Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli Rosetta (DE3) cells | Bombyx mori |
General Stability | Organism |
---|---|
if instead of the phosphate buffer an acetate buffer is used, enzymatic activity is reduced to 74% and almost no activity is recorded when a citrate buffer is used | Bombyx mori |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0441 | - |
pyridoxal | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori | |
0.0579 | - |
ATP | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | - |
Bombyx mori | |
Co2+ | - |
Bombyx mori | |
Fe2+ | - |
Bombyx mori | |
K+ | when only triethanolamine is present as the cation, K+ is an activator of the enzyme | Bombyx mori | |
Mn2+ | - |
Bombyx mori | |
Zn2+ | Zn2+ is the most effective cation for catalysis under saturating substrate concentrations | Bombyx mori |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33900 | - |
2 * 33900, SDS-PAGE | Bombyx mori |
68000 | - |
gel filtration | Bombyx mori |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bombyx mori | Q1PCB1 | - |
- |
Purification (Comment) | Organism |
---|---|
Ni Sepharose affinity column chromatography | Bombyx mori |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.07 | - |
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori |
1.8 | - |
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + pyridoxal | - |
Bombyx mori | ADP + pyridoxal 5'-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 33900, SDS-PAGE | Bombyx mori |
Synonyms | Comment | Organism |
---|---|---|
PLK | - |
Bombyx mori |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Bombyx mori |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
greatest stability is at below 40°C | Bombyx mori |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.23 | - |
ATP | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori | |
1.35 | - |
pyridoxal | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | 6 | - |
Bombyx mori |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4.5 | 8.5 | the enzyme is inactive below pH 4.5. Enzyme activity decreases slowly above pH 6.0, to approximately 35% at pH 8.5 | Bombyx mori |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Bombyx mori | calculated from amino acid sequence | - |
6.3 |
General Information | Comment | Organism |
---|---|---|
physiological function | pyridoxal kinase is a key enzyme in the metabolism of vitamin B6 | Bombyx mori |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
21.2 | - |
ATP | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori | |
30.6 | - |
pyridoxal | in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C | Bombyx mori |