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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
thiamin pyrophosphokinase, thiamine monophosphate kinase, thiamin phosphate kinase, thiamin-monophosphate kinase, thiamine-phosphate kinase, thiamin monophosphate kinase,
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ATP:thiamin-phosphate phosphotransferase
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kinase, thiamin monophosphate (phosphorylating)
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thiamin monophosphatase
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thiamin monophosphate kinase
thiamin monophosphokinase
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thiamin pyrophosphokinase
thiamin-monophosphate kinase
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thiamin-phosphate kinase
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thiamine monophosphate kinase
thiamine monophosphokinase
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additional information
ThiL is a member of a small ATP binding superfamily
thiamin monophosphate kinase
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thiamin monophosphate kinase
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thiamin monophosphate kinase
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thiamin phosphate kinase
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thiamin phosphate kinase
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thiamin phosphate kinase
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thiamin phosphate kinase
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thiamin pyrophosphokinase
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thiamin pyrophosphokinase
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thiamine monophosphate kinase
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thiamine monophosphate kinase
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thiamine monophosphate kinase
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thiamine monophosphate kinase
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ThiL
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TP kinase
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ATP + thiamine phosphate = ADP + thiamine diphosphate
ATP + thiamine phosphate = ADP + thiamine diphosphate
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ATP + thiamine phosphate = ADP + thiamine diphosphate
Aquifex aeolicus ThiL utilizes a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate, reaction mechanism, overview
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phospho group transfer
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ATP:thiamine-phosphate phosphotransferase
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ADP + thiamine phosphate
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poor substrate
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?
ATP + oxythiamine monophosphate
ADP + ?
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
ITP + thiamine phosphate
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poor substrate
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?
additional information
?
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oxythiamine, pyrithiamine, and amprolium, are not phosphorylated
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ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
ThiL catalyzes the ATP-dependent phosphorylation of thiamin monophosphate to form thiamin diphosphate, the active form of vitamin B1
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
substrate and product binding site structures, conformational changes in ThiL upon substrate binding, overview
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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no substrates: thiamine, GTP, CTP, UTP, AMP
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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enzyme is involved in thiamin diphosphate biosynthesis
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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random bi-bi mechanism. Thiamine diphosphate is not further phosphorylated by ThiL
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ATP + thiamine phosphate
ADP + thiamine diphosphate
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ATP + thiamine phosphate
ADP + thiamine diphosphate
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ATP + thiamine phosphate
ADP + thiamine diphosphate
no substrates: thiamine, GTP, CTP, UTP, AMP
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
enzyme plays an important role in the thiamine diphosphate biosynthetic pathway, thiamine diphosphate is the regulatory molecule for thiamine synthesis and predicts the existence of a sensor/regulatory protein
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?
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ATP + thiamine phosphate
ADP + thiamine diphosphate
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
ThiL catalyzes the ATP-dependent phosphorylation of thiamin monophosphate to form thiamin diphosphate, the active form of vitamin B1
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ATP + thiamine phosphate
ADP + thiamine diphosphate
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ATP + thiamine phosphate
ADP + thiamine diphosphate
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enzyme is involved in thiamin diphosphate biosynthesis
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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?
ATP + thiamine phosphate
ADP + thiamine diphosphate
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ATP + thiamine phosphate
ADP + thiamine diphosphate
enzyme plays an important role in the thiamine diphosphate biosynthetic pathway, thiamine diphosphate is the regulatory molecule for thiamine synthesis and predicts the existence of a sensor/regulatory protein
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?
