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Literature summary for 2.7.1.49 extracted from
- A strictly monofunctional bacterial hydroxymethylpyrimidine phosphate kinase precludes damaging errors in thiamin biosynthesis (2017), Biochem. J., 474, 2887-2895 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a thiD knockout mutant strain, complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2, ThiD2 proteins catalyze phosphorylation of HMP monophosphate, but not of HMP or its toxic analogues and damage products such as bacimethrin and 5-(hydroxymethyl)-2-methylpyrimidin-4-ol. As strictly monofunctional HMP monophosphate kinases (EC 2.7.4.7), ThiD2 proteins eliminate a potentially fatal vulnerability of canonical ThiD, at the cost of the ability to reclaim HMP formed by thiamin turnover | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00104 | - |
4-Amino-5-hydroxymethyl-2-methylpyrimidine | pH 7.5, temperature not specified in the publication, recombinant enzyme ThiD | Escherichia coli |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | Escherichia coli | - |
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | Escherichia coli BW25113 | - |
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine | Escherichia coli | - |
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine | Escherichia coli BW25113 | - |
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P76422 | - |
- |
| Escherichia coli BW25113 | P76422 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
Escherichia coli | ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | reaction of EC 2.7.4.7 | Escherichia coli | ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
Escherichia coli BW25113 | ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | reaction of EC 2.7.4.7 | Escherichia coli BW25113 | ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine | - |
Escherichia coli | ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
? | |
| ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine | - |
Escherichia coli BW25113 | ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine | - |
? | |
| additional information | the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) | Escherichia coli | ? | - |
- |
|
| additional information | the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) | Escherichia coli BW25113 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HMP kinase | - |
Escherichia coli |
| hydroxymethylpyrimidine phosphate kinase | - |
Escherichia coli |
| More | see also EC 2.7.4.7 | Escherichia coli |
| ThiD | - |
Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.285 | - |
4-Amino-5-hydroxymethyl-2-methylpyrimidine | pH 7.5, temperature not specified in the publication, recombinant enzyme ThiD | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | ThiD is a member of the ribokinase family, but differs from other members in catalyzing two consecutive phosphorylations. The other members of the family catalyze only the phosphorylation of a hydroxymethyl group to give a monophosphate, i.e. the equivalent of the HMP kinase reaction. The HMP kinase activity of ThiD is hence presumably ancestral and the HMP-P kinase activity is an evolutionary novelty | Escherichia coli |
| metabolism | the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview | Escherichia coli |
| physiological function | the bifunctional canonical kinase (ThiD) that converts the thiamin biosynthesis intermediate hydroxymethylpyrimidine (HMP) monophosphate into the diphosphate (EC 2.7.4.7) can also very efficiently convert free HMP into the monophosphate (EC 2.7.1.49) in prokaryotes, plants, and fungi. This HMP kinase activity enables salvage of HMP, but it is not substrate-specific and so allows toxic HMP analogues and damage products to infiltrate the thiamin biosynthesis pathway | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 274.04 | - |
4-Amino-5-hydroxymethyl-2-methylpyrimidine | pH 7.5, temperature not specified in the publication, recombinant enzyme ThiD | Escherichia coli | |
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