node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
btuE | chaC | b1710 | b1218 | 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. | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | 0.903 |
btuE | ggt | b1710 | b3447 | 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. | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | 0.932 |
btuE | gor | b1710 | b3500 | 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. | 0.986 |
btuE | gshB | b1710 | b2947 | 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. | 0.930 |
btuE | gss | b1710 | b2988 | 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. | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | 0.900 |
btuE | gstA | b1710 | b1635 | 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. | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.944 |
btuE | gstB | b1710 | b0838 | 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 S-transferase; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes the glutathione-dependent dehalogenation of bromoacetate. | 0.927 |
btuE | yfcF | b1710 | b2301 | 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 S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | 0.938 |
chaC | btuE | b1218 | b1710 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | 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. | 0.903 |
chaC | ggt | b1218 | b3447 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | 0.903 |
chaC | gor | b1218 | b3500 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.900 |
chaC | gshB | b1218 | b2947 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Protein involved in glutathione biosynthetic process. | 0.905 |
chaC | gss | b1218 | b2988 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Glutathionylspermidine amidase and glutathionylspermidine synthetase; Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. [...] | 0.900 |
chaC | gstA | b1218 | b1635 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.901 |
chaC | gstB | b1218 | b0838 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Glutathione S-transferase; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes the glutathione-dependent dehalogenation of bromoacetate. | 0.931 |
chaC | yfcF | b1218 | b2301 | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | 0.916 |
ggt | btuE | b3447 | b1710 | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | 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. | 0.932 |
ggt | chaC | b3447 | b1218 | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | Cation transport regulator; Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. | 0.903 |
ggt | gor | b3447 | b3500 | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | Glutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.925 |
ggt | gshB | b3447 | b2947 | Gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D- gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acce [...] | Protein involved in glutathione biosynthetic process. | 0.934 |