2.7.1.50: hydroxyethylthiazole kinase
This is an abbreviated version!
For detailed information about hydroxyethylthiazole kinase, go to the full flat file.
Word Map on EC 2.7.1.50
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2.7.1.50
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thiamin
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pyrophosphate
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monophosphate
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salvage
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hydroxymethylpyrimidine
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pyrimidine
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4-amino-5-hydroxymethyl-2-methylpyrimidine
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2.7.1.35
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tpp
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protomers
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pyrophosphorylase
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octamer
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2-methyl-4-amino-5-hydroxymethylpyrimidine
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ribokinase
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antimetabolite
- 2.7.1.50
- thiamin
- pyrophosphate
- monophosphate
-
salvage
- hydroxymethylpyrimidine
- pyrimidine
- 4-amino-5-hydroxymethyl-2-methylpyrimidine
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2.7.1.35
- tpp
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protomers
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pyrophosphorylase
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octamer
- 2-methyl-4-amino-5-hydroxymethylpyrimidine
- ribokinase
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antimetabolite
Reaction
Synonyms
4-methyl-5-(beta-hydroxyethyl) thiazole kinase, 4-methyl-5-(beta-hydroxyethyl)thiazole kinase, 4-methyl-5-beta-hydroxyethylthiazole kinase, 4-methyl-5-beta-hydroxyethylthiazole kinase
ECTree
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General Information
General Information on EC 2.7.1.50 - hydroxyethylthiazole kinase
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evolution
malfunction
metabolism
physiological function
additional information
THI6 is a bifunctional enzyme found in the thiamin biosynthetic pathway in eukaryotes. In prokaryotes, thiamin phosphate synthase and 4-methyl-5-hydroxyethylthiazole kinase are separate gene products
evolution
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three-quarters of the residues involved in interfacial regions are conserved, also the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK)
evolution
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three-quarters of the residues involved in interfacial regions are conserved, also the amino-acid residues in the nucleotide-binding, magnesium ion-binding and substrate-binding sites are conserved. The overall structure of PhThiK is similar to those of Bacillus subtilis ThiK (BsThiK) and Enterococcus faecalis V583 ThiK (EfThiK)
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thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional cofactors by the bacterium, can function as prodrugs which thus block various cofactor dependent pathways
malfunction
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thiamin analogous compounds, when introduced into the vitamin B1 biosynthetic pathway and further converted into non-functional cofactors by the bacterium, can function as prodrugs which thus block various cofactor dependent pathways
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THI6 is a bifunctional enzyme of the thiamin biosynthetic pathway
metabolism
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway
metabolism
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enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway
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the N-terminal domain of THI6 catalyzes the ligation of the thiamin thiazole and pyrimidine moieties to form thiamin phosphate, and the C-terminal domain catalyzes the phosphorylation of 4-methyl-5-hydroxyethylthiazole in a salvage pathway
physiological function
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway. Thiamin in its activated form, thiamin diphosphate, is an essential cofactor for all organisms
physiological function
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enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway. Thiamin in its activated form, thiamin diphosphate, is an essential cofactor for all organisms
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the enzyme topology shows the typical ribokinase fold of an alpha/beta protein. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the trimeric quaternary association
additional information
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the enzyme topology shows the typical ribokinase fold of an alpha/beta protein. Binding of the nucleotide and substrate to the ThiK enzyme do not influence the trimeric quaternary association
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