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Literature summary extracted from
- Substrate inhibition of L-cysteine alpha,beta-elimination reaction catalyzed by L-cystathionine gamma-lyase of Saccharomyces cerevisiae (2002), Biosci. Biotechnol. Biochem., 66, 2706-2709.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.1 | L-cysteine | substrate inhibition mainly due to removal of cofactor | Saccharomyces cerevisiae |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.1 | 0.46 | - |
L-cysteine | - |
Saccharomyces cerevisiae | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.4.1.1 | Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.1 | L-cysteine + H2O | - |
Saccharomyces cerevisiae | sulfide + NH3 + pyruvate | - |
? | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.1 | pyridoxal 5'-phosphate | Km value 0.003 mM | Saccharomyces cerevisiae | |
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