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ATP + 4'-deoxypyridoxine
ADP + 4'-deoxypyridoxine 5'-phosphate
-
-
-
?
ATP + 4'-O-methylpyridoxine
ADP + 4'-O-methylpyridoxine 5'-phosphate
-
-
-
?
ATP + ginkgotoxin
ADP + ginkgotoxin 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
additional information
?
-
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
no substrate: GTP
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
additional information
?
-
no activity with GTP
-
-
?
additional information
?
-
-
no activity with GTP
-
-
?
additional information
?
-
pyridoxal kinase catalyzes the forward reactions with pyridoxal, pyridoxamine, and pyridoxine, while pyridoxal phosphotase (PL phosphatase, PDXP, EC 3.1.3.74) catalyzes the reverse reaction of dephophorylation
-
-
-
additional information
?
-
-
pyridoxal kinase catalyzes the forward reactions with pyridoxal, pyridoxamine, and pyridoxine, while pyridoxal phosphotase (PL phosphatase, PDXP, EC 3.1.3.74) catalyzes the reverse reaction of dephophorylation
-
-
-
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Zn2+
in complex with ATP preferred substrate in vitro
Ca2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Fe2+
-
cations activate in decreaseing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Li+
-
poor activator which seems to modify the enzymatic mechanism from a random to an ordered sequential pattern with ATP bound before pyridoxal. Km: 37 mM
K+
affinity to pyridoxal and ATP is increased manifold in the presence of K+ compared to Na+, 2.5fold increase of activity
K+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
Mg2+
required
Mg2+
in complex with ATP most likely preferred substrate in vivo
Mg2+
acts in complex with ATP
Na+
6fold increase of activity
Na+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
Co2+
-
-
Co2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Cu2+
-
-
Cu2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
K+
-
-
K+
-
most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM
K+
-
most effective activator of the monovalent cations
Mg2+
-
-
Mg2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mg2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mg2+
-
enzyme requires a divalent cation, optimal concentration is 0.416 mM
Mn2+
-
-
Mn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Na+
-
activates
Na+
-
increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal
Ni2+
-
-
Ni2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
-
-
Zn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+. Optimum at about 0.1 mM Zn2+
Zn2+
-
divalent cation required, optimal concentration is 0.33 mM. Zn2+ is superior to Mg2+ below the optimum concentration of Zn2+
Zn2+
-
activator at low concentrations (0.019 mM optimal concentration), most effective divalent cation for catalysis
additional information
Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
-
Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
no singnificant activity with Li+, Cs+, Rb+
additional information
-
no singnificant activity with Li+, Cs+, Rb+
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4'-O-methylpyridoxine
i.e. ginkgotoxin. Treatment leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
Caffeine
21% inhibition at 0.1 mM
enprofylline
33% inhibition at 0.1 mM
lamotrigine
45% inhibition at 0.1 mM
Theobromine
22% inhibition at 0.1 mM
theophylline
60% inhibition at 0.1 mM
cycloserine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 42% inhibition
D-penicillamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 20% inhibition
dopamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% inhibition
gamma-aminobutyric acid
-
-
isoniazid
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 81% inhibition
levodopa
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 16% inhibition
muzolimine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 27% inhibition
N-Dansyl-1,8-diaminooctane
-
-
primaquine
-
competitive inhibition, complete inhibition at 0.75 mM
progabide
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate
theophylline
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate, 86% inhibition of reaction with pyridoxal, 88% inhibition of reaction with pyridoxamine
Thiamphenicol
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 31% inhibition
ZnATP2-
-
weak substrate inhibition
ginkgotoxin
-
ginkgotoxin
i.e. 4'-O-methylpyridoxine, complete inhibition at 0.1 mM
pyridoxal
-
-
pyridoxal
-
substrate inhibition
pyridoxal
-
effective competitive inhibitor
pyridoxamine
-
-
pyridoxamine
-
effective competitive inhibitor
Zn2+
-
-
Zn2+
-
slight inhibition above the optimum of 0.33 mM
additional information
-
ATP4- and HATP3- do not affect the enzyme activity. Free Mg2+ does not inhibit enzyme activity
-
additional information
-
not inhibited by chloroquine
-
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Anemia, Sideroblastic
Erythrocyte pyridoxine kinase levels in patients with sideroblastic anemia.
