scholarly journals Overexpression of key enzymes of the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway for improving squalene production in Escherichia coli

2017 ◽  
Vol 16 (50) ◽  
pp. 2307-2316
Author(s):  
Liu Haiyuan ◽  
Han Shu ◽  
Xie Liping ◽  
Pan Jie ◽  
Zhang Wei ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Mep Pathway ◽  
Key Enzymes

scholarly journals Improvement of isoprene production in Escherichia coli by rational optimization of RBSs and key enzymes screening

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Meijie Li ◽  
Hailin Chen ◽  
Changqing Liu ◽  
Jing Guo ◽  
Xin Xu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Key Enzymes

scholarly journals Isoprenoid biosynthesis in higher plants and in Escherichia coli: on the branching in the methylerythritol phosphate pathway and the independent biosynthesis of isopentenyl diphosphate and dimethylallyl diphosphate

2002 ◽  
Vol 366 (2) ◽  
pp. 573-583 ◽  
Author(s):  
Jean-François HOEFFLER ◽  
Andréa HEMMERLIN ◽  
Catherine GROSDEMANGE-BILLIARD ◽  
Thomas J. BACH ◽  
Michel ROHMER
Keyword(s):  
Escherichia Coli ◽  
Higher Plants ◽  
Mevalonic Acid ◽  
Cell Suspension Cultures ◽  
Mep Pathway ◽  
Isopentenyl Diphosphate ◽  
Higher Plant ◽  
Methylerythritol Phosphate Pathway ◽  
Dimethylallyl Diphosphate ◽  
Deuterium Retention

In the bacterium Escherichia coli, the mevalonic-acid (MVA)-independent 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway is characterized by two branches leading separately to isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). The signature of this branching is the retention of deuterium in DMAPP and the deuterium loss in IPP after incorporation of 1-[4-2H]deoxy-d-xylulose ([4-2H]DX). Feeding tobacco BY-2 cell-suspension cultures with [4-2H]DX resulted in deuterium retention in the isoprene units derived from DMAPP, as well as from IPP in the plastidial isoprenoids, phytoene and plastoquinone, synthesized via the MEP pathway. This labelling pattern represents direct evidence for the presence of the DMAPP branch of the MEP pathway in a higher plant, and shows that IPP can be synthesized from DMAPP in plant plastids, most probably via a plastidial IPP isomerase.

Properties and inhibition of the first two enzymes of the non-mevalonate pathway of isoprenoid biosynthesis

2000 ◽  
Vol 28 (6) ◽  
pp. 792-793 ◽  
Author(s):  
C. Mueller ◽  
J. Schwender ◽  
J. Zeidler ◽  
H. K. Lichtenthaler
Keyword(s):  
Escherichia Coli ◽  
Mevalonate Pathway ◽  
Isoprenoid Biosynthesis ◽  
Mep Pathway ◽  
Ph Optimum ◽  
Antibacterial Drugs ◽  
Chloroplast Stroma

Enzymes of the 1-deoxy-D-xylulose 5-phosphate/2-C-methylerythritol 4-phosphate (DOXP/MEP) pathway are targets for new herbicides and antibacterial drugs. Until now, no inhibitors for the DOXP synthase have been known of. We show that one of the breakdown products of the herbicide clomazone affects the DOXP synthase. One inhibitor of the non-mevalonate pathway, fosmidomycin, blocks the DOXP reductoisomerase (DXR) of plants and bacteria. The I50 values of plants are, however, higher than those found for the DXR of Escherichia coli. The DXR of plants, isolated from barley seedlings, shows a pH optimum of 8.1, which is typical for enzymes active in the chloroplast stroma.

scholarly journals Enhanced Lycopene Production in Escherichia coli by Expression of Two MEP Pathway Enzymes from Vibrio sp. Dhg

Catalysts ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 1003 ◽  
Author(s):  
Min Jae Kim ◽  
Myung Hyun Noh ◽  
Sunghwa Woo ◽  
Hyun Gyu Lim ◽  
Gyoo Yeol Jung
Keyword(s):  
Escherichia Coli ◽  
Cell Membrane ◽  
Electron Transport Chain ◽  
Farnesyl Diphosphate ◽  
Mep Pathway ◽  
Farnesyl Diphosphate Synthase ◽  
Mva Pathway ◽  
Transport Chain ◽  
Lycopene Production ◽  
Specific Activities

Microbial production is a promising method that can overcome major limitations in conventional methods of lycopene production, such as low yields and variations in product quality. Significant efforts have been made to improve lycopene production by engineering either the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway or mevalonate (MVA) pathway in microorganisms. To further improve lycopene production, it is critical to utilize metabolic enzymes with high specific activities. Two enzymes, 1-deoxy-d-xylulose-5-phosphate synthase (Dxs) and farnesyl diphosphate synthase (IspA), are required in lycopene production using MEP pathway. Here, we evaluated the activities of Dxs and IspA of Vibrio sp. dhg, a newly isolated and fast-growing microorganism. Considering that the MEP pathway is closely related to the cell membrane and electron transport chain, the activities of the two enzymes of Vibrio sp. dhg were expected to be higher than the enzymes of Escherichia coli. We found that Dxs and IspA in Vibrio sp. dhg exhibited 1.08-fold and 1.38-fold higher catalytic efficiencies, respectively. Consequently, the heterologous overexpression improved the specific lycopene production by 1.88-fold. Our findings could be widely utilized to enhance production of lycopene and other carotenoids.

Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyl diphosphate from mevalonate: a novel system for the genetic analysis of the 2-C-methyl-d-erythritol 4-phosphate pathway for isoprenoid biosynthesis

2000 ◽  
Vol 353 (1) ◽  
pp. 59-67 ◽  
Author(s):  
Narciso CAMPOS ◽  
Manuel RODRÍGUEZ-CONCEPCIÓN ◽  
Susanna SAURET-GÜETO ◽  
Francesca GALLEGO ◽  
Luisa-María LOIS ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Genetic Analysis ◽  
Mevalonate Pathway ◽  
Mep Pathway ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
E Coli ◽  
Dimethylallyl Diphosphate ◽  
And Function ◽  
Synthetic Operon

Isopentenyl diphosphate (IPP) and its isomer dimethylallyl diphosphate (DMAPP) constitute the basic building block of isoprenoids, a family of compounds that is extraordinarily diverse in structure and function. IPP and DMAPP can be synthesized by two independent pathways: the mevalonate pathway and the recently discovered 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway. Although the MEP pathway is essential in most eubacteria, algae and plants and has enormous biotechnological interest, only some of its steps have been determined. We devised a system suitable for the genetic analysis of the MEP pathway in Escherichia coli. A synthetic operon coding for yeast 5-diphosphomevalonate decarboxylase, human 5-phosphomevalonate kinase, yeast mevalonate kinase and E. coli isopentenyl diphosphate isomerase was incorporated in the chromosome of this bacterium. The expression of this operon allowed the synthesis of IPP and DMAPP from mevalonate added exogenously and complementation of lethal mutants of the MEP pathway. We used this system to show that the ygbP, ychB and ygbB genes are essential in E. coli and that the steps catalysed by the products of these genes belong to the trunk line of the MEP pathway.

scholarly journals Further Insight into Crystal Structures of Escherichia coli IspH/LytB in Complex with Two Potent Inhibitors of the MEP Pathway: A Starting Point for Rational Design of New Antimicrobials

ChemBioChem ◽  
2017 ◽  
Vol 18 (21) ◽  
pp. 2137-2144 ◽  
Author(s):  
Franck Borel ◽  
Elodie Barbier ◽  
Sergiy Krasutsky ◽  
Karnjapan Janthawornpong ◽  
Philippe Chaignon ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Rational Design ◽  
Mep Pathway ◽  
Starting Point ◽  
Insight Into

scholarly journals Enhanced lycopene Production in Escherichia coli by Expression of Two MEP Pathway Enzymes from Vibrio sp. dhg

2019 ◽  
Author(s):  
Min Jae Kim ◽  
Myung Hyun Noh ◽  
Sunghwa Woo ◽  
Hyun Gyu Lim ◽  
Gyoo Yeol Jung
Keyword(s):  
Escherichia Coli ◽  
Electron Transport Chain ◽  
Farnesyl Diphosphate ◽  
Mep Pathway ◽  
Farnesyl Diphosphate Synthase ◽  
Mva Pathway ◽  
E Coli ◽  
Transport Chain ◽  
Lycopene Production ◽  
Specific Activities

Microbial production is a promising method that can overcome major limitations in conventional methods of lycopene production, such as low yields and variations in product quality. Significant efforts have been made to improve lycopene production by engineering either the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway or mevalonate (MVA) pathway in microorganisms. To further improve lycopene production, it is critical to utilize metabolic enzymes with high specific activities. Two enzymes, 1-deoxy-D-xylulose-5-phosphate synthase (Dxs) and farnesyl diphosphate synthase (IspA), are required in lycopene production using MEP pathway. Here, we evaluated the activities of Dxs and IspA of Vibrio sp. dhg, a newly isolated and fast-growing microorganism. Considering that the MEP pathway is closely related to the cell membrane and electron transport chain, the activities of the two enzymes of Vibrio sp. dhg were expected to be higher than the enzymes of E. coli. We found that Dxs and IspA in Vibrio sp. dhg exhibited 1.08-fold and 1.38-fold higher catalytic efficiencies, respectively. Consequently, the heterologous overexpression improved the specific lycopene production by 1.88-fold. Our findings could be widely utilized to enhance production of lycopene and other carotenoids.

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