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ATP
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Co2+
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requirement, about 95% as effective as Mg2+
Fe2+
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activation, about 10% as effective as Mg2+
Mn2+
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activation, about 30% as effective as Mg2+
Zn2+
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activation, about 30% as effective as Mg2+
Mg2+
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additional information
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no activation by Ba2+, Ca2+, Cu2+, Cs+, Li+, Na+
additional information
no effects of K+ on the enzyme at 0.1-0.5 M
additional information
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no effects of K+ on the enzyme at 0.1-0.5 M
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5-hydroxyindolacetic acid
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uncompetitive inhibitor
Cs+
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antagonizes stimulation by K+
Li+
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antagonizes stimulation by K+
Na+
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antagonizes stimulation by K+
PCMB
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2-mercaptoethanol reverses
Pyrithiamine phosphate
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WAY213613
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noncompetitive inhibitor
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additional information
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no inhibition by phosphate, KCN, iodoacetic acid, arsenate or arsenite
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AMP
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AMP
the mode of AMP inhibition is uncompetitive for both thiamine phosphate and ATP
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Avitaminosis
[Enzyme activity of thiamine diphosphate biosynthesis and degradation in the mouse liver in the dynamics of B1 avitaminosis development]
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0.152
oxythiamine monophosphate
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pH 8.0, temperature not specified in the publication
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0.000043 - 0.008
thiamine phosphate
0.00013
ATP
pH 7.0, 100°C, recombinant His-tagged mutant S196A
0.039
ATP
pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
0.111
ATP
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pH 8.0, temperature not specified in the publication
0.28
ATP
pH 7.0, 100°C, recombinant His-tagged mutant R136M
0.000043
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant S196A
0.0002
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
0.0011
thiamine phosphate
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pH 7.5, 37°C
0.0013
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant R136M
0.008
thiamine phosphate
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pH 8.0, temperature not specified in the publication
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0.006 - 0.092
thiamine phosphate
0.006
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant S196A
0.063
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
0.092
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant R136M
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68 - 320
thiamine phosphate
0.33
ATP
pH 7.0, 100°C, recombinant His-tagged mutant R136M
1.6
ATP
pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
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ATP
pH 7.0, 100°C, recombinant His-tagged mutant S196A
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thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant R136M
140
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged mutant S196A
320
thiamine phosphate
pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
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0.114
5-hydroxyindolacetic acid
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pH 8.0, temperature not specified in the publication
0.36
pyrithiamine
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pH 7.5, 37°C
0.0134
WAY213613
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pH 8.0, temperature not specified in the publication
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0.53
AMP
with ATP, pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
0.56
AMP
with thiamine phosphate, pH 7.0, 100°C, recombinant His-tagged wild-type enzyme
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80 - 120
10% of maximal activity at 80°C, 50% at 100°C, maximal activity at 120°C, inactive on ice
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UniProt
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UniProt
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Uniprot
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gene Pcal_0657 or THI80
UniProt
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gene Pcal_0657 or THI80
UniProt
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LT2
SwissProt
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K12
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drug target
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the enzyme represents a potential drug target for the development of an augmented repertoire of antibiotics against Pseudomonas aeruginosa
metabolism
biosynthesis pathways of thiamine, thiamine phosphate, and thiamine diphosphate, overview
metabolism
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biosynthesis pathways of thiamine, thiamine phosphate, and thiamine diphosphate, overview
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physiological function
in this archaeon, the phosphorylation of thiamine phosphate is the only way to synthesize thiamine diphosphate, it cannot use exogenous thiamine and direct diphosphorylation for the salvage synthesis of thiamine diphosphate
physiological function
