scholarly journals Substrate‐activated expression of a biosynthetic pathway in Escherichia coli

2021 ◽  
pp. 2000433
Author(s):  
Cynthia Ni ◽  
Kevin J. Fox ◽  
Kristala L. J. Prather
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway

Engineering endogenous l-proline biosynthetic pathway to boost trans-4-hydroxy-l-proline production in Escherichia coli

2021 ◽  
Vol 329 ◽  
pp. 104-117
Author(s):  
Liangzhen Jiang ◽  
Jing Pang ◽  
Lixia Yang ◽  
Wei Li ◽  
Lili Duan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway

scholarly journals Identification and Characterization of a New Enoyl Coenzyme A Hydratase Involved in Biosynthesis of Medium-Chain-Length Polyhydroxyalkanoates in Recombinant Escherichia coli

2003 ◽  
Vol 185 (18) ◽  
pp. 5391-5397 ◽  
Author(s):  
Si Jae Park ◽  
Sang Yup Lee
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Chain Length ◽  
Biosynthetic Pathway ◽  
Pha Synthase ◽  
Enzymatic Analysis ◽  
E Coli ◽  
Medium Chain ◽  
Medium Chain Length ◽  
Enoyl Coa Hydratase

ABSTRACT The biosynthetic pathway of medium-chain-length (MCL) polyhydroxyalkanoates (PHAs) from fatty acids has been established in fadB mutant Escherichia coli strain by expressing the MCL-PHA synthase gene. However, the enzymes that are responsible for the generation of (R)-3-hydroxyacyl coenzyme A (R3HA-CoAs), the substrates for PHA synthase, have not been thoroughly elucidated. Escherichia coli MaoC, which is homologous to Pseudomonas aeruginosa (R)-specific enoyl-CoA hydratase (PhaJ1), was identified and found to be important for PHA biosynthesis in a fadB mutant E. coli strain. When the MCL-PHA synthase gene was introduced, the fadB maoC double-mutant E. coli WB108, which is a derivative of E. coli W3110, accumulated 43% less amount of MCL-PHA from fatty acid compared with the fadB mutant E. coli WB101. The PHA biosynthetic capacity could be restored by plasmid-based expression of the maoCEc gene in E. coli WB108. Also, E. coli W3110 possessing fully functional β-oxidation pathway could produce MCL-PHA from fatty acid by the coexpression of the maoCEc gene and the MCL-PHA synthase gene. For the enzymatic analysis, MaoC fused with His6-Tag at its C-terminal was expressed in E. coli and purified. Enzymatic analysis of tagged MaoC showed that MaoC has enoyl-CoA hydratase activity toward crotonyl-CoA. These results suggest that MaoC is a new enoyl-CoA hydratase involved in supplying (R)-3-hydroxyacyl-CoA from the β-oxidation pathway to PHA biosynthetic pathway in the fadB mutant E. coli strain.

Biosynthetic pathway for poly(3-Hydroxypropionate) in recombinant Escherichia coli

2012 ◽  
Vol 50 (4) ◽  
pp. 693-697 ◽  
Author(s):  
Qi Wang ◽  
Changshui Liu ◽  
Mo Xian ◽  
Yongguang Zhang ◽  
Guang Zhao
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway ◽  
Recombinant Escherichia Coli

scholarly journals Artificial Biosynthetic Pathway for an Unnatural Terpenoid with an Iridiumcontaining P450

2020 ◽  
Author(s):  
Jing Huang ◽  
Zhennan Liu ◽  
brandon bloomer ◽  
Douglas Clark ◽  
Aindrila Mukhopadhyay ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Synthetic Biology ◽  
Chemical Reactions ◽  
Biosynthetic Pathway ◽  
Metabolic Networks ◽  
Complex Molecules ◽  
Whole Cells ◽  
Porphyrin Complex ◽  
Heme Transport ◽  
Artificial Metalloenzymes

<div>Synthetic biology enables microbial hosts to produce complex molecules that are</div><div>otherwise produced by organisms that are rare or difficult to cultivate, but the structures of these</div><div>molecules are limited to chemical reactions catalyzed by natural enzymes. The integration of</div><div>artificial metalloenzymes (ArMs) that catalyze abiotic reactions into metabolic networks could</div><div>broaden the cache of molecules produced biosynthetically by microorgansms. We report the</div><div>assembly of an ArM containing an iridium-porphyrin complex in the cytoplasm of a terpene</div><div>producing Escherichia coli by a heterologous heme transport machinery, and insertion of this ArM</div><div>into a natural biosynthetic pathway to produce an unnatural terpenoid. This work shows that</div><div>synthetic biology and synthetic chemistry, incorporated together in whole cells, can produce</div><div>molecules previously inaccessible to nature.</div>

scholarly journals Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility–mass spectrometry

2019 ◽  
Vol 476 (21) ◽  
pp. 3125-3139 ◽  
Author(s):  
Daniel Shiu-Hin Chan ◽  
Jeannine Hess ◽  
Elen Shaw ◽  
Christina Spry ◽  
Robert Starley ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Structural Biology ◽  
Ion Mobility ◽  
Biosynthetic Pathway ◽  
Screening Tool ◽  
Native Mass Spectrometry ◽  
Ion Mobility Mass Spectrometry ◽  
E Coli ◽  
Structural Insights

Abstract CoaBC, part of the vital coenzyme A biosynthetic pathway in bacteria, has recently been validated as a promising antimicrobial target. In this work, we employed native ion mobility–mass spectrometry to gain structural insights into the phosphopantothenoylcysteine synthetase domain of E. coli CoaBC. Moreover, native mass spectrometry was validated as a screening tool to identify novel inhibitors of this enzyme, highlighting the utility and versatility of this technique both for structural biology and for drug discovery.

scholarly journals Regulation of the heme biosynthetic pathway for combinational biosynthesis of phycocyanobilin in Escherichia coli

2018 ◽  
Vol 71 ◽  
pp. 23-30 ◽  
Author(s):  
Baosheng Ge ◽  
Yao Chen ◽  
Qian Yu ◽  
Xiaojun Lin ◽  
Jiqiang Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biosynthetic Pathway
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