Anemia, Sideroblastic
Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients.
Brain Diseases
Biomedical aspects of pyridoxal 5'-phosphate availability.
Carcinoma
Effects of vitamin B6 metabolism on oncogenesis, tumor progression and therapeutic responses.
Carcinoma
Nephrotoxicity Profile of Cadmium Revealed by Proteomics in Mouse Kidney.
Carcinoma
[Pyridoxal kinase activity in human tumor tissues]
Carcinoma, Hepatocellular
Vitamin B6 metabolism in liver and liver-derived tumors.
Carcinoma, Non-Small-Cell Lung
Effects of vitamin B6 metabolism on oncogenesis, tumor progression and therapeutic responses.
Carcinoma, Non-Small-Cell Lung
Negative prognostic value of high levels of intracellular poly(ADP-ribose) in non-small cell lung cancer.
Down Syndrome
Expression of cystathionine beta-synthase, pyridoxal kinase, and ES1 protein homolog (mitochondrial precursor) in fetal Down syndrome brain.
Down Syndrome
Increased activity of pyridoxal kinase in tongue in Down's syndrome.
Epilepsy
Inborn errors in the vitamin B6 salvage enzymes associated with neonatal epileptic encephalopathy and other pathologies.
Epilepsy
[Distribution and activity of pyridoxal kinase in human brain during ontogenesis]
Leishmaniasis, Visceral
Evaluation of Leishmania infantum pyridoxal kinase protein for the diagnosis of human and canine visceral leishmaniasis.
Leishmaniasis, Visceral
Leishmania infantum pyridoxal kinase evaluated in a recombinant protein and DNA vaccine to protects against visceral leishmaniasis.
Leukemia, Myeloid, Acute
Vitamin B6 Fuels Acute Myeloid Leukemia Growth.
Lung Neoplasms
Negative prognostic value of high levels of intracellular poly(ADP-ribose) in non-small cell lung cancer.
Lymphopenia
Inhibition of human pyridoxal kinase by 2-acetyl-4-((1R,2S,3R)-1,2,3,4-tetrahydroxybutyl)imidazole (THI).
Malaria
The antimalarial drugs chloroquine and primaquine inhibit pyridoxal kinase, an essential enzyme for vitamin B6 production.
Neoplasms
Pyridoxal kinase and poly(ADP-ribose) affect the immune microenvironment of locally advanced cancers.
Neoplasms
Vitamin B6 metabolism in Morris hepatomas.
Neoplasms
[Pyridoxal kinase activity in human tumor tissues]
Nervous System Diseases
Biomedical aspects of pyridoxal 5'-phosphate availability.
Ovarian Neoplasms
[Pyridoxal kinase (PDXK) promotes the proliferation of serous ovarian cancer cells and is associated with poor prognosis].
Parkinson Disease
A loss of Pdxk model of Parkinson disease in Drosophila can be suppressed by Buffy.
Parkinson Disease
Association of pyridoxal kinase and Parkinson disease.
Parkinson Disease
Single-cell expression profiling of dopaminergic neurons combined with association analysis identifies pyridoxal kinase as Parkinson's disease gene.
pyridoxal kinase deficiency
Apparent pyridoxine transport mutants of Escherichia coli with pyridoxal kinase deficiency.
Seizures
Biomedical aspects of pyridoxal 5'-phosphate availability.
Seizures
Changes in pyridoxal kinase immunoreactivity in the gerbil hippocampus following spontaneous seizure.
Seizures
Correlative changes of pyridoxal kinase pyridoxal-5'-phosphate and glutamate decarboxylase in brain, during drug-induced convulsions.
Seizures
Inborn errors in the vitamin B6 salvage enzymes associated with neonatal epileptic encephalopathy and other pathologies.
