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Literature summary for 3.4.19.6 extracted from
- Analysis of the thyrotropin-releasing hormone-degrading ectoenzyme by site-directed mutagenesis of cysteine residues. Cys68 is involved in disulfide-linked dimerization (2000), Eur. J. Biochem., 267, 2617-2623.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| full-length enzyme, mutant enzymes and truncated enzyme | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C279S | specific activity is 10fold lower than that of the wild-type enzyme | Rattus norvegicus |
| C338S | specific activity is 5fold lower than that of the wild-type enzyme | Rattus norvegicus |
| C68S | specific enzymatic activities are similar to that of the wild-type enzyme | Rattus norvegicus |
| C823S | mutant enzyme is completely inactive | Rattus norvegicus |
| C830S | mutant enzyme is completely inactive | Rattus norvegicus |
| C859S | mutant enzyme is completely inactive | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.027 | - |
Thyroliberin | mutant enzyme C279S | Rattus norvegicus |  |
| 0.0293 | - |
Thyroliberin | mutant enzyme C68S | Rattus norvegicus | |
| 0.0325 | - |
Thyroliberin | wild-type enzyme | Rattus norvegicus | |
| 0.033 | - |
Thyroliberin | mutant enzyme C338S | Rattus norvegicus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 116000 | - |
2 * 116000, proteolytically truncated enzyme form, SDS-PAGE | Rattus norvegicus |
| 230000 | - |
proteolytically truncated enzyme form, gel filtration | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| thyroliberin + H2O | - |
Rattus norvegicus | pyroglutamic acid + His-Pro-NH2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 116000, proteolytically truncated enzyme form, SDS-PAGE | Rattus norvegicus |
| More | proteolytically truncated and enzymatically fully active enzyme consists of two subunits that are associated noncovalently by protein-protein interactions but not via S-S bridges | Rattus norvegicus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 40 | 40 min, stable | Rattus norvegicus |
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Release 2023.1 (January 2023)
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