu
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Active Site ◽  
Three Dimensional ◽  
Structural Similarity ◽  
Dimensional Structure ◽  
Acid Decarboxylase ◽  
Content Type ◽  
Ferulic Acid Decarboxylase

ABSTRACTThe nonoxidative 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 bases for how these enzymes function are only beginning to be examined. Here we present the 2.35-Å-resolution X-ray crystal structure of the ferulic acid decarboxylase (FDC1; UbiD) fromSaccharomyces cerevisiae. FDC1 shares structural similarity with the UbiD family of enzymes that are involved in ubiquinone biosynthesis. The position of 4-vinylphenol, the product ofp-coumaric acid decarboxylation, in the structure identifies a large hydrophobic cavity as the active site. Differences in the β2e-α5 loop of chains in the crystal structure suggest that the conformational flexibility of this loop allows access to the active site. The structure also implicates Glu285 as the general base in the nonoxidative decarboxylation reaction catalyzed by FDC1. Biochemical analysis showed a loss of enzymatic activity in the E285A mutant. Modeling of 3-methoxy-4-hydroxy-5-decaprenylbenzoate, a partial structure of the physiological UbiD substrate, in the binding site suggests that an ∼30-Å-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail 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.

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