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ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate
ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
additional information
?
-
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthesis
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
-
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
enzyme has both 2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate kinase and thiamin-phosphate diphosphatase activities
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
enzyme has both 2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate kinase and thiamin-phosphate diphosphatase activities, involved in thiamine biosynthesis
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
-
-
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
-
specific for ATP
product demonstrated in crude extract
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
enzyme is required for thiamin biosynthesis
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
the Thi20p protein has a greater ability than the Thi21p protein to catalyze the reaction
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
enzyme is required for thiamin biosynthesis
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
the Thi20p protein has a greater ability than the Thi21p protein to catalyze the reaction
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
the enzyme is involved in biosynthesis of thiamine
-
-
?
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
Thi20p is involved in thiamine synthesis from pyrithiamin and oxythiamin
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate
ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthesis
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
the enzyme is involved in biosynthesis of thiamine
-
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
enzyme has both 2-methyl-4-amino-5-hydroxymethylpyrimidine phosphate kinase and thiamin-phosphate diphosphatase activities, involved in thiamine biosynthesis
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
-
-
-
?
ATP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ADP + 2-methyl-4-amino-5-diphosphomethylpyrimidine
-
specific for ATP
product demonstrated in crude extract
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
-
-
-
?
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
enzyme is required for thiamin biosynthesis
-
-
?
ATP + 4-amino-2-methyl-phosphomethylpyrimidine
ADP + 4-amino-2-methyl-5-diphosphomethylpyrimidine
-
enzyme is required for thiamin biosynthesis
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
evolution
ThiN is a versatile domain of transcriptional repressors and catalytic enzymes of thiamine biosynthesis in archaea, residues that distinguish catalytic from noncatalytic ThiN domains, overview. Structural architecture comparisons of ThiD, ThiE, and ThiN domain-containing proteins in select haloarchaea
metabolism
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
metabolism
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
metabolism
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
metabolism
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
metabolism
the salvage of HMP is accomplished by its phosphorylation to HMP-P by the HMP kinase activity (HMPK)
metabolism
the salvage of HMP is accomplished by its phosphorylation to HMP-P by the HMP kinase activity (HMPK)
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
-
metabolism
-
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
-
metabolism
-
the enzyme takes part in the bacterial thiamin biosynthesis and salvage pathways, overview
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
metabolism
-
the enzyme is involved in the de novo pathway of thiamine biosynthesis in Haloferax volcanii. Thiamine biosynthesis in archaea is regulated by a transcriptional repressor, ThiR, and not by a riboswitch
-
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
physiological function
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme StHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
physiological function
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme TtHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
physiological function
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. ThiD2 genes confer resistance to bacimethrin
physiological function
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. ThiD2 genes confer resistance to bacimethrin
physiological function
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
physiological function
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
physiological function
the enzyme is involved in biosynthesis of thiamine
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme StHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
physiological function
-
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. ThiD2 genes confer resistance to bacimethrin
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme StHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
physiological function
-
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. ThiD2 genes confer resistance to bacimethrin
-
physiological function
-
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. ThiD2 genes confer resistance to bacimethrin
-
physiological function
-
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme TtHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
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
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the hydroxymethylpyrimidine phosphate kinases (HMPPK) encoded by the thiD gene are involved in the thiamine biosynthesis pathway, can perform two consecutive phosphorylations of 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) and are found in thermophilic and mesophilic bacteria. The enzyme TtHMPPK is able to catalyze two related reactions in consecutive steps, besides the phosphorylation of HMP to give HMP-P (EC 2.7.1.49), the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
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additional information
molecular dynamics simulation shows that Salmonella typhimurium StHMPPK and Thermus thermophilus TtHMPPK have striking differences in their conformational flexibility, which can be correlated with the hydrophobic packing and electrostatic interaction network given mainly by salt bridge bonds, but interestingly not by the number of hydrogen bond interactions as reported for other thermophilic enzymes, stucture comparisons, all-atom explicit solvent molecular dynamics simulation of StHMPPK and TtHMPPK, overview
additional information
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molecular dynamics simulation shows that Salmonella typhimurium StHMPPK and Thermus thermophilus TtHMPPK have striking differences in their conformational flexibility, which can be correlated with the hydrophobic packing and electrostatic interaction network given mainly by salt bridge bonds, but interestingly not by the number of hydrogen bond interactions as reported for other thermophilic enzymes, stucture comparisons, all-atom explicit solvent molecular dynamics simulation of StHMPPK and TtHMPPK, overview
additional information
molecular dynamics simulation shows that Salmonella typhimurium StHMPPK and Thermus thermophilus TtHMPPK have striking differences in their conformational flexibility, which can be correlated with the hydrophobic packing and electrostatic interaction network given mainly by salt bridge bonds, but interestingly not by the number of hydrogen bond interactions as reported for other thermophilic enzymes, stucture comparisons, all-atom explicit solvent molecular dynamics simulation of StHMPPK and TtHMPPK, overview
additional information
-
molecular dynamics simulation shows that Salmonella typhimurium StHMPPK and Thermus thermophilus TtHMPPK have striking differences in their conformational flexibility, which can be correlated with the hydrophobic packing and electrostatic interaction network given mainly by salt bridge bonds, but interestingly not by the number of hydrogen bond interactions as reported for other thermophilic enzymes, stucture comparisons, all-atom explicit solvent molecular dynamics simulation of StHMPPK and TtHMPPK, overview
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additional information
complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2. Strains expressing a standalone ThiD2 protein are 10fold more resistant than wild-type against bacimethrin toxicity. ThiD2 genes confer resistance to bacimethrin
additional information
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complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2. Strains expressing a standalone ThiD2 protein are 10fold more resistant than wild-type against bacimethrin toxicity. ThiD2 genes confer resistance to bacimethrin
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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
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
-
additional information
complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2. Strains expressing a standalone ThiD2 protein are 10fold more resistant than wild-type against bacimethrin toxicity. ThiD2 genes confer resistance to bacimethrin
additional information
-
complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2. Strains expressing a standalone ThiD2 protein are 10fold more resistant than wild-type against bacimethrin toxicity. ThiD2 genes confer resistance to bacimethrin
-
additional information
-
complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2. Strains expressing a standalone ThiD2 protein are 10fold more resistant than wild-type against bacimethrin toxicity. ThiD2 genes confer resistance to bacimethrin
-
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Kim, Y.S.; Nosaka, K.; Downs, D.M.; Kwak, J.M.; Park, D.; Chung, I.K.; Nam, H.G.
