EC Number | General Stability | Organism |
---|---|---|
5.1.1.1 | in 0.6 M to 1.5 M guanidine hydrochloride the dimeric enzyme is dissociated into a monomeric form, which is catalytically inactive | Geobacillus stearothermophilus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.1 | Geobacillus stearothermophilus | - |
- |
- |
EC Number | Renatured (Comment) | Organism |
---|---|---|
5.1.1.1 | enzyme denatured in 6 M guanidine hydrochloride is renatured either by dialysis or dilution to reduce the guanidine hydrochloride concentration | Geobacillus stearothermophilus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.1 | L-Ala | - |
Geobacillus stearothermophilus | D-Ala | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
5.1.1.1 | pyridoxal 5'-phosphate | the monomeric inactive enzyme appears to bind the cofactor pyridoxal 5'-phosphate by a non-covalent linkage, although the native dimeric enzyme binds the cofactor through an aldimine Schiff base linkage | Geobacillus stearothermophilus |