2.4.1.250: D-inositol-3-phosphate glycosyltransferase
This is an abbreviated version!
For detailed information about D-inositol-3-phosphate glycosyltransferase, go to the full flat file.
Reaction
Synonyms
CgMshA, MshA, MSMEG0924, mycothiol glycosyltransferases
ECTree
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General Information
General Information on EC 2.4.1.250 - D-inositol-3-phosphate glycosyltransferase
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malfunction
metabolism
physiological function
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characterization of mutant mshA::Tn5 which is defective in MshA produces no measurable amount of the pseudodisaccharide precursors of mycothiol, 1D-myo-inosityl 2-acetamido-2-deoxy-alpha-D-glucopyranoside and 1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside
malfunction
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inability to disrupt the mshA gene in Mycobacterium tuberculosis containing a single copy of mshA. Directed knock-out of the mshA gene in Mycobacterium tuberculosis Erdman is only possible when a second copy of mshA is first incorporated into the chromosome. Bacteria with only a single copy of mshA that grew after mutagenesis produced normal levels of mycothiol
malfunction
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seven independent missense or frameshift mutations within mshA are identified and characterized. Precise null deletion mutations of the mshA gene are generated by specialized transduction in three different strains of Mycobacterium tuberculosis. The mshA deletion mutants are defective in mycothiol biosynthesis, are only ethionamide-resistant and require catalase to grow. Biochemical studies suggest that the mechanism of ethionamide resistance in mshA mutants is likely due to a defect in ethionamide activation. In vivo, a mycothiol-deficient strain grows normally in immunodeficient mice, but is slightly defective for growth in immunocompetent mice. Mutations in mshA demonstrate the nonessentiality of mycothiol for growth in vitro and in vivo
malfunction
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inability to disrupt the mshA gene in Mycobacterium tuberculosis containing a single copy of mshA. Directed knock-out of the mshA gene in Mycobacterium tuberculosis Erdman is only possible when a second copy of mshA is first incorporated into the chromosome. Bacteria with only a single copy of mshA that grew after mutagenesis produced normal levels of mycothiol
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key enzyme responsible for the first step of mycothiol biosynthesis
metabolism
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key enzyme responsible for the first step of mycothiol biosynthesis
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overexpression of the gene, MshA, coding for mycothiol glycosyl transferase improves the robustness of Corynebacterium glutamicum to various stresses. Intracellular mycothiol content is increased by 114% upon overexpression of MshA. Survival rates increased by 44, 39, 90, 77, 131, 87, 52, 47, 57, 85 and 33% as compared to wild-type under stress by H2O2 (40 mM), methylglyoxal (5.8 mM), erythromycin (0.08 mg/ml), streptomycin (0.005 mg/ml), Cd2+ (0.01 mM), Mn2+ (2 mM), formic acid (0.05%), acetic acid (0.15%), levulinic acid (0.25%), furfural (7.2 mM), and ethanol (10% v/v), respectively. Increased mycothiol content also decreases the concentration of reactive oxygen species in the presence of the above stresses
physiological function
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overexpression of the gene, MshA, coding for mycothiol glycosyl transferase improves the robustness of Corynebacterium glutamicum to various stresses. Intracellular mycothiol content is increased by 114% upon overexpression of MshA. Survival rates increased by 44, 39, 90, 77, 131, 87, 52, 47, 57, 85 and 33% as compared to wild-type under stress by H2O2 (40 mM), methylglyoxal (5.8 mM), erythromycin (0.08 mg/ml), streptomycin (0.005 mg/ml), Cd2+ (0.01 mM), Mn2+ (2 mM), formic acid (0.05%), acetic acid (0.15%), levulinic acid (0.25%), furfural (7.2 mM), and ethanol (10% v/v), respectively. Increased mycothiol content also decreases the concentration of reactive oxygen species in the presence of the above stresses
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