Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily.

Protein involved in glutathione biosynthetic process.

Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily.

Oxidative and nitrosative stress transcriptional regulator; Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto- [...]

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Hydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Protein involved in glutathione biosynthetic process.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.

Hydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Hydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.

Protein involved in glutathione biosynthetic process.

Hydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.

Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Protein involved in glutathione biosynthetic process.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Oxidative and nitrosative stress transcriptional regulator; Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto- [...]

Protein involved in glutathione biosynthetic process.

Glutathione peroxidase; Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert- butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. Belongs to the glutathione peroxidase family. BtuE subfamily.

Protein involved in glutathione biosynthetic process.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.

Protein involved in glutathione biosynthetic process.

Hydroxyacylglutathione hydrolase; Type II glyoxalase that catalyzes the hydrolysis of (R)-S- lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.

Protein involved in glutathione biosynthetic process.

Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Isc operon transcriptional repressor; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. Transcriptional repressor of the iscRSUA operon, which is involved in the assembly of Fe-S clusters into Fe-S proteins. In its apoform, under conditions of oxidative stress or iron deprivation, it activates the suf operon, which is a second operon involved in the assembly of Fe-S clusters. Represses its own transcription as well as that of toxin rnlA.

Oxidative and nitrosative stress transcriptional regulator; Hydrogen peroxide sensor. Activates the expression of a regulon of hydrogen peroxide-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA. OxyR expression is negatively autoregulated by binding to a 43 bp region upstream of its own coding sequence. OxyR is inactivated by reduction of its essential disulfide bond by the product of GrxA, itself positively regulated by OxyR. Has also a positive regulatory effect on the production of surface proteins that control the colony morphology and auto- [...]

Methylglyoxal synthase; Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.

Glyoxalase I, Ni-dependent; Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S- lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification (Probable). Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response.