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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
-
the enzyme shows lower affinity to 2-methyl-4-amino-5-hydroxymethylpyrimidine monophosphate than to 2-methyl-4-amino-5-hydroxymethylpyrimidine
-
-
ir
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
ATP + 4-amino-5-hydroxy-2-methylpyrimidine
ADP + 4-amino-2-methyl-5-phosphopyrimidine
-
-
-
?
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-5-phosphomethyl-2-methylpyrimidine
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
ATP + bacimethrin
ADP + ?
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
CTP + 5-hydroxy-2-methylpyrimidine
CDP + 2-methyl-5-phosphopyrimidine
-
-
-
?
GTP + 5-hydroxy-2-methylpyrimidine
GDP + 2-methyl-5-phosphopyrimidine
-
-
-
?
UTP + 5-hydroxy-2-methylpyrimidine
UDP + 5-hydroxy-2-methylpyrimidine monophosphate
-
-
-
?
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 biosynthetic pathway, first steps
-
?
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 biosynthetic pathway, first steps
-
?
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
-
-
-
?
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 biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
involved in thiamine biosynthetic pathway, first steps
-
?
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 biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
-
-
-
ir
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
-
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
-
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
reaction of EC 2.7.4.7
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
reaction of EC 2.7.1.35
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
reaction of EC 2.7.1.35
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
reaction of EC 2.7.1.35
-
-
?
additional information
?
-
-
the enzyme has both a biosynthetic and a salvage pathway function
-
-
?
additional information
?
-
-
no activity with pyridoxal, pyridoxine, or pyridoxamine
-
-
?
additional information
?
-
bifunctional hydroxypyrimidine kinase/thiamin-phosphate pyrophosphorylase
-
-
?
additional information
?
-
-
bifunctional hydroxypyrimidine kinase/thiamin-phosphate pyrophosphorylase
-
-
?
additional information
?
-
-
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
-
-
?
additional information
?
-
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
-
-
?
additional information
?
-
-
enzyme is probably different from previously isolated HMP kinase, because the subunit molecular masses are significantly different
-
-
?
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
-
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase
-
-
?
additional information
?
-
the enzyme performs double phosphorylation on 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP)
-
-
-
additional information
?
-
-
pyridoxine, pyridoxal, and pyridoxamine are no substrates
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Thi20p is involved in thiamine synthesis from pyrithiamin and oxythiamin
-
-
?
additional information
?
-
-
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
-
-
?
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), 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), 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), 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 + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
ATP + 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine
ADP + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine
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-5-phosphomethyl-2-methylpyrimidine
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
additional information
?
-
-
the enzyme has both a biosynthetic and a salvage pathway function
-
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
ATP + 2-methyl-4-amino-5-hydroxymethylpyrimidine
ADP + 2-methyl-4-amino-5-phosphomethylpyrimidine
-
involved in thiamine biosynthetic pathway, first steps
-
?
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
-
-
-
?
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-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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
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 catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
ATP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ADP + 4-amino-5-diphosphomethyl-2-methylpyrimidine
-
enzyme also performs the reaction of EC 2.7.4.7, phosphomethylpyrimidine kinase
-
-
?
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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
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
-
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
-
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
-
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
-
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
-
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
-
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 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 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 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 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 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 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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) 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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
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 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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
physiological function
-
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
physiological function
-
the enzyme catalyzes an essential step for the biosynthesis of thiamin pyrophosphate
-
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, the same enzyme catalyzes the phosphorylation of its reaction product to generate hydroxymethylpyrimidine pyrophosphate (HMPPK, EC 2.7.4.7) being this last reaction an essential step for the biosynthesis of thiamin diphosphate
-
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 enzyme is involved in biosynthesis of thiamine
-
physiological function
-
the enzyme is involved in biosynthesis of thiamine
-
additional information
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor
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
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
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
-
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor
-
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
-
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
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