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Literature summary for 4.4.1.1 extracted from
- Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis (2004), Appl. Environ. Microbiol., 70, 3766-3768.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| immobilization on aminohexyl-Sepharose | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CTT | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
0.1 M potassium phosphate buffer | Saccharomyces cerevisiae |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 55 | 0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 55 | rapid loss of activity at 60°C, 0.1 M potassium phosphate buffer, pH 7.8, 0.2 mM pyridoxal-5'-phosphate and 1 mM EDTA | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
0.1 M potassium phosphate buffer | Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Saccharomyces cerevisiae |  |
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Release 2023.1 (January 2023)
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