General Stability | Organism |
---|---|
bovine serum albumin stabilizes enzyme in dilute solution | Oryctolagus cuniculus |
repeated thawing and refreezing: denaturation | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-deoxypyridoxine 5'-phosphate | - |
Oryctolagus cuniculus | |
pyridoxal 5'-phosphate | - |
Oryctolagus cuniculus | |
pyridoxal 5'-phosphate oxime | - |
Oryctolagus cuniculus | |
pyridoxaloxime 5'-phosphate | - |
Oryctolagus cuniculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
27000 | - |
2 * 27000, SDS-PAGE | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyridoxamine 5'-phosphate + H2O + O2 | Oryctolagus cuniculus | in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.41 | - |
- |
Oryctolagus cuniculus |
Storage Stability | Organism |
---|---|
-20°C, 4 years stable, shell-frozen apo- and holoenzyme | Oryctolagus cuniculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyridoxamine 5'-phosphate + H2O + O2 | - |
Oryctolagus cuniculus | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? | |
pyridoxamine 5'-phosphate + H2O + O2 | in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine | Oryctolagus cuniculus | pyridoxal 5'-phosphate + NH3 + H2O2 | - |
? | |
pyridoxine 5'-phosphate + H2O + O2 | - |
Oryctolagus cuniculus | pyridoxal 5'-phosphate + H2O2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 27000, SDS-PAGE | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | bound poorly to apoenzyme | Oryctolagus cuniculus | |
FMN | binds 1 mol of FMN per mol of dimer | Oryctolagus cuniculus | |
FMN | analogs modified at position 2, 3, 7, 8, 8alpha and at the ribityl side chain are all bound by the apoenzyme but less tightly than FMN | Oryctolagus cuniculus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0018 | - |
4'-deoxypyridoxine-5'-phosphate | - |
Oryctolagus cuniculus | |
0.002 | - |
pyridoxal 5'-phosphate oxime | - |
Oryctolagus cuniculus | |
0.003 | - |
pyridoxal 5'-phosphate | - |
Oryctolagus cuniculus |