Directed Evolution of Methanococcus jannaschii Citramalate Synthase for Biosynthesis of 1-Propanol and 1-Butanol by Escherichia coli

@article{Atsumi2008DirectedEO,
  title={Directed Evolution of Methanococcus jannaschii Citramalate Synthase for Biosynthesis of 1-Propanol and 1-Butanol by Escherichia coli},
  author={Shota Atsumi and James C. Liao},
  journal={Applied and Environmental Microbiology},
  year={2008},
  volume={74},
  pages={7802 - 7808}
}
  • S. Atsumi, J. Liao
  • Published 24 October 2008
  • Biology
  • Applied and Environmental Microbiology
ABSTRACT Biofuels synthesized from renewable resources are of increasing interest because of global energy and environmental problems. We have previously demonstrated production of higher alcohols from Escherichia coli using a 2-keto acid-based pathway. Here, we took advantage of the growth phenotype associated with 2-keto acid deficiency to construct a hyperproducer of 1-propanol and 1-butanol by evolving citramalate synthase (CimA) from Methanococcus jannaschii. This new pathway, which… 
Metabolic engineering of the 2-ketobutyrate biosynthetic pathway for 1-propanol production in Saccharomyces cerevisiae
TLDR
The results indicate that the engineering of a citramalate-mediated pathway as a production method for 1-propanol in S. cerevisiae is effective and is a promising candidate for the large-scale production of 1- Propanol.
Photosynthetic production of 2-methyl-1-butanol from CO2 in cyanobacterium Synechococcus elongatus PCC7942 and characterization of the native acetohydroxyacid synthase
TLDR
The first photosynthetic production of 2-methyl-1-butanol (2MB), an energy-dense fuel molecule, from CO2 in the genetically engineered cyanobacterium Synechococcus elongatus PCC7942 is reported, suggesting the advantage of utilizing branched-chain amino acid pathways in this organism for the production of fuels and chemicals.
3-Methyl-1-butanol Biosynthesis in an Engineered Corynebacterium glutamicum
Biofuel offers a promising solution to the adverse environmental problems and depletion in reserves of fossil fuels. Higher alcohols including 3-methyl-1-butanol were paid much more attention as fuel
Dehydratase mediated 1-propanol production in metabolically engineered Escherichia coli
TLDR
It is speculated that dragging more carbon flux towards methylglyoxal by manipulating glycolytic pathway and eliminating competing pathways such as lactate generation can further enhance the production of 1-propanol.
ATP drives direct photosynthetic production of 1-butanol in cyanobacteria
TLDR
It is shown that artificially engineered ATP consumption through a pathway modification can drive this reaction forward and enables for the first time the direct photosynthetic production of 1-butanol from cyanobacteria Synechococcus elongatus PCC 7942.
Metabolic engineering of Escherichia coli for the production of 1-propanol.
Systematically engineering Escherichia coli for enhanced production of 1,2-propanediol and 1-propanol.
TLDR
The production of 1,2-propanediol at enhanced titer and enhanced yield simultaneously in E. coli for the first time is reported and an efficient system for the production of biofuel 1- Propanol biologically is established.
Fermentative production of 1-propanol from sugars using wild-type and recombinant Shimwellia blattae
TLDR
Two 1,2-PD production pathways were constructed in S. blattae, resulting in two methods for 1-propanol production with the bacterium, which is expected to be used as a fuel substitute and a precursor of polypropylene.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 21 REFERENCES
Metabolic engineering of Escherichia coli for 1-butanol and 1-propanol production via the keto-acid pathways.
Isoleucine Biosynthesis in Leptospira interrogans Serotype lai Strain 56601 Proceeds via a Threonine-Independent Pathway
TLDR
The existence of a leucine-like pathway for isoleucine biosynthesis in L. interrogans under physiological conditions was unequivocally proven and the similarity of this metabolic pathway in leptospires and archaea is consistent with the evolutionarily primitive status of the eubacterial spirochetes.
Metabolic engineering of Escherichia coli for 1-butanol production.
Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli.
TLDR
A mechanism is proposed for the enzyme that involves irreversible and rate-determining reaction of pyruvate, at a site which accepts 2-ketobutyrate poorly, if at all, to form an intermediate common to all the reactions.
Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
TLDR
This strategy uses the host’s highly active amino acid biosynthetic pathway and diverts its 2-keto acid intermediates for alcohol synthesis to achieve high-yield, high-specificity production of isobutanol from glucose.
( R )-Citramalate Synthase in Methanogenic Archaea
TLDR
The Methanococcus jannaschii gene MJ1392 was cloned, and its protein product was hyperexpressed in Escherichia coli and shown to catalyze the condensation of pyruvate and acetyl coenzyme A, with the formation of (R)-citramalate.
Multiple pathways for isoleucine biosynthesis in the spirochete Leptospira
TLDR
It is found that the pyruvate pathway is not controlled by leucine and that the two isoleucine pathways are independently regulated.
The effects of feed and intracellular pyruvate levels on the redistribution of metabolic fluxes in Escherichia coli.
TLDR
The role of the intracellular pyruvate pool in the redirection of metabolic fluxes at this important node is focused on and the increased competitiveness of the lactate pathway may be due to the allosteric activation of LDH as a result of increased pyruve levels.
Distribution of the Isopropylmalate Pathway to Leucine Among Diverse Bacteria
TLDR
Results suggest that the isopropylmalate pathway is widespread among organisms that can synthesize leucine.
Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis.
  • N. Koon, C. Squire, E. Baker
  • Chemistry, Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2004
TLDR
Sequence and structural similarities point to a catalytic mechanism similar to that of malate synthase and an evolutionary relationship with an aldolase that catalyzes the reverse reaction on a similar substrate.
...
1
2
3
...