node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GGT1 | GGT6 | ENSSSCP00000030498 | ENSSSCP00000018943 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Gamma-glutamyltransferase 6. | 0.935 |
GGT1 | GGT7 | ENSSSCP00000030498 | ENSSSCP00000007757 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Gamma-glutamyltransferase 7. | 0.921 |
GGT1 | GPX1 | ENSSSCP00000030498 | ENSSSCP00000042853 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Glutathione peroxidase 1; Protects the hemoglobin in erythrocytes from oxidative breakdown. | 0.915 |
GGT1 | GPX4 | ENSSSCP00000030498 | ENSSSCP00000046912 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Phospholipid hydroperoxide glutathione peroxidase; Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide. Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non- apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (By similarity). The presence of s [...] | 0.913 |
GGT1 | GPX5 | ENSSSCP00000030498 | ENSSSCP00000001283 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Epididymal secretory glutathione peroxidase; May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction. | 0.910 |
GGT1 | GPX7 | ENSSSCP00000030498 | ENSSSCP00000037921 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Glutathione peroxidase; Belongs to the glutathione peroxidase family. | 0.910 |
GGT1 | GSR | ENSSSCP00000030498 | ENSSSCP00000016790 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Glutathione reductase; Maintains high levels of reduced glutathione in the cytosol. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.916 |
GGT1 | GSS | ENSSSCP00000030498 | ENSSSCP00000034338 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Glutathione synthetase. | 0.958 |
GGT1 | PRDX6 | ENSSSCP00000030498 | ENSSSCP00000053767 | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | Peroxiredoxin-6; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role [...] | 0.919 |
GGT6 | GGT1 | ENSSSCP00000018943 | ENSSSCP00000030498 | Gamma-glutamyltransferase 6. | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.935 |
GGT6 | GGT7 | ENSSSCP00000018943 | ENSSSCP00000007757 | Gamma-glutamyltransferase 6. | Gamma-glutamyltransferase 7. | 0.945 |
GGT6 | GPX1 | ENSSSCP00000018943 | ENSSSCP00000042853 | Gamma-glutamyltransferase 6. | Glutathione peroxidase 1; Protects the hemoglobin in erythrocytes from oxidative breakdown. | 0.910 |
GGT6 | GPX4 | ENSSSCP00000018943 | ENSSSCP00000046912 | Gamma-glutamyltransferase 6. | Phospholipid hydroperoxide glutathione peroxidase; Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins. Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide. Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non- apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (By similarity). The presence of s [...] | 0.910 |
GGT6 | GPX5 | ENSSSCP00000018943 | ENSSSCP00000001283 | Gamma-glutamyltransferase 6. | Epididymal secretory glutathione peroxidase; May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. Since the purified porcine enzyme has very little activity towards hydrogen peroxide or organic hydroperoxides the protective effect is not likely to be exerted by its enzymatic activity. Instead, may protect sperm from premature acrosome reaction in the epididymis by binding to lipid peroxides, which might otherwise interact with phospholipase A2 and induce the acrosome reaction. | 0.910 |
GGT6 | GPX7 | ENSSSCP00000018943 | ENSSSCP00000037921 | Gamma-glutamyltransferase 6. | Glutathione peroxidase; Belongs to the glutathione peroxidase family. | 0.910 |
GGT6 | GSR | ENSSSCP00000018943 | ENSSSCP00000016790 | Gamma-glutamyltransferase 6. | Glutathione reductase; Maintains high levels of reduced glutathione in the cytosol. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. | 0.912 |
GGT6 | GSS | ENSSSCP00000018943 | ENSSSCP00000034338 | Gamma-glutamyltransferase 6. | Glutathione synthetase. | 0.957 |
GGT6 | PRDX6 | ENSSSCP00000018943 | ENSSSCP00000053767 | Gamma-glutamyltransferase 6. | Peroxiredoxin-6; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role [...] | 0.912 |
GGT7 | GGT1 | ENSSSCP00000007757 | ENSSSCP00000030498 | Gamma-glutamyltransferase 7. | Glutathione hydrolase 1 heavy chain; Cleaves the gamma-glutamyl bond of extracellular 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. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione [...] | 0.921 |
GGT7 | GGT6 | ENSSSCP00000007757 | ENSSSCP00000018943 | Gamma-glutamyltransferase 7. | Gamma-glutamyltransferase 6. | 0.945 |