Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition

Zhu, Jiangfeng; Shimizu, Kazuyuki

doi:10.1016/j.ymben.2004.10.004

Cited by 105 publications

(81 citation statements)

References 36 publications

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“…1). It is also consistent with the previous study which showed that the PFL flux was significantly reduced in an adhE mutant strain under microaerobic condition (Zhu and Shimizu, 2005). This may also explain the high PFL fluxes in the yfiD mutant and the yfiDarcA double mutant strains under microaerobic conditions.…”

Section: Resultssupporting

confidence: 93%

The YfiD protein contributes to the pyruvate formate‐lyase flux in an Escherichia coli arcA mutant strain

Zhu¹,

Shalel-Levanon²,

Bennett³

et al. 2006

Biotech & Bioengineering

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The product of yfiD gene is similar to pyruvate formate-lyase (PFL) activase and it has been reported to activate PFL by replacing the glycyl radical domain. To quantitate the effect of YfiD on the cell metabolism in microaerobic cultures, glucose-limited chemostat cultures were conducted with Escherichia coli yfiD mutant and yfiDarcA mutant strains. The microaerobic condition was controlled by purging the culture media with 2.5% O(2) in N(2). The intracellular metabolic flux distributions in these cultures were estimated based on C-13 labeling experiments. By comparing with the flux distributions in wild-type E. coli and the arcA mutant, it was shown that YfiD contributes to about 18% of the PFL flux in the arcA mutant, but it did not contribute to the PFL flux in wild-type E. coli. It was also shown that the cell used both PFL and pyruvate dehydrogenase (PDH) to supplement the acetyl-coenzyme A (AcCoA) pool under microaerobic conditions. The flux through PDH was about 22-30% of the total flux toward AcCoA in the wild-type, the yfiD mutant and yfiDarcA mutant strains. Relatively higher lactate production was seen in the yfiDarcA mutant than the other strains, which was due to the lower total flux through PFL and PDH toward AcCoA in this strain.

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Section: Resultssupporting

confidence: 93%

The YfiD protein contributes to the pyruvate formate‐lyase flux in an Escherichia coli arcA mutant strain

Zhu¹,

Shalel-Levanon²,

Bennett³

et al. 2006

Biotech & Bioengineering

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“…The pfl1 mutant cells also accumulate elevated intracellular levels of amino acids, which may help recycle NADH and limit the potentially damaging consequences of pyruvate accumulation Zabalza et al, 2009). Aspects of electron rerouting observed in the Chlamydomonas pfl1 strain are similar to those observed for analogous E. coli mutants (Clark, 1989;Zhu and Shimizu, 2005), suggesting that the pathways and potentially some of the compensatory mechanisms are conserved between bacteria and eukaryotic green algae.…”

supporting

confidence: 58%

“…In E. coli, adhE mutants exhibit increased acetate production and lower lactate/formate levels under microaerobic conditions, consistent with a down-regulation of both PFL and LDH activities in the mutant strain (Zhu and Shimizu, 2005). At this point, there is no experimental evidence that defines the participation of the three potential ADH proteins of Chlamydomonas in fermentative ethanol production.…”

mentioning

confidence: 94%

A Mutant in theADH1Gene ofChlamydomonas reinhardtiiElicits Metabolic Restructuring during Anaerobiosis

et al. 2012

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The green alga Chlamydomonas reinhardtii has numerous genes encoding enzymes that function in fermentative pathways. Among these, the bifunctional alcohol/acetaldehyde dehydrogenase (ADH1), highly homologous to the Escherichia coli AdhE enzyme, is proposed to be a key component of fermentative metabolism. To investigate the physiological role of ADH1 in dark anoxic metabolism, a Chlamydomonas adh1 mutant was generated. We detected no ethanol synthesis in this mutant when it was placed under anoxia; the two other ADH homologs encoded on the Chlamydomonas genome do not appear to participate in ethanol production under our experimental conditions. Pyruvate formate lyase, acetate kinase, and hydrogenase protein levels were similar in wild-type cells and the adh1 mutant, while the mutant had significantly more pyruvate:ferredoxin oxidoreductase. Furthermore, a marked change in metabolite levels (in addition to ethanol) synthesized by the mutant under anoxic conditions was observed; formate levels were reduced, acetate levels were elevated, and the production of CO 2 was significantly reduced, but fermentative H 2 production was unchanged relative to wild-type cells. Of particular interest is the finding that the mutant accumulates high levels of extracellular glycerol, which requires NADH as a substrate for its synthesis. Lactate production is also increased slightly in the mutant relative to the control strain. These findings demonstrate a restructuring of fermentative metabolism in the adh1 mutant in a way that sustains the recycling (oxidation) of NADH and the survival of the mutant (similar to wild-type cell survival) during dark anoxic growth.

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“…Various applications are reported, such as optimization of synthesis of amino-acids (AA), [19][20][21][22] ethanol, [23][24] succinate, 25 lactate, 26 or other metabolites in mutant cells 27,28 . Deterministic simulation platforms allow in silico design of modified cells with desirable gene circuits and 'motifs' of practical applications in the biosynthesis industry, environmental engineering, and medicine.…”

Section: Department Of Chemical and Biochemical Engineering University mentioning

confidence: 99%

unIn silico Derivation of a Reduced Kinetic Model for Stationary or Oscillating Glycolysis in Escherichia coli Bacterium

Maria

2015

Chem.Biochem.Eng.Q.

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Effect of a single-gene knockout on the metabolic regulation in Escherichia coli for D-lactate production under microaerobic condition

Cited by 105 publications

References 36 publications

The YfiD protein contributes to the pyruvate formate‐lyase flux in an Escherichia coli arcA mutant strain

The YfiD protein contributes to the pyruvate formate‐lyase flux in an Escherichia coli arcA mutant strain

A Mutant in theADH1Gene ofChlamydomonas reinhardtiiElicits Metabolic Restructuring during Anaerobiosis

unIn silico Derivation of a Reduced Kinetic Model for Stationary or Oscillating Glycolysis in Escherichia coli Bacterium

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