Seizures
Seizure susceptibility in the developing mouse and its relationship to glutamate decarboxylase and pyridoxal phosphate in brain.
Seizures
The status of vitamin B6 metabolism in brains of genetically epilepsy-prone rats.
Seizures
Vigabatrin inhibits pyridoxine-5'-phosphate oxidase, not pyridoxal kinase in the hippocampus of seizure prone gerbils.
Stomach Neoplasms
The differential proteome profile of stomach cancer: identification of the biomarker candidates.
Vitamin B 6 Deficiency
Evidence of a theophylline-induced vitamin B6 deficiency caused by noncompetitive inhibition of pyridoxal kinase.
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0.0216
4'-deoxypyridoxine
0.00495
4'-O-methylpyridoxine
pH 6.2, 37°C
0.00495
ginkgotoxin
in 70 mM potassium phosphate buffer, pH 6.2
0.035 - 0.126
pyridoxamine
0.00987 - 0.02
pyridoxine
0.00172 - 0.016
pyridoxine
0.0216
4'-deoxypyridoxine
pH 6.2, 37°C
0.0216
4'-deoxypyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
0.025
ATP
in the presence of K+, and in complex with Mg2+
0.025
ATP
presence of 40 mM Na+, pH 7.3, 37°C
0.17
ATP
D235A mutant protein
0.17
ATP
ATP in form of MgATP
0.18
ATP
D235N mutant protein
0.18
ATP
ATP in form of MgATP
0.19
ATP
wild-type protein
0.19
ATP
ATP in form of MgATP
0.377
ATP
pH 7.3, 37°C recombinant mutant D87H
0.407
ATP
pH 7.3, 37°C recombinant wild-type enzyme
0.42
ATP
with pyridoxal as substrate, pH 7.3, 37°C
0.42
ATP
ATP in form of MgATP
0.5
ATP
in the presence of Na+, and in complex with Mg2+
0.5
ATP
presence of 40 mM Na+, pH 7.3, 37°C
0.901
ATP
pH 7.3, 37°C recombinant mutant H246Q
1.024
ATP
pH 7.3, 37°C recombinant mutant A243G
3.096
ATP
pH 7.3, 37°C recombinant mutant V128I
0.0028
pyridoxal
in 70 mM potassium phosphate buffer, pH 6.2
0.01
pyridoxal
in the presence of K+
0.01
pyridoxal
presence of 40 mM Na+, pH 7.3, 37°C
0.024
pyridoxal
wild-type protein
0.03
pyridoxal
with MgATP2- as substrate, pH 7.3, 37°C
0.058
pyridoxal
D235N mutant protein
0.0587
pyridoxal
pH 6.2, 37°C
0.075
pyridoxal
in the presence of Na+
0.075
pyridoxal
presence of 40 mM Na+, pH 7.3, 37°C
0.141
pyridoxal
pH 7.3, 37°C recombinant mutant H246Q
0.17
pyridoxal
D235A mutant protein
0.177
pyridoxal
pH 7.3, 37°C recombinant mutant A243G
0.189
pyridoxal
pH 7.3, 37°C recombinant wild-type enzyme
0.35
pyridoxal
with ZnATP2- as substrate, pH 7.3, 37°C
2.09
pyridoxal
pH 7.3, 37°C recombinant mutant D87H
3.839
pyridoxal
pH 7.3, 37°C recombinant mutant V128I
0.035
pyridoxamine
with MgATP2- as substrate, pH 7.3, 37°C
0.126
pyridoxamine
pH 6.2, 37°C
0.126
pyridoxamine
in 70 mM potassium phosphate buffer, pH 6.2
0.00987
pyridoxine
pH 6.2, 37°C
0.00987
pyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
0.015
pyridoxine
with ZnATP2- as substrate, pH 7.3, 37°C
0.02
pyridoxine
with MgATP2- as substrate, pH 7.3, 37°C
0.012
ATP
-
pH 7, 37°C
0.02
ATP
-
in the presence of Zn2+, at pH 6.5 and 37°C
