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
-
2.7.1.50
-
thiamin
-
pyrophosphate
-
monophosphate
-
salvage
-
hydroxymethylpyrimidine
-
pyrimidine
-
4-amino-5-hydroxymethyl-2-methylpyrimidine
-
2.7.1.35
-
tpp
-
protomers
-
pyrophosphorylase
-
octamer
-
2-methyl-4-amino-5-hydroxymethylpyrimidine
-
ribokinase
-
antimetabolite
- 2.7.1.50
- thiamin
- pyrophosphate
- monophosphate
-
salvage
- hydroxymethylpyrimidine
- pyrimidine
- 4-amino-5-hydroxymethyl-2-methylpyrimidine
-
2.7.1.35
- tpp
-
protomers
-
pyrophosphorylase
-
octamer
- 2-methyl-4-amino-5-hydroxymethylpyrimidine
- ribokinase
-
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
Advanced search results
Subunits
Subunits on EC 2.7.1.50 - hydroxyethylthiazole kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
homohexamer
the six protomers form a cage-like structure. Each protomer is composed of two domains, which are structurally homologous to their monofunctional bacterial counterparts. Two loop regions not found in the bacterial enzymes provide interactions between the two domains
homotrimer
octamer
-
8 * 60000, bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity, SDS-PAGE
trimer
additional information
homotrimer
the quaternary structure of SaThiM is a triangular homotrimer with dimensions of approximately 72 A on a side and 47 A thick with three independent active sites, each located within interface regions between two monomers. Secondary structure of SaThiM consists of approximately 50% alpha-helical and approximately 18% beeta-sheet structural elements, overview
homotrimer
-
the quaternary structure of SaThiM is a triangular homotrimer with dimensions of approximately 72 A on a side and 47 A thick with three independent active sites, each located within interface regions between two monomers. Secondary structure of SaThiM consists of approximately 50% alpha-helical and approximately 18% beeta-sheet structural elements, overview
-
-
residues involved in hydrogen bonds between subunits in the enzyme trimer, overview
trimer
-
residues involved in hydrogen bonds between subunits in the enzyme trimer, overview
-
as determined from crystallization data the enzyme is a trimer of identical subunits, the active site is formed at the interface between two subunits within the trimer
additional information
-
as determined from crystallization data the enzyme is a trimer of identical subunits, the active site is formed at the interface between two subunits within the trimer
additional information
-
monomer structure, docking of ternary complexes, tertiary structure, molecular modelling, overview
additional information
-
monomer structure, docking of ternary complexes, tertiary structure, molecular modelling, overview
-