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2.7.1.89: thiamine kinase

This is an abbreviated version!
For detailed information about thiamine kinase, go to the full flat file.

Word Map on EC 2.7.1.89

Reaction

ATP
+
thiamine
=
ADP
+
thiamine phosphate

Synonyms

ATP:thiamin phosphotransferase, kinase, thiamin (phosphorylating), thiamin kinase, thiamin kinase (phosphorylating), thiamin phosphokinase, ThiK, YcfN

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.89 thiamine kinase

General Information

General Information on EC 2.7.1.89 - thiamine kinase

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a thiK deletion strain (DELTAthiK) reveals decreased thiamine sensitivity, since this enzyme is required for the phosphorylation of thiamine to thiamine diphosphate. Deleting the thiamine kinase ThiK abolishes thiamine and triazolethiamine-dependent inhibition of reporter gene expression. The reporter gene expression in the thiK deletion strain is dramatically decreased in the presence of pyrithiamine
metabolism
thiamine is synthesized from two precursors, hydroxymethylpyrimidine diphosphate and hydroxyethylthiazole phosphate, which are produced independently and finally joined to form thiamine phosphate
physiological function
riboswitches are conserved regions within mRNA molecules that bind specific metabolites and regulate gene expression. TPP-riboswitches, which respond to thiamine diophosphate, are involved in the regulation of thiamine metabolism. Thiamine analogues containing a central 1,2,3-triazole group induce repression of thiM-riboswitch dependent gene expression in different Escherichiac coli strains. Triazolethiamine shows concentration-dependent reporter gene repression that is dependent on the presence of thiamine kinase ThiK, whereas the effect of pyrithiamine, a known TPP-riboswitch modulator, is ThiK-independent, overview. ThiK dependency is bypassed by triazolethiamine-derivatives that bear phosphate mimicking and metal-ion chelating moieties