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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 + 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 + 5-(2-hydroxyethyl)-4-methylthiazole
ADP + 4-methyl-5-(2-phosphoethyl)-thiazole
-
-
-
-
?
CTP + 4-methyl-5-(2-hydroxyethyl)thiazole
CDP + 4-methyl-5-(2-phosphonooxyethyl)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
-
-
-
?
GTP + 4-methyl-5-(2-hydroxyethyl)thiazole
GDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
TTP + 4-methyl-5-(2-hydroxyethyl)thiazole
TDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
-
-
?
UTP + 4-methyl-5-(2-hydroxyethyl)thiazole
UDP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
additional information
?
-
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
-
-
-
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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-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
-
-
-
?
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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
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
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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
-
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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
octamer
-
8 * 60000, bifunctional enzyme with hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase activity, SDS-PAGE
?
x * 28000, SDS-PAGE
?
x * 28100, calculated from amino acid sequence
homotrimer
3 * 28950 Da, crystal structure, calculated
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
-
trimer
-
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
-
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
-
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
-
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crystallization by vapor diffusion equilibration, crystal structure at 1.5 A resolution
enzyme with a phosphate ion occupying the position of the beta-phosphate of the nucleotide, mixing of 0.001 ml of protein solution containing 1.95 mg/ml protein in 20 mM Tris-HCl containing 200 mM NaCl and 1 mM DTT, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M CHESS buffer, pH 9.3, and 0.88 M sodium citrate as the precipitant, 20°C, 1 week, 25% v/v glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 1.85 A resolution
-
precipitant: sodium citrate, pH 9.3, 293 K
purified enzyme SaThiM in apoform and in complexes with the natural substrate 5-(hydroxyethyl)-4-methylthiazole (THZ) and two selected substrate analogues, cpd1 and cpd2, sitting drop vapor diffusion method using 10-20 mg/ml protein in 100 mM Tris, and 150 mM NaCl, pH 8.0, with an equal volume of 0.5 M magnesium formate, microcrystal seeding, with precipitant solution containing 18, 20 or 22% PEG 3350 w/v, 0.2 M magnesium formate, and 5% isopropanol (v/v), against a 0.5 ml reservoir of precipitant, X-ray diffraction structure determination and analysis at 1.62-2.09 A resolution. The homologue structure of Bacillus subtilis ThiK (PDB ID 1C3Q), sharing 38% sequence identity, is used as a search model for molecular replacement phasing
purified recombinant detagged enzyme, in complex with beta,gamma-methyleneadenosine 5'-diphosphate, thiamin phosphate, 4-amino-5-hydroxymethyl-2-trifluoromethylpyrimidine diphosphate, or 4-methyl-5-hydroxyethylthiazole phosphate, hanging-drop vapor diffusion method, mixing of0.001 ml protein solution with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 0.2-0.25 M MgCl2, and 25-32% PEG400, 22°C, 2-3 days, method optimization, X-ray diffraction structure determination and analysis at 2.6-3.3 A resolution, modeling
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Camiener, G.W.; Brown, G.M.
The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates
J. Biol. Chem.
235
2411-2417
1960
Saccharomyces cerevisiae
brenda
Kawasaki, Y.
Copurification of hydroxyethylthiazole kinase and thiamine-phosphate pyrophosphorylase of Saccharomyces cerevisiae: characterization of hydroxyethylthiazole kinase as a bifunctional enzyme in the thiamine biosynthetic pathway
J. Bacteriol.
175
5153-5158
1993
Saccharomyces cerevisiae
brenda
Campobasso, N.; Mathews, II; Begley, T.P.; Ealick, S.E.
Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution
Biochemistry
39
7868-7877
2000
Bacillus subtilis (P39593), Bacillus subtilis
brenda
Dyguda, E.; Szefczyk, B.; Sokalski, W.A.
The mechanism of phosphoryl transfer reaction and the role of active site residues on the basis of ribokinase-like kinases
Int. J. Mol. Sci.
5
141-153
2004
Bacillus subtilis
-
brenda
Karunakaran, R.; Ebert, K.; Harvey, S.; Leonard, M.E.; Ramachandran, V.; Poole, P.S.
Thiamine is synthesized by a salvage pathway in Rhizobium leguminosarum bv. viciae strain 3841
J. Bacteriol.
188
6661-6668
2006
Rhizobium leguminosarum
brenda
Dyguda-Kazimierowicz, E.; Sokalski, W.A.; Leszczynski, J.
Non-empirical study of the phosphorylation reaction catalyzed by 4-methyl-5-beta-hydroxyethylthiazole kinase: relevance of the theory of intermolecular interactions
J. Mol. Model.
13
839-849
2007
Bacillus subtilis (P39593)
brenda
Jeyakanthan, J.; Thamotharan, S.; Velmurugan, D.; Rao, V.S.; Nagarajan, S.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.
New structural insights and molecular-modelling studies of 4-methyl-5-beta-hydroxyethylthiazole kinase from Pyrococcus horikoshii OT3 (PhThiK)
Acta Crystallogr. Sect. F
65
978-986
2009
Pyrococcus horikoshii OT3 (O58877), Pyrococcus horikoshii OT3
brenda
Drebes, J.; Perbandt, M.; Wrenger, C.; Betzel, C.
Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus
Acta Crystallogr. Sect. F
67
479-481
2011
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Paul, D.; Chatterjee, A.; Begley, T.P.; Ealick, S.E.
Domain organization in Candida glabrata THI6, a bifunctional enzyme required for thiamin biosynthesis in eukaryotes
Biochemistry
49
9922-9934
2010
[Candida] glabrata (Q6FV03), [Candida] glabrata
brenda
Tani, Y.; Kimura, K.; Mihara, H.
Purification and properties of 4-methyl-5-hydroxyethylthiazole kinase from Escherichia coli
Biosci. Biotechnol. Biochem.
80
514-517
2016
Escherichia coli (P76423), Escherichia coli
brenda
Yazdani, M.; Zallot, R.; Tunc-Ozdemir, M.; de Crecy-Lagard, V.; Shintani, D.K.; Hanson, A.D.
Identification of the thiamin salvage enzyme thiazole kinase in Arabidopsis and maize
Phytochemistry
94
68-73
2013
Zea mays (K7VCB9), Zea mays, Arabidopsis thaliana (Q9LIQ4)
brenda
Drebes, J.; Kuenz, M.; Windshuegel, B.; Kikhney, A.G.; Mueller, I.B.; Eberle, R.J.; Oberthuer, D.; Cang, H.; Svergun, D.I.; Perbandt, M.; Betzel, C.; Wrenger, C.
Structure of ThiM from vitamin B1 biosynthetic pathway of Staphylococcus aureus - insights into a novel pro-drug approach addressing MRSA infections
Sci. Rep.
6
22871
2016
Staphylococcus aureus (Q6GEY3), Staphylococcus aureus, Staphylococcus aureus MRSA252 (Q6GEY3)
brenda