Any feedback?
Information on EC 2.7.1.50 - hydroxyethylthiazole kinase
for references in articles please use BRENDA:EC2.7.1.50Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.50 hydroxyethylthiazole kinaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
hydroxyethylthiazole kinase, thz kinase, 4-methyl-5-beta-hydroxyethylthiazole kinase, 4-methyl-5-hydroxyethylthiazole kinase, thiazole kinase, grmzm2g094558, at3g24030, sathim, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-methyl-5-(beta-hydroxyethyl)thiazole kinase
-
-
-
-
4-methyl-5-beta-hydroxyethylthiazole kinase
4-methyl-5-beta-hydroxyethylthiazole kinase
-
-
-
-
4-methyl-5-hydroxyethylthiazole kinase
hydroxyethylthiazole kinase/thiamine-phosphate pyrophosphorylase
-
bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity
kinase, hydroxyethylthiazole (phosphorylating)
-
-
-
-
SaThiM
TH kinase
-
-
-
-
thiazole kinase
ThiK
ThiM
THZ kinase
additional information
-
the enzyme belongs to the family of ribokinase-like carbohydrate kinases
ThiK
-
-
-
-
THZ kinase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
-
-
-
-
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
catalytic mechanism of phosphoryl transfer reaction and role of active site residues, e.g. R121 and C198, calculated on the basis of data on crystal structures of ribokinase-like kinases, transition state stabilization involves an oxyanion hole and a magnesium ion
-
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
SN2-like mechanism, with gamma-phosphate acting as an alcohol-activation base. Mg2+ ion 2, residues E126 and C198 play a major catalytic role, whereas Mg2+ ion 1 and C198 are responsible for product release
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:4-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9026-56-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + 4-methyl-5-(2-hydroxyethyl)thiazole
AMP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
3.4% of the activity with ATP
-
-
?
ATP + 1,3,5-trimethyl-4-(2-hydroxyethyl)pyrazole
ADP + 2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethyl phosphate
ATP + 2-methyl-3-(2-hydroxyethyl)imidazole
ADP + 2-(2-methyl-1H-imidazol-1-yl)ethyl phosphate
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphoethyl)thiazole
-
-
-
-
?
ATP + 5-(2-hydroxyethyl)-4-methylthiazole
ADP + 4-methyl-5-(2-phosphoethyl)-thiazole
-
-
-
-
?
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole
dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
dCTP + 4-methyl-5-(2-hydroxyethyl)thiazole
dCDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
dGTP + 4-methyl-5-(2-hydroxyethyl)thiazole
dGDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
dUTP + 4-methyl-5-(2-hydroxyethyl)thiazole
dUDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
TTP + 4-methyl-5-(2-hydroxyethyl)thiazole
TDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 1,3,5-trimethyl-4-(2-hydroxyethyl)pyrazole
ADP + 2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethyl phosphate
cpd1
-
-
ir
ATP + 1,3,5-trimethyl-4-(2-hydroxyethyl)pyrazole
ADP + 2-(1,3,5-trimethyl-1H-pyrazol-4-yl)ethyl phosphate
cpd1
-
-
ir
ATP + 2-methyl-3-(2-hydroxyethyl)imidazole
ADP + 2-(2-methyl-1H-imidazol-1-yl)ethyl phosphate
cpd2
-
-
ir
ATP + 2-methyl-3-(2-hydroxyethyl)imidazole
ADP + 2-(2-methyl-1H-imidazol-1-yl)ethyl phosphate
cpd2
-
-
ir
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
phosphate transfer occurs by an inline mechanism
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
the bifunctioinal enzyme hydroxyethylthiazole kinase/thiamine-phosphate pyrophosphorylase catalyzes two sequential steps in the synthesis of thiamin monophosphate from hydroxyethylthiazole
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
enzyme involved in biosynthesis of thiamine
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
-
-
-
?
CTP + 4-methyl-5-(2-hydroxyethyl)thiazole
CDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
CTP + 4-methyl-5-(2-hydroxyethyl)thiazole
CDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
13.7% of the activity with ATP
-
-
?
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole
dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
the enzyme shows a preference for dATP as a phosphate donor over ATP
-
-
?
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole
dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
24.8% of the activity with ATP
-
-
?
