Advances in protein engineering and its application in synthetic biology

2022 ◽  
pp. 147-158
Author(s):  
Rongming Liu ◽  
Liya Liang ◽  
Maria Priscila Lacerda ◽  
Emily F. Freed ◽  
Carrie A. Eckert
2012 ◽  
Vol 30 (3) ◽  
pp. 541-549 ◽  
Author(s):  
Jee Loon Foo ◽  
Chi Bun Ching ◽  
Matthew Wook Chang ◽  
Susanna Su Jan Leong

2017 ◽  
Vol 2 (3) ◽  
pp. 208-218 ◽  
Author(s):  
Chun You ◽  
Rui Huang ◽  
Xinlei Wei ◽  
Zhiguang Zhu ◽  
Yi-Heng Percival Zhang

Author(s):  
Chengjun Jiang ◽  
Guilin Cheng ◽  
Fan Xu ◽  
Qi Wu

: Enzyme-catalyzed cascade reactions have attracted an increasing attention with many advantages, such as environmental protection, high efficiency and no need for intermediate purification. The present overview has summarized enzymatic cascade benefit systems, including double-enzyme, multi-enzyme and chemical-enzyme catalytic one-pot reactions. With the continuous developments in protein engineering, metabolic engineering, synthetic biology and systems biocatalysis, multi-step biotransformations will expand the scope of application, as well as enhance the biocatalytic efficiency.


2019 ◽  
Vol 41 (3) ◽  
pp. 40-44
Author(s):  
Curran Oi ◽  
Diana Tokarska ◽  
Lynne Regan

The discovery of intrinsically fluorescent proteins revolutionized our ability to visualize proteins within living cells. Since that original observation, a plethora of fluorescent proteins with varied colour and brightness have been obtained. For a number of imaging purposes, however, synthetic biology approaches have been required to create new labelling methodologies. Here, we describe the protein engineering technologies that underlie some of those key designs and show how they have been used to great effect in different cell types.


mSystems ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
Rafael Giraldo

ABSTRACT Amyloids are protein polymers that were initially linked to human diseases. Across the whole Tree of Life, many disease-unrelated proteins are now emerging for which amyloids represent distinct functional states. Most bacterial amyloids described are extracellular, contributing to biofilm formation. However, only a few have been found in the bacterial cytosol. This paper reviews from the perspective of synthetic biology (SynBio) our understanding of the subtle line that separates functional from pathogenic and transmissible amyloids (prions). In particular, it is focused on RepA-WH1, a functional albeit unconventional natural amyloidogenic protein domain that participates in controlling DNA replication of bacterial plasmids. SynBio approaches, including protein engineering and the design of allosteric effectors such as diverse ligands and an optogenetic module, have enabled the generation in RepA-WH1 of an intracellular cytotoxic prion-like agent in bacteria. The synthetic RepA-WH1 prion has the potential to develop into novel antimicrobials.


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