A Brassica cDNA clone encoding a bifunctional hydroxymethylpyrimidine kinase/thiamin-phosphate pyrophosphorylase involved in thiamin biosynthesis
Plant Mol. Biol.
37
955-966
1998
Brassica napus (O48881)
brenda
Lewin, L.M.; Brown, G.M.
The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine
J. Biol. Chem.
236
2768-2771
1961
Saccharomyces cerevisiae
-
brenda
Reddick, J.J.; Kinsland, C.; Nicewonger, R.; Christian, T.; Downs, D.M.; Winkler, M.E.; Begley, T.P.
Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase
Tetrahedron
54
15983-15991
1998
Escherichia coli
-
brenda
Cheng, G.; Bennett, E.M.; Begley, T.P.; Ealick, S.E.
Crystal structure of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase from Salmonella typhimurium at 2.3.ANG. resolution
Structure
10
225-235
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Haas, A.L.; Laun, N.P.; Begley, T.P.
Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
Bioorg. Chem.
33
338-344
2005
Saccharomyces cerevisiae (Q08224)
brenda
Kawasaki, Y.; Onozuka, M.; Mizote, T.; Nosaka, K.
Biosynthesis of hydroxymethylpyrimidine pyrophosphate in Saccharomyces cerevisiae
Curr. Genet.
47
156-162
2005
Saccharomyces cerevisiae
brenda
Onozuka, M.; Konno, H.; Kawasaki, Y.; Akaji, K.; Nosaka, K.
Involvement of thiaminase II encoded by the THI20 gene in thiamin salvage of Saccharomyces cerevisiae
FEMS Yeast Res.
8
266-275
2008
Saccharomyces cerevisiae (Q08224)
brenda
French, J.B.; Begley, T.P.; Ealick, S.E.
Structure of trifunctional THI20 from yeast
Acta Crystallogr. Sect. D
67
784-791
2011
Saccharomyces cerevisiae (Q08224)
brenda
Nodwell, M.B.; Menz, H.; Kirsch, S.F.; Sieber, S.A.
Rugulactone and its analogues exert antibacterial effects through multiple mechanisms including inhibition of thiamine biosynthesis
ChemBioChem
13
1439-1446
2012
Staphylococcus aureus (P66915)
brenda
Cea, P.A.; Araya, G.; Vallejos, G.; Recabarren, R.; Alzate-Morales, J.; Babul, J.; Guixe, V.; Castro-Fernandez, V.
Characterization of hydroxymethylpyrimidine phosphate kinase from mesophilic and thermophilic bacteria and structural insights into their differential thermal stability
Arch. Biochem. Biophys.
688
108389
2020
Salmonella enterica subsp. enterica serovar Typhimurium (P55882), Salmonella enterica subsp. enterica serovar Typhimurium, Thermus thermophilus (Q5SKG3), Thermus thermophilus, Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (P55882), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P55882), Thermus thermophilus DSM 579 (Q5SKG3), Thermus thermophilus ATCC 27634 (Q5SKG3)
brenda
Thamm, A.M.; Li, G.; Taja-Moreno, M.; Gerdes, S.Y.; de Crecy-Lagard, V.; Bruner, S.D.; Hanson, A.D.
A strictly monofunctional bacterial hydroxymethylpyrimidine phosphate kinase precludes damaging errors in thiamin biosynthesis
Biochem. J.
474
2887-2895
2017
Campylobacter concisus (A7ZG21), Escherichia coli (P76422), Sulfurimonas denitrificans (Q30NV2), Sulfurimonas denitrificans DSM 1251 (Q30NV2), Campylobacter concisus 13826 (A7ZG21), Sulfurimonas denitrificans ATCC 33889 (Q30NV2), Escherichia coli BW25113 (P76422)
brenda
Hwang, S.; Cordova, B.; Abdo, M.; Pfeiffer, F.; Maupin-Furlow, J.
ThiN as a versatile domain of transcriptional repressors and catalytic enzymes of thiamine biosynthesis
J. Bacteriol.
199
e00810-16
2017
Haloferax volcanii (D4GV38), Haloferax volcanii NCIMB 2012 (D4GV38), Haloferax volcanii JCM 8879 (D4GV38), Haloferax volcanii DS2 (D4GV38), Haloferax volcanii DSM 3757 (D4GV38), Haloferax volcanii ATCC 29605 (D4GV38), Haloferax volcanii NBRC 14742 (D4GV38), Haloferax volcanii VKM B-1768 (D4GV38)
brenda