Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
M134K | phosphomethylpyrimidine kinase activity similar to wild-type, thiamin-phosphate diphosphorylase activity almost completely abolished | Zea mays |
M134K/T472D | 83-97% residual phosphomethylpyrimidine kinase activity, 19-32% residual thiamin-phosphate diphosphorylase activity | Zea mays |
Q373L | phosphomethylpyrimidine kinase activity similar to wild-type, 64-75% residual thiamin-phosphate diphosphorylase activity | Zea mays |
Q98L | phosphomethylpyrimidine kinase activity similar to wild-type, thiamin-phosphate diphosphorylase activity almost completely abolished | Zea mays |
Q98L/Q373L | phosphomethylpyrimidine kinase activity similar to wild-type, 7-13% residual thiamin-phosphate diphosphorylase activity | Zea mays |
S444A | almost complete loss of phosphomethylpyrimidine kinase activity, 80-91% residual thiamin-phosphate diphosphorylase activity | Zea mays |
T472D | phosphomethylpyrimidine kinase activity similar to wild-type, 46-54% residual thiamin-phosphate diphosphorylase activity | Zea mays |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate | uncompetitive | Zea mays | |
ATP | uncompetitive | Zea mays |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0085 | - |
4-methyl-5-(2-hydroxyethyl)thiazole phosphate | - |
Zea mays | |
0.0128 | - |
4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate | 37°C, pH 8.0 | Zea mays |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Zea mays |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
2 * 57800, calculated, 2 * 55000, SDS-PAGE | Zea mays |
57800 | - |
2 * 57800, calculated, 2 * 55000, SDS-PAGE | Zea mays |
95000 | - |
gel filtration | Zea mays |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | Q2UVH9 | isoform Thi3, bifunctional phosphomethylpyrimidine kinase/thiamin-phosphate diphosphorylase | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.05 | - |
37°C, pH 8.0, presence of ATP | Zea mays |
0.52 | - |
37°C, pH 8.0 | Zea mays |
2.46 | - |
37°C, pH 8.0, presence of Mg2+ | Zea mays |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate + 4-methyl-5-(2-hydroxyethyl)thiazole phosphate | - |
Zea mays | thiamine monophosphate + diphosphate + phosphate | - |
? | |
additional information | substrate 4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate cannot be replaced by 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate or 4-amino-5-hydroxymethyl-2-methylpyrimidine, nor substrate 4-methyl-5-(2-hydroxyethyl)thiazole phosphate by 4-methyl-5-(2-hydroxyethyl)thiazole | Zea mays | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 57800, calculated, 2 * 55000, SDS-PAGE | Zea mays |
More | the activities of bifunctional phosphomethylpyrimidine kinase/thiamin-phosphate diphosphorylase are located in two distinct, N-terminal kinase and C-terminal synthase, domains | Zea mays |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0034 | - |
ATP | - |
Zea mays | |
0.0148 | - |
4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate | 37°C, pH 8.0 | Zea mays |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Zea mays | calculated | - |
8.5 |