Glycolytic pathway as an ATP generation system and its application to the production of glutathione and NADP

Murata, Kousaku; Tani, Keiko; Chibata, Ichiro

doi:10.1016/0141-0229(81)90092-2

Cited by 35 publications

(25 citation statements)

References 11 publications

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“…The glutathione production using a permeable cellular ATP‐regenerating system has been studied for a cost‐effective supply of ATP for glutathione production. However, the efficiency of the ATP regeneration for glutathione production is only 0.5% of the ATP synthesized by the glycolytic pathway (Murata et al , 1981). Recently, Liao et al (2008) found that the irreversible transformation of added adenosine into hypoxanthine was one of the reasons why the efficiency of ATP regeneration in glutathione production was quite low in E. coli .…”

Section: Introductionmentioning

confidence: 99%

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Hara

Shimodate

Hirokawa

et al. 2009

FEMS Microbiology Letters

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There is an ongoing demand to improve the ATP-regenerating system for industrial ATP-driven bioprocesses because of the low efficiency of ATP regeneration. To address this issue, we investigated the efficiency of ATP regeneration in Escherichia coli using the Permeable Cell Assay. This assay identified 40 single-gene deletion strains that had over 150% higher total cellular ATP synthetic activity relative to the parental strain. Most of them also showed higher ATP-driven glutathione synthesis. The deleted genes of the identified strains that showed increased efficiency of ATP regeneration for glutathione production could be divided into the following four groups: (1) glycolytic pathway-related genes, (2) genes related to degradation of ATP or adenosine, (3) global regulatory genes, and (4) genes whose contribution to the ATP regeneration is unknown. Furthermore, the high glutathione productivity of DeltanlpD, the highest glutathione-producing mutant strain, was due to its reduced sensitivity to the externally added ATP for ATP regeneration. This study showed that the Permeable Cell Assay was useful for improving the ATP-regenerating activity of E. coli for practical applications in various ATP-driven bioprocesses, much as that of glutathione production.

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Section: Introductionmentioning

confidence: 99%

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Hara

Shimodate

Hirokawa

et al. 2009

FEMS Microbiology Letters

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“…We have been studying the production of glutathione in a bioreactor system containing an ATP regenerating process. This tripeptide has been found to be continuously produced in a column packed with immobilized Escherichia coli B cells (7,8) or immobilized Saccharomyces cerevisiae cells (6,9,11,12), although the amount produced in these systems is relatively lower than the amounts produced either by organic synthesis or by extraction from yeast cells, both of which are now available industrially.…”

mentioning

confidence: 99%

Cloning of a gene responsible for the biosynthesis of glutathione in Escherichia coli B

Murata¹,

Kimura²

1982

Appl Environ Microbiol

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A gene (gshI) responsible for-y-glutamylcysteine synthetase (GSH-I) activity was cloned to construct an Escherichia coli B strain having high glutathione synthesizing activity. For this purpose, two E. coli B mutants (strains C912 and RC912) were used. C912 was deficient in GSH-I activity. RC912, a revertant of C912, had a GSH-I activity that was desensitized to feedback inhibition of reduced glutathione. To clone gshI, chromosomal DNAs of RC912 and plasmid vector pBR322 were digested with various restriction endonucleases and then ligated with T4 DNA ligase. The whole ligation mixture was used to transform C912, and the transformants were selected as tetramethylthiuramdisulfide-resistant colonies. Of about 20 resistant colonies, 2 or 3 became red when treated with nitroprusside and showed appreciably high GSH-I activities. The chimeric plasmid DNA, designated pBR322-gshI, was isolated from the strain having the highest GSH-I activity and transformed into RC912. The structure and molecular size of pBR322-gshI in RC912 were determined. The molecular size of this plasmid was 6.2 megadaltons, and the plasmid contained a 3.4-megadalton segment derived from RC912 chromosomal DNA, which included gshI gene. The GSH-I activity of RC912 cells containing pBR322-gshl was fourfold higher than that of RC912 cells without pBR322-gshI.

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“…In contrast with these conventional ATP-regenerating bioprocesses, our developed coupling system of the ATP photosynthetic vesicle with the ATP-driven enzymes (Fig. 1) has many advantages: (1) light is economic and clean energy source producing no byproduct, (2) only centrifugation which is required for purification of the ATP photosynthetic vesicle is simpler than continuous column works that is typically required for purification of ATP-regenerating enzymes (Kino et al 2008(Kino et al , 2009) from harvested cells, and (3) cytoplasmic ATP-hydrolyzing enzymes that inhibit the ATP-regenerating efficiency can be removed in the contrast to the resting-cell (Murata et al 1981). These advantages suggest that the ATP photosynthetic vesicles have the potential to be applied as an ATP regenerator or controller for various ATPhydrolyzing bioprocesses.…”

Section: Potential Application Of the Atp Photosynthetic Vesicle In Amentioning

confidence: 99%

“…In industrial applications of ATP-regenerating bioproduction, coupled with ATP-regenerating ability of enzymes (Kino et al 2008(Kino et al , 2009 or resting cells (Murata et al 1981;Fujio and Furuya 1985;Fujio and Maruyama 1997;Mori et al 1997;Hara et al 2009), the requirement for costly ATP-supplying substrates (e.g., a phosphate donor or carbohydrate) and inhibition of production by byproducts from ATP regeneration are problems. In contrast with these conventional ATP-regenerating bioprocesses, our developed coupling system of the ATP photosynthetic vesicle with the ATP-driven enzymes (Fig.…”

Section: Potential Application Of the Atp Photosynthetic Vesicle In Amentioning

confidence: 99%

ATP Photosynthetic vesicles for light-driven bioprocesses

Hara

Suzuki

Suzuki³

et al. 2011

Biotechnol Lett

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We prepared ATP photosynthetic vesicles from inside-out membranes of Escherichia coli cells that express delta-rhodopsin (a novel light-driven H(+) transporter) and TF(0)F(1)-ATP synthase (a thermo-stable ATP synthase). These vesicles showed light-dependent ATP synthesis. Furthermore, coupling the ATP photosynthetic vesicles with an ATP-hydrolyzing hexokinase enabled light-dependent glucose consumption. The ATP photosynthetic vesicles indicate their potential to applied to light-driven ATP-regenerating bioprocess for various ATP-hydrolyzing bioproductions.

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Glycolytic pathway as an ATP generation system and its application to the production of glutathione and NADP

Cited by 35 publications

References 11 publications

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Cloning of a gene responsible for the biosynthesis of glutathione in Escherichia coli B

ATP Photosynthetic vesicles for light-driven bioprocesses

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Glycolytic pathway as an ATP generation system and its application to the production of glutathione and NADP

Cited by 35 publications

References 11 publications

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Cloning of a gene responsible for the biosynthesis of glutathione in Escherichia coli B

ATP Photosynthetic vesicles for light-driven bioprocesses

Contact Info

Product

Resources

About

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants

Glutathione production by efficient ATP-regeneratingEscherichia coliâmutants