Directed evolution of artificial enzymes (XNAzymes) from diverse repertoires of synthetic genetic polymers

2015 ◽  
Vol 10 (10) ◽  
pp. 1625-1642 ◽  
Author(s):  
Alexander I Taylor ◽  
Philipp Holliger
Keyword(s):  
Directed Evolution ◽  
Artificial Enzymes

Artificial Enzymes bringing together Computational Design and Directed Evolution

2021 ◽  
Author(s):  
Beatriz de Pina Mariz ◽  
Sara S Carvalho ◽  
Iris Batalha ◽  
Ana Sofia Pina
Keyword(s):  
Directed Evolution ◽  
Chemical Reactions ◽  
Computational Design ◽  
Industrial Processes ◽  
Artificial Enzymes ◽  
Ancient Times

Enzymes are proteins that catalyse chemical reactions and, as such, have been widely used to facilitate a variety of natural and industrial processes, dating back to ancient times. In fact,...

scholarly journals Optimization of the Turnover in Artificial Enzymes via Directed Evolution Results in the Coupling of Protein Dynamics to Chemistry

2019 ◽  
Vol 141 (26) ◽  
pp. 10431-10439 ◽  
Author(s):  
Joseph W. Schafer ◽  
Ioanna Zoi ◽  
Dimitri Antoniou ◽  
Steven D. Schwartz
Keyword(s):  
Directed Evolution ◽  
Protein Dynamics ◽  
Artificial Enzymes

Fe-N-C Artificial Enzyme: Activation of Oxygen for Dehydrogenation and Monoxygenation of Organic Substrates under Mild Condition and Cancer Therapeutic Application

2018 ◽  
Author(s):  
Fei He ◽  
Li Mi ◽  
Yanfei Shen ◽  
Toshiyuki Mori ◽  
Songqin Liu ◽  
...  
Keyword(s):  
Mild Condition ◽  
Enzyme Activation ◽  
Artificial Enzymes ◽  
Organic Substrates ◽  
Artificial Enzyme ◽  
Therapeutic Application ◽  
Highly Efficient ◽  
Activation Of Oxygen

Developing highly efficient artificial enzymes that directly employ O<sub>2</sub> as terminal oxidant has long been pursued but has rarely achieved yet. We report Fe-N-C has unusual enzyme-like activity in both dehydrogenation and monoxygenation of organic substrates with ~100% selectivity by direct using O<sub>2</sub>.

Directed Evolution of P450 Fatty Acid Decarboxylases via High-Throughput Screening Towards Improved Catalytic Activity

2019 ◽  
Author(s):  
Huifang Xu ◽  
Weinan Liang ◽  
Linlin Ning ◽  
Yuanyuan Jiang ◽  
Wenxia Yang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Fatty Acid ◽  
Directed Evolution ◽  
High Throughput ◽  
High Throughput Screening ◽  
Colorimetric Detection ◽  
Screening Method ◽  
Random Mutagenesis ◽  
Direct Production ◽  
Consumption Activity

P450 fatty acid decarboxylases (FADCs) have recently been attracting considerable attention owing to their one-step direct production of industrially important 1-alkenes from biologically abundant feedstock free fatty acids under mild conditions. However, attempts to improve the catalytic activity of FADCs have met with little success. Protein engineering has been limited to selected residues and small mutant libraries due to lack of an effective high-throughput screening (HTS) method. Here, we devise a catalase-deficient <i>Escherichia coli</i> host strain and report an HTS approach based on colorimetric detection of H<sub>2</sub>O<sub>2</sub>-consumption activity of FADCs. Directed evolution enabled by this method has led to effective identification for the first time of improved FADC variants for medium-chain 1-alkene production from both DNA shuffling and random mutagenesis libraries. Advantageously, this screening method can be extended to other enzymes that stoichiometrically utilize H<sub>2</sub>O<sub>2</sub> as co-substrate.

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