Engineered heterologous FPP synthases-mediated Z,E-FPP synthesis in E. coli

Wang, Chonglong; Zhou, Jia; Jang, Hui-Jeong; Yoon, Sang-Hwal; Kim, Jae‐Yean; Lee, Dae-Hee; Choi, Eui‐Sung; Kim, Seon-Won

doi:10.1016/j.ymben.2013.04.002

Cited by 29 publications

(27 citation statements)

References 47 publications

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“…The fusion product of monoterpene synthase with IspA may be an interesting platform for excess GPP supply to overproduce monoterpenebased biofuels. It was also reported that the Z,E-isoform of FPP did not restore the growth of the ispA deletion mutant and that it was not metabolized by E. coli for the synthesis of its essential isoprenoids (57). Utilization of isoprenoid precursor isomers also reduced the precursors' flux toward other endogenous isoprenoids.…”

Section: Figmentioning

confidence: 99%

“…3). For the production of farnesol (another sesquiterpene derivative) in E. coli, endogenous phosphatases and pyrophosphatases have been utilized (33,56,57). Later sections briefly discuss strain improvement strategies for the overproduction of isoprenoid-based biofuels and fuel precursors from prokaryotic hosts.…”

Section: Isoprenoid Biosynthesismentioning

confidence: 99%

“…Later, Wang and coworkers produced a Z,E isoform of FOH (Z,E-FOH), via expression of a heterologous Z,E-FPP synthase (Rv1086) from Mycobacterium tuberculosis in E. coli (57). In nature, the chain elongation of the newly formed double bonds can proceed in two possible stereospecific configurations of E and Z.…”

Section: Figmentioning

confidence: 99%

“…This allowed Rv1068 to effectively compete with IspA for GPP and IPP. Z,E-FOH at 115 mg liter Ϫ1 was produced by the engineered strain harboring the IspA-Rv1068 fusion product, which was 80.7% of the total FOH production (57). The strategy of using the fusion protein might also be utilized for the production of monoterpenes in microbial hosts, where efficient GPP synthase is not available.…”

Section: Figmentioning

confidence: 99%

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Isoprenoid-Based Biofuels: Homologous Expression and Heterologous Expression in Prokaryotes

Phulara

Chaturvedi

Gupta

2016

Appl Environ Microbiol

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bEnthusiasm for mining advanced biofuels from microbial hosts has increased remarkably in recent years. Isoprenoids are one of the highly diverse groups of secondary metabolites and are foreseen as an alternative to petroleum-based fuels. Most of the prokaryotes synthesize their isoprenoid backbone via the deoxyxylulose-5-phosphate pathway from glyceraldehyde-3-phosphate and pyruvate, whereas eukaryotes synthesize isoprenoids via the mevalonate pathway from acetyl coenzyme A (acetyl-CoA). Microorganisms do not accumulate isoprenoids in large quantities naturally, which restricts their application for fuel purposes. Various metabolic engineering efforts have been utilized to overcome the limitations associated with their natural and nonnatural production. The introduction of heterologous pathways/genes and overexpression of endogenous/homologous genes have shown a remarkable increase in isoprenoid yield and substrate utilization in microbial hosts. Such modifications in the hosts' genomes have enabled researchers to develop commercially competent microbial strains for isoprenoid-based biofuel production utilizing a vast array of substrates. The present minireview briefly discusses the recent advancement in metabolic engineering efforts in prokaryotic hosts for the production of isoprenoid-based biofuels, with an emphasis on endogenous, homologous, and heterologous expression strategies.

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Section: Figmentioning

confidence: 99%

Section: Isoprenoid Biosynthesismentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

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Isoprenoid-Based Biofuels: Homologous Expression and Heterologous Expression in Prokaryotes

Phulara

Chaturvedi

Gupta

2016

Appl Environ Microbiol

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“…Modulating a synthetic pathway in a dynamic manner would result in a decreased metabolic burden to the host than the aforementioned static regulations. Isoprenyl diphosphates, including FPP, are toxic to E. coli when they overaccumulate in cells [25,35]. It is desirable to dynamically control the santalol synthetic pathway using an FPP responsive promoter, and this approach has been demonstrated in amorphadiene synthesis in E. coli [36].…”

Section: Engineering a Robust Santalol Synthetic Pathway In E Colimentioning

confidence: 99%

Shaking up ancient scents: Insights into santalol synthesis in engineered Escherichia coli

Wang

Kim

2015

Process Biochemistry

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Insight into Isoprenoid Biosynthesis by Functional Analysis of Isoprenyl Diphosphate Synthases from Mycobacterium vanbaalenii and Mycobacterium tuberculosis

et al. 2020

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Comprehensive functional analyses of E-isoprenyl diphosphate synthases (E-IDSs) from nonpathogenic Mycobacterium vanbaalenii have been performed. Mv0992 and Mv1577 represent a nonaprenyl diphosphate (E-C 45) synthase and a geranylgeranyl diphosphate (E-C 20) synthase, respectively. Although Mv3536 was identified as an E-C 20 synthase using a single enzyme, coincubation of Mv3536 and Z-IDSs (Mv4662 and Mv3822) strongly suggested it releases an intermediate geranyl diphosphate (E-C 10) during a continuous condensation reaction. Mv0992 and Mv3536 functions differed from those of the previously reported pathogenic Mycobacterium tuberculosis homologues Rv0562 and Rv2173, respectively. Re-analysis of Rv0562 and Rv2173 demonstrated that their functions were similar to those of Mv0992 and Mv3536 (Rv0562: E-C 45 synthase; Rv2173: E-C 10-15 synthase). The newly proposed functions of Rv0562 and Rv2173 would be in the biosynthesis of menaquinone and glycosyl carrier lipids essential for growth. Furthermore, a reduced allylic diphosphate could be used as the Z-IDS of the Mv3822 substrate, thereby introducing a potentially novel pathway of cyclic sesquarterpene biosynthesis.

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Engineered heterologous FPP synthases-mediated Z,E-FPP synthesis in E. coli

Cited by 29 publications

References 47 publications

Isoprenoid-Based Biofuels: Homologous Expression and Heterologous Expression in Prokaryotes

Isoprenoid-Based Biofuels: Homologous Expression and Heterologous Expression in Prokaryotes

Shaking up ancient scents: Insights into santalol synthesis in engineered Escherichia coli

Insight into Isoprenoid Biosynthesis by Functional Analysis of Isoprenyl Diphosphate Synthases from Mycobacterium vanbaalenii and Mycobacterium tuberculosis

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