Improved production of D-pantothenic acid in Escherichia coli by integrated strain engineering and fermentation strategies

2021 ◽  
Author(s):  
Shuping Zou ◽  
Kuo Zhao ◽  
Heng Tang ◽  
Zheng Zhang ◽  
Bo Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pantothenic Acid ◽  
Strain Engineering

Metabolic engineering of Escherichia coli for d-pantothenic acid production

2019 ◽  
Vol 294 ◽  
pp. 267-275 ◽  
Author(s):  
Bo Zhang ◽  
Xiao-Ming Zhang ◽  
Wei Wang ◽  
Zhi-Qiang Liu ◽  
Yu-Guo Zheng
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Acid Production ◽  
Pantothenic Acid

Integrated strain engineering and bioprocessing strategies for high-level bio-based production of 3-hydroxyvalerate in Escherichia coli

2020 ◽  
Vol 104 (12) ◽  
pp. 5259-5272
Author(s):  
Dragan Miscevic ◽  
Ju-Yi Mao ◽  
Teshager Kefale ◽  
Daryoush Abedi ◽  
Chih-Ching Huang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Strain Engineering ◽  
High Level

Overproduction of Exopolysaccharide Colanic Acid by Escherichia coli by Strain Engineering and Media Optimization

2020 ◽  
Vol 193 (1) ◽  
pp. 111-127
Author(s):  
Hyeong Min Han ◽  
In Jung Kim ◽  
Eun Ju Yun ◽  
Jae Won Lee ◽  
Yoonho Cho ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Strain Engineering ◽  
Media Optimization ◽  
Colanic Acid

SOME VITAMIN AND AMINO ACID INTERRELATIONSHIPS IN ESCHERICHIA COLI 113-3: I. THE INHIBITORY EFFECTS OF CYSTINE AND CYSTEINESULPHINIC ACID

1957 ◽  
Vol 3 (7) ◽  
pp. 967-974 ◽  
Author(s):  
J. M. McLaughlan
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Pantothenic Acid ◽  
Inhibitory Effect ◽  
Inhibitory Effects ◽  
Aerobic Conditions ◽  
High Concentrations

Cystine, cysteinesulphinic acid (CSA), and other closely related sulphur-containing amino acids inhibited growth of Escherichia coli 113-3, particularly in aerobic conditions. The cystine inhibition was completely prevented by aspartic acid, partially reversed by pantothenic acid or β-alanine and slightly reversed by lysine or thiamine. The inhibitory effect of CSA was completely or partially reversed by aspartic acid, lysine, glutamic acid, proline, ornithine, or homoserine. Aspartic acid and glutamic acid appeared to reverse the inhibition competitively while lysine seemed to reverse the inhibition in a noncompetitive manner. Reversal of the inhibitory effect of relatively high concentrations of CSA by lysine was not complete, however, unless methionine was also present. Possible mechanisms of the cystine and CSA inhibition are discussed.

scholarly journals De novo biosynthesis of para-nitro-L-phenylalanine in Escherichia coli

2021 ◽  
Author(s):  
Neil D. Butler ◽  
Sabyasachi Sen ◽  
Minwei Lin ◽  
Aditya M. Kunjapur
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Shake Flask ◽  
De Novo ◽  
Strain Engineering ◽  
Biological Macromolecules ◽  
List Type ◽  
Bacterial Cells ◽  
Defined Media

AbstractNitroaromatic functional groups can impart valuable properties to chemicals and to biological macromolecules including polypeptides. Para-nitro-L-phenylalanine (pN-Phe) is a nitroaromatic amino acid with uses including immune stimulation and fluorescence quenching. As the chemical synthesis of pN-Phe does not follow green chemistry principles and impedes provision of pN-Phe to engineered bacterial cells in some contexts, we sought to design a de novo biosynthetic pathway for pN-Phe in Escherichia coli. To generate the nitro chemical functional group, we identified natural diiron monooxygenases with measurable in vitro and in vivo activity on envisioned amine-containing precursors of para-amino-L-phenylalanine (pA-Phe) and para-aminophenylpyruvate. By expressing one of these N-oxygenase genes together with previously characterized genes for the biosynthesis of pA-Phe, we achieved the synthesis of pN-Phe from glucose. Through further optimization of the chassis, plasmid constructs, and media conditions, we were able to improve the selectivity of pN-Phe biosynthesis, resulting in a maximum titer of 819 µM in rich defined media under shake-flask conditions. These results provide a foundation for the biosynthesis of related nitroaromatic chemicals and for downstream biological applications that could utilize pN-Phe as a building block.HighlightsPara-nitro-L-phenylalanine (pN-Phe) is a valuable small molecule for its applications in genetic code expansion.We establish de novo biosynthesis of pN-Phe from glucose in E. coli, which is also the first example of a de novo pathway design for an unnatural but commonly used non-standard amino acid.We show the first use of an N-oxygenase enzyme in the de novo synthesis of a nitroaromatic product.Screening of natural N-oxygenases and strain engineering resulted in final pN-Phe titers of 820 ± 130 µM in shake flask experiments with rich defined media.

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