EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    2.7.1.49 | more |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase |
Escherichia coli |
? |
- |
? |
| 2.7.1.49 | more |
enzyme is probably different from previously isolated HMP kinase, because the subunit molecular masses are significantly different |
Escherichia coli |
? |
- |
? |
| 2.7.1.49 | more |
bifunctional hydroxypyrimidine kinase/thiamin-phosphate pyrophosphorylase |
Brassica napus |
? |
- |
? |
| 2.7.1.49 | more |
the enzyme has both a biosynthetic and a salvage pathway function |
Bacillus subtilis |
? |
- |
? |
| 2.7.1.49 | more |
no activity with pyridoxal, pyridoxine, or pyridoxamine |
Bacillus subtilis |
? |
- |
? |
| 2.7.1.49 | more |
the isozymes Thi20p and Thi21p are bifunctional and show both phosphomethylpyrimidine kinase, EC 2.7.4.7, and hydroxymethylpyrimidine kinase, EC 2.7.1.49, activity, Thi20p exhibits higher activity than Thi21p |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.7.1.49 | more |
pyridoxine, pyridoxal, and pyridoxamine are no substrates |
Plasmodium falciparum |
? |
- |
? |
| 2.7.1.49 | more |
Thi20p is involved in thiamine synthesis from pyrithiamin and oxythiamin |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.7.1.49 | more |
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) |
Escherichia coli |
? |
- |
- |
| 2.7.1.49 | more |
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), it is specific for HMP and does not use pyridoxal-like molecules (pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM)) as substrates |
Salmonella enterica subsp. enterica serovar Typhimurium |
? |
- |
- |