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in this archaeon, the phosphorylation of thiamine phosphate is the only way to synthesize thiamine diphosphate, it cannot use exogenous thiamine and direct diphosphorylation for the salvage synthesis of thiamine diphosphate
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additional information
residue Ser196 plays a pivotal role in the catalytic process
additional information
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residue Ser196 plays a pivotal role in the catalytic process
additional information
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residue Ser196 plays a pivotal role in the catalytic process
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35000
recombinant enzyme, amino acid sequence
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monomer
1 * 35000, SDS-PAGE
dimer
SDS-PAGE and gel filtration, neither R136 nor S196 are important for enzyme dimerization
dimer
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SDS-PAGE and gel filtration, neither R136 nor S196 are important for enzyme dimerization
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sitting drop method, crystal structures of thiamine monophosphate kinase in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate
purified recombinant enzyme in complex with nonhydrolyzable AMP-PCP and TMP, or with the reaction products ADP and TPP, ThiL is incubated with 4 mM AMP-PCP or ATP and 4 mM MgCl2 on ice for 1 h prior to crystallization experiments, optimized conditions for the ThiL binary complexes include 100 mM HEPES, pH 7.4, 6-11% isopropyl alcohol, 200 mM NaCl, and 4-6% 2-methyl-2,4-pentanediol, 100 mM CaCl2 is used as an additive in a 1:9 ratio with the reservoir solution, TMP is soaked into the co-crystallized ThiL and AMP-PCP crystals by transferring the crystals to a solution containing the mother liquor and 20 mM TMP and allowing the crystals to soak for 5 min before being frozen. To obtain ThiL ADP-TPP crystals, ThiL is incubated on ice with 4 mM ADP, 4 mM TPP, and 4 mM MgCl2, optimized conditions for the product complex include 100 mM imidazole, pH 8.0, 7-10% PEG 8000, and 100-250 mM Ca(C2H3O2)2, 3-7 days, cryoprotection by 15% ethylene glycol, X-ray diffraction structure determination and analysis at 1.5-2.6 A resolution
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R136M
site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type
S196A
site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type
R136M
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site-directed mutagenesis, the mutant shows 80% reduced activity compared to the wild-type
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S196A
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site-directed mutagenesis, the mutant shows 90% reduced activity compared to the wild-type
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100
purified recombinant ThiL protein, loss of about 45% activity after 15 min at 100°C and 20% after 60 min, ATP can partially stabilize the activity, addition of 0.5 M NaCl or 0.5 M KCl to the enzyme solution does not improve the thermostability
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ATP stabilizes the enzyme
glycerol stabilizes during purification
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-20°C, 3 days, t1/2: 10 days
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by metal affinity chromatography and ultrafiltration
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construction of the thiamine monophosphate kinase (thiL) overexpression plasmid, overexpression from pCLK710
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encoded by thiL, thiL is not transcriptionally regulated by thiamine or thiamine diphosphate
expression in Escherichia coli
expression in Escherichia coli BL21
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expression in Escherichia coli Rosetta BL21(DE3)R3
gene THI80 or Pcal_0657, sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
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Nishino, H.
Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase
J. Biochem.
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1093-1100
1972
Escherichia coli
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Webb, E.; Downs, D.
Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium
J. Biol. Chem.
272
15702-15707
1997
Salmonella enterica subsp. enterica serovar Typhimurium (P55881), Salmonella enterica subsp. enterica serovar Typhimurium
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Melnick, J.S.; Sprinz, K.I.; Reddick, J.J.; Kinsland, C.; Begley, T.P.
An efficient enzymatic synthesis of thiamin pyrophosphate
Bioorg. Med. Chem. Lett.
13
4139-4141
2003
Escherichia coli
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McCulloch, K.M.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
Structural studies of thiamin monophosphate kinase in complex with substrates and products
Biochemistry
47
3810-3821
2008
Aquifex aeolicus (O67883), Aquifex aeolicus
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Hayashi, M.; Nosaka, K.
Characterization of thiamin phosphate kinase in the hyperthermophilic archaeon Pyrobaculum calidifontis
J. Nutr. Sci. Vitaminol.
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369-374
2015
Pyrobaculum calidifontis (A3MTW6), Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548 (A3MTW6)
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Kim, H.J.; Lee, H.; Lee, Y.; Choi, I.; Ko, Y.; Lee, S.; Jang, S.
The ThiL enzyme is a valid antibacterial target essential for both thiamine biosynthesis and salvage pathways in Pseudomonas aeruginosa
J. Biol. Chem.
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10081-10091
2020
Pseudomonas aeruginosa
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Sullivan, A.H.; Dranow, D.M.; Horanyi, P.S.; Lorimer, D.D.; Edwards, T.E.; Abendroth, J.
Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products
Sci. Rep.
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4392
2019
Acinetobacter baumannii (A0A0D5YC82), Acinetobacter baumannii, Acinetobacter baumannii AB5075-UW (A0A0D5YC82)
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Transporter Classification Database (TCDB):
8.A.159.1.2
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