0.00122
pyridoxal
-
in the presence of K+, at pH 7.0 and 30°C
0.0739
pyridoxal
-
in the presence of Na+, at pH 7.0 and 30°C
0.097
pyridoxal
-
pH 7, 37°C
0.49
pyridoxal
-
at pH 6.5 and 37°C
0.00172
pyridoxine
-
pH 7.0, 37°C
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1.535 - 2.94
4'-deoxypyridoxine
0.46
4'-O-methylpyridoxine
pH 6.2, 37°C
0.46
ginkgotoxin
in 70 mM potassium phosphate buffer, pH 6.2
1.9
ATP
-
in the presence of Zn2+, at pH 6.5 and 37°C
1.535
4'-deoxypyridoxine
pH 6.2, 37°C
2.94
4'-deoxypyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
0.47
ATP
pH 7.3, 37°C recombinant mutant A243G
0.58
ATP
pH 7.3, 37°C recombinant mutant H246Q
0.67
ATP
pH 7.3, 37°C recombinant mutant D87H
0.97
ATP
pH 7.3, 37°C recombinant wild-type enzyme
1.12
ATP
pH 7.3, 37°C recombinant mutant V128I
0.03
pyridoxal
D235A mutant protein
0.23
pyridoxal
D235N mutant protein
0.47
pyridoxal
pH 7.3, 37°C recombinant mutant A243G
0.48
pyridoxal
wild-type protein
0.5
pyridoxal
with ZnATP2- as substrate, pH 7.3, 37°C
0.58
pyridoxal
pH 7.3, 37°C recombinant mutant H246Q
0.67
pyridoxal
pH 7.3, 37°C recombinant mutant D87H
0.8
pyridoxal
with MgATP2- as substrate, pH 7.3, 37°C
0.97
pyridoxal
pH 7.3, 37°C recombinant wild-type enzyme
0.995
pyridoxal
pH 6.2, 37°C
1.12
pyridoxal
pH 7.3, 37°C recombinant mutant V128I
1.42
pyridoxal
presence of 40 mM K+, pH 7.3, 37°C
3.3
pyridoxal
presence of 40 mM Na+, pH 7.3, 37°C
6.08
pyridoxal
in 70 mM potassium phosphate buffer, pH 6.2
0.3
pyridoxamine
with MgATP2- as substrate, pH 7.3, 37°C
0.79
pyridoxamine
in 70 mM potassium phosphate buffer, pH 6.2
0.79
pyridoxamine
pH 6.2, 37°C
0.1
pyridoxine
with ZnATP2- as substrate, pH 7.3, 37°C
0.3
pyridoxine
with MgATP2- as substrate, pH 7.3, 37°C
1.233
pyridoxine
pH 6.2, 37°C
6.08
pyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
0.12
pyridoxal
-
in the presence of K+, at pH 7.0 and 30°C
0.23
pyridoxal
-
in the presence of Na+, at pH 7.0 and 30°C
3.2
pyridoxal
-
at pH 6.5 and 37°C
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McCormick, D.B.; Gregory, M.E.; Snell, E.E.
Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties
J. Biol. Chem.
236
2076-2084
1961
Bos taurus, Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, Lactobacillus delbrueckii subsp. bulgaricus, Meleagris gallopavo, Mus musculus, Neurospora crassa, Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae
brenda
Kerry, J.A.; Kwok, F.
Purification and characterization of pyridoxal kinase from human erythrocytes
Prep. Biochem.
16
199-216
1986
Homo sapiens
brenda
Solomon, L.R.; Hillman, R.S.
Pyridoxine kinase activity in human erythrocytes and leukocytes: assay and properties
Biochem. Med.
16
223-233
1976
Homo sapiens
brenda
Chern, C.J.; Beutler, E.
Purification and characterization of human erythrocyte pyridoxine kinase
Clin. Chim. Acta
61
353-365
1975
Homo sapiens
brenda
Chern, C.J.; Beutler, E.
