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Literature summary extracted from
- Mammalian selenoprotein thioredoxin/glutathione reductase: roles in disulfide bond formation and sperm maturation (2005), J. Biol. Chem., 280, 26491-26498.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.1.7 | tissue expression analysis | Mus musculus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | selenium | regulates the enzyme expression pattern, enzyme contains a catalytic selenocysteine | Mus musculus |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.7 | glutathione disulfide + NADPH | Mus musculus | - |
glutathione + NADP+ | - |
? | |
| 1.8.1.7 | glutathione disulfide + NADPH | Rattus norvegicus | - |
glutathione + NADP+ | - |
? | |
| 1.8.1.7 | additional information | Rattus norvegicus | enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4 | ? | - |
? | |
| 1.8.1.7 | additional information | Mus musculus | enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4, selenium regulates the enzyme expression pattern | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.B1 | Mus musculus | - |
- |
- |
| 1.8.1.7 | Mus musculus | - |
enzyme is a bifunctional selenoprotein | - |
| 1.8.1.7 | Rattus norvegicus | - |
enzyme is a bifunctional selenoprotein | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.8.1.7 | 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ | enzyme contains a catalytic selenocysteine | Rattus norvegicus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.8.1.B1 | testis | TGR is not detected in the testes of a 20-day-old mouse. It is highly expressed in 7-month-old mouse testes. The enzyme accumulates in testes after puberty. The protein is particularly abundant in elongating spermatids at the site of mitochondrial sheath formation but is absent in mature sperm | Mus musculus | - |
| 1.8.1.7 | heart | expression only before puberty | Mus musculus | - |
| 1.8.1.7 | liver | expression only before puberty | Mus musculus | - |
| 1.8.1.7 | lung | expression only before puberty | Mus musculus | - |
| 1.8.1.7 | additional information | tissue expression analysis | Mus musculus | - |
| 1.8.1.7 | spermatid | at the site of mitochondrial sheath formation in elongating spermatids, absent in mature sperm | Mus musculus | - |
| 1.8.1.7 | spermatid | at the site of mitochondrial sheath formation in elongating spermatids, absent in mature sperm | Rattus norvegicus | - |
| 1.8.1.7 | testis | accumulation after puberty | Mus musculus | - |
| 1.8.1.7 | testis | accumulation after puberty | Rattus norvegicus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.B1 | additional information | TGR promotes isomerization of disulfide bonds formed between glutathione peroxidase 4 and certain sperm proteins, generating a 46-kDa species containing glutathione peroxidase 4 from high molecular weight nonspecific cross-links | Mus musculus | ? | - |
? | |
| 1.8.1.7 | glutathione disulfide + NADPH | - |
Mus musculus | glutathione + NADP+ | - |
? | |
| 1.8.1.7 | glutathione disulfide + NADPH | - |
Rattus norvegicus | glutathione + NADP+ | - |
? | |
| 1.8.1.7 | additional information | enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4 | Rattus norvegicus | ? | - |
? | |
| 1.8.1.7 | additional information | enzyme forms a disulfide bond formation system together with glutathione peroxidase GPx4, selenium regulates the enzyme expression pattern | Mus musculus | ? | - |
? | |
| 1.8.1.7 | additional information | enzyme can catalyze isomerization of protein and interprotein disulfide bonds, the function is localized in the thiol domain | Mus musculus | ? | - |
? | |
| 1.8.1.7 | additional information | enzyme can catalyze isomerization of protein and interprotein disulfide bonds, the function is localized in the thiol domain | Rattus norvegicus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.8.1.7 | More | enzyme is a fusion protein consisting of an N-terminal glutaredoxin domain and the thioredoxin reductase module | Mus musculus |
| 1.8.1.7 | More | enzyme is a fusion protein consisting of an N-terminal glutaredoxin domain and the thioredoxin reductase module | Rattus norvegicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.B1 | TGR | - |
Mus musculus |
| 1.8.1.B1 | thioredoxin-glutathione reductase | - |
Mus musculus |
| 1.8.1.7 | thioredoxin/glutathione reductase | - |
Rattus norvegicus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | NADPH | - |
Mus musculus | |
| 1.8.1.7 | NADPH | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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