RETRACTED ARTICLE: Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis

2015 ◽  
Vol 99 (22) ◽  
pp. 9473-9481 ◽  
Author(s):  
Hyunji Lee ◽  
Jiyoung Park ◽  
Chaewon Jung ◽  
Dongfei Han ◽  
Jiyoung Seo ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Ferulic Acid ◽  
Site Directed Mutagenesis ◽  
Acid Decarboxylase ◽  
Directed Mutagenesis ◽  
Ferulic Acid Decarboxylase ◽  
Retracted Article

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

scholarly journals Improving the Performance of Horseradish Peroxidase by Site-Directed Mutagenesis

2019 ◽  
Vol 20 (4) ◽  
pp. 916 ◽  
Author(s):  
Diana Humer ◽  
Oliver Spadiut
Keyword(s):  
Catalytic Activity ◽  
Horseradish Peroxidase ◽  
Signal Sequence ◽  
Enzyme Engineering ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Promising Alternative ◽  
Wide Range ◽  
Quadruple Mutant ◽  
Commercial Applications

Horseradish peroxidase (HRP) is an intensely studied enzyme with a wide range of commercial applications. Traditionally, HRP is extracted from plant; however, recombinant HRP (rHRP) production is a promising alternative. Here, non-glycosylated rHRP was produced in Escherichia coli as a DsbA fusion protein including a Dsb signal sequence for translocation to the periplasm and a His tag for purification. The missing N-glycosylation results in reduced catalytic activity and thermal stability, therefore enzyme engineering was used to improve these characteristics. The amino acids at four N-glycosylation sites, namely N13, N57, N255 and N268, were mutated by site-directed mutagenesis and combined to double, triple and quadruple enzyme variants. Subsequently, the rHRP fusion proteins were purified by immobilized metal affinity chromatography (IMAC) and biochemically characterized. We found that the quadruple mutant rHRP N13D/N57S/N255D/N268D showed 2-fold higher thermostability and 8-fold increased catalytic activity with 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) as reducing substrate when compared to the non-mutated rHRP benchmark enzyme.

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