Assay for human erythrocyte pyridoxine kinase
Anal. Biochem.
67
97-109
1975
Homo sapiens
brenda
Laine-Cessac, P.; Cailleux, A.; Allain, P.
Mechanisms of the inhibition of human erythrocyte pyridoxal kinase by drugs
Biochem. Pharmacol.
54
863-870
1997
Homo sapiens
brenda
Lee, H.S.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.
Human pyridoxal kinase: overexpression and properties of the recombinant enzyme
Mol. Cells
10
452-459
2000
Homo sapiens
brenda
Laine-Cessac, P.; Allain, P.
Kinetic studies of the effects of K+, Na+, and Li+ on the catalytic activity of human erythrocyte pyridoxal kinase
Enzyme Protein
49
291-304
1997
Homo sapiens
brenda
di Salvo, M.L.; Hunt, S.; Schirch, V.
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases
Protein Expr. Purif.
36
300-306
2004
Escherichia coli, Homo sapiens (O00764), Homo sapiens
brenda
Kim, D.W.; Kim, C.K.; Choi, S.H.; Choi, H.S.; Kim, S.Y.; An, J.J.; Lee, S.R.; Lee, S.H.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, Y.J.; Cho, S.W.; Kang, J.H.; Kim, T.Y.; Lee, K.S.; Park, J.; Eum, W.S.; Choi, S.Y.
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Homo sapiens
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Kaestner, U.; Hallmen, C.; Wiese, M.; Leistner, E.; Drewke, C.
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Homo sapiens (O00764), Homo sapiens
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Flanagan, J.M.; Beutler, E.
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2006
Homo sapiens
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Bach, S.; Knockaert, M.; Reinhardt, J.; Lozach, O.; Schmitt, S.; Baratte, B.; Koken, M.; Coburn, S.P.; Tang, L.; Jiang, T.; Liang, D.C.; Galons, H.; Dierick, J.F.; Pinna, L.A.; Meggio, F.; Totzke, F.; Schaechtele, C.; Lerman, A.S.; Carnero, A.; Wan, Y.; Gray, N.; Meijer, L.
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Ovis aries, Homo sapiens
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Homo sapiens (O00764), Homo sapiens
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Musayev, F.N.; Di Salvo, M.L.; Ko, T.P.; Gandhi, A.K.; Goswami, A.; Schirch, V.; Safo, M.K.
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Homo sapiens (O00764), Homo sapiens
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Gandhi, A.K.; Ghatge, M.S.; Musayev, F.N.; Sease, A.; Aboagye, S.O.; di Salvo, M.L.; Schirch, V.; Safo, M.K.
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Homo sapiens (O00764), Homo sapiens
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Gandhi, A.K.; Desai, J.V.; Ghatge, M.S.; di Salvo, M.L.; Di Biase, S.; Danso-Danquah, R.; Musayev, F.N.; Contestabile, R.; Schirch, V.; Safo, M.K.
Crystal structures of human pyridoxal kinase in complex with the neurotoxins, ginkgotoxin and theophylline: insights into pyridoxal kinase inhibition
PLoS ONE
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Homo sapiens (O00764), Homo sapiens
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Navarro, F.; Ramirez-Sarmiento, C.A.; Guixe, V.
Catalytic and regulatory roles of species involved in metal-nucleotide equilibriums in human pyridoxal kinase
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2013
Homo sapiens
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Kimura, T.; Shirakawa, R.; Yaoita, N.; Hayashi, T.; Nagano, K.; Horiuchi, H.
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Homo sapiens, Plasmodium vivax (A5K1Z8), Trypanosoma cruzi (Q4D946), Plasmodium vivax Salvador I (A5K1Z8), Trypanosoma cruzi CL Brener (Q4D946)
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Ramos, R.J.; Albersen, M.; Vringer, E.; Bosma, M.; Zwakenberg, S.; Zwartkruis, F.; Jans, J.J.M.; Verhoeven-Duif, N.M.
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2019
Homo sapiens (O00764), