Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetaldehyde | the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition | Clostridium pasteurianum | |
glycine | the enzymic cleavage of L-threonine stops when about 30% of the amino acid is converted to glycine and acetaldehyde. By dialysis of the incubation medium against buffer the full activity of the enzyme is restored, product inhibition | Clostridium pasteurianum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium pasteurianum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threonine | no activity with L-allo-threonine | Clostridium pasteurianum | glycine + acetaldehyde | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Clostridium pasteurianum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Clostridium pasteurianum |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.01 | - |
glycine | pH and temperature not specified in the publication | Clostridium pasteurianum | |
0.4 | - |
acetaldehyde | pH and temperature not specified in the publication | Clostridium pasteurianum |