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coli glutathione synthetase gsh-II

" Expression of the glutathione synthetase gene of Escherichia coli B in Saccharomyces cerevisiae "

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Glutathione: an overview of biosynthesis and modulation …

Glutathione biosynthesis has been traditionally viewed as a conserved process relying on the sequential activity of two separate ligases, but recently, an enzyme (GshF) that unifies both necessary reactions in one platform has been identified and characterized in a number of pathogenic and free-living bacteria.

Glutathione Synthetase is the second enzyme in the glutathione biosynthesis pathway.

N2 - Acyl carrier protein (ACPSH) functions as the acyl carrier in fatty acid biosynthesis. The acyl moieties are bound to the sole sulfhydryl of the protein located on the 4'-phosphopantetheine prosthetic group. Disulfide-linked dimers of ACPSH were formed by the reaction of ACPSH with acyl-ACP or the mixed disulfide of ACPSH and thionitrobenzoate. The formation of ACP dimers was established by electrophoresis, gel filtration, and sedimentation equilibrium. ACP purified from stationary phase Escherichia coli B cells was found to exist primarily as a mixed disulfide with glutathione. This species was identified by gel electrophoresis amino acid analysis and 31P NMR spectroscopy. A non-denaturing gel electrophoresis system was developed that allows the comparison of the effects of various protein and sulfhydryl modifications on the stability of the ACP protein moiety to pH-induced denaturation. In general, attachment of hydrophilic ligands to the sulfhydryl of ACPSH resulted in less stable protein structures whereas the presence of a hydrophobic thioester resulted in stabilization of the protein conformation. The less stable ACP structures were found to have 31P NMR chemical shifts displaced downfield from ACPSH and the more stable acyl-ACP derivatives were found to have chemical shifts displaced upfield from ACPSH.

Restricting glutathione biosynthesis to the cytosol is …

Two strains of group A streptococci and one of Escherichia coli produced hercyninelike material, as yet unidentified.


Steinbach Online, November 2017
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The protein functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione.

coli which would synthesize glutathione and its …

AB - Acyl carrier protein (ACPSH) functions as the acyl carrier in fatty acid biosynthesis. The acyl moieties are bound to the sole sulfhydryl of the protein located on the 4'-phosphopantetheine prosthetic group. Disulfide-linked dimers of ACPSH were formed by the reaction of ACPSH with acyl-ACP or the mixed disulfide of ACPSH and thionitrobenzoate. The formation of ACP dimers was established by electrophoresis, gel filtration, and sedimentation equilibrium. ACP purified from stationary phase Escherichia coli B cells was found to exist primarily as a mixed disulfide with glutathione. This species was identified by gel electrophoresis amino acid analysis and 31P NMR spectroscopy. A non-denaturing gel electrophoresis system was developed that allows the comparison of the effects of various protein and sulfhydryl modifications on the stability of the ACP protein moiety to pH-induced denaturation. In general, attachment of hydrophilic ligands to the sulfhydryl of ACPSH resulted in less stable protein structures whereas the presence of a hydrophobic thioester resulted in stabilization of the protein conformation. The less stable ACP structures were found to have 31P NMR chemical shifts displaced downfield from ACPSH and the more stable acyl-ACP derivatives were found to have chemical shifts displaced upfield from ACPSH.

Acyl carrier protein (ACPSH) functions as the acyl carrier in fatty acid biosynthesis. The acyl moieties are bound to the sole sulfhydryl of the protein located on the 4'-phosphopantetheine prosthetic group. Disulfide-linked dimers of ACPSH were formed by the reaction of ACPSH with acyl-ACP or the mixed disulfide of ACPSH and thionitrobenzoate. The formation of ACP dimers was established by electrophoresis, gel filtration, and sedimentation equilibrium. ACP purified from stationary phase Escherichia coli B cells was found to exist primarily as a mixed disulfide with glutathione. This species was identified by gel electrophoresis amino acid analysis and 31P NMR spectroscopy. A non-denaturing gel electrophoresis system was developed that allows the comparison of the effects of various protein and sulfhydryl modifications on the stability of the ACP protein moiety to pH-induced denaturation. In general, attachment of hydrophilic ligands to the sulfhydryl of ACPSH resulted in less stable protein structures whereas the presence of a hydrophobic thioester resulted in stabilization of the protein conformation. The less stable ACP structures were found to have 31P NMR chemical shifts displaced downfield from ACPSH and the more stable acyl-ACP derivatives were found to have chemical shifts displaced upfield from ACPSH.

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  • Biosynthesis of Trypanothione Protects Escherichia coli from ..

    coli harboring plasmids carrying ERG biosynthetic genes () was cultured in 3 mL of M9Y media at 30 °C for 16 h.

  • in glutathione biosynthesis, ..

    coli has an orthologue, , which is responsible for glutathione biosynthesis, we expressed the other genes, , , , and .

  • Glutathione biosynthesis has been traditionally ..

    Systematic manipulation of glutathione metabolism in Escherichia coli for improved glutathione production

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