GTP + 4-methyl-5-(2-hydroxyethyl)thiazole
GDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
GTP + 4-methyl-5-(2-hydroxyethyl)thiazole
GDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
3.2% of the activity with ATP
-
-
?
UTP + 4-methyl-5-(2-hydroxyethyl)thiazole
UDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
UTP + 4-methyl-5-(2-hydroxyethyl)thiazole
UDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
75.1% of the activity with ATP
-
-
?
additional information
?
-
-
ATP-dependent phosphorylation of small molecules containing hydroxymethyl groups, reaction pathway mapping, molecular mechanism optimization and quantum mechanis calculations on the basis of enzyme crystal structure, PDB code 1C3Q and 1ESQ, overview
-
-
?
additional information
?
-
-
the active site is located at the interface between adjacent subunits. Each active site contains a thiazole-binding site and a nucleotide-binding site, structure, overview. Asp residue as a catalytic base
-
-
?
additional information
?
-
-
the active site is located at the interface between adjacent subunits. Each active site contains a thiazole-binding site and a nucleotide-binding site, structure, overview. Asp residue as a catalytic base
-
-
?
additional information
?
-
enzyme-substrate binding structure analysis, overview
-
-
-
additional information
?
-
-
enzyme-substrate binding structure analysis, overview
-
-
-
additional information
?
-
enzyme-substrate binding structure analysis, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
the bifunctioinal enzyme hydroxyethylthiazole kinase/thiamine-phosphate pyrophosphorylase catalyzes two sequential steps in the synthesis of thiamin monophosphate from hydroxyethylthiazole
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
enzyme involved in biosynthesis of thiamine
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
-
-
-
?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mg2+
amino-acid residues in the magnesium ion-binding site are conserved
Mg2+
4-methyl-5-(2-hydroxyethyl)thiazole (THZ) forms six direct H-bonds to residues M39, P37, G61, T186 and C190. For the ThiM-THZ complex four Mg2+ ions, essential for the phosphor transfer reaction, are located within four active sites of the two trimers in the asymmetric unit. The Mg2+ ions are coordinated by residues D88, K115 and E120 and one solvent water molecule. No Mg2+ ion is found in the native structure
Mg2+
required, two ions per enzyme molecule, binding structure involving C467, D340, and E372, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PCMB
-
0.01 mM, 98.5% inhibition, inhibition prevented by addition of 2-mercaptoethanol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Malaria
Isolation, characterization, interaction of a thiazolekinase (Plasmodium falciparum) with silver nanoparticles.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
modeling of stationary points along the reaction pathway, determination of relative energies of the transition state and product
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.9
with UTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
1.1
with CTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
1.4
with ATP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
11
14
15
with dCTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
24
with GTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
3.2
with GTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
3.9
with dCTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
37
with dATP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
4
with dUTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
4.3
with UTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
4.88
substrate 4-methyl-5-(2-hydroxyethyl)thiazole, pH 7.5, 37°C
45
with TTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
5.2
with CTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
7.3
substrate 1,3,5-trimethyl-4-(2-hydroxyethyl)pyrazole, pH 7.5, 37°C
7.42
substrate 2-methyl-3-(2-hydroxyethyl)imidazole, pH 7.5, 37°C
8.9
with TTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
9.2
with dATP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
11
with ATP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
11
with dGTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
14
with dGTP as phosphate donor, in the presence of Mg2+, at pH 10.0 and 50°C
14
with dUTP as phosphate donor, in the presence of Co2+, at pH 10.0 and 50°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 9.2
-
pH 7.4: about 80% of activity maximum, pH 9.2: about 25% of activity maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity
-
-
brenda
mutant resistant to 2-amino-4-methyl-5-beta-hydroxyethylthiazole, an antimetabolite of 4-methyl-5-beta-hydroxyethylthiazole, deficient in activity of both EC 2.5.1.3 and EC 2.7.1.50
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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
-
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
-
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)
-
malfunction
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
-
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
-
metabolism
THI6 is a bifunctional enzyme of the thiamin biosynthetic pathway
metabolism
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway
metabolism
-
enzyme ThiM is involved in the vitamin B1 (thiamin) biosynthetic pathway
-
physiological function
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
-
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
-
additional information
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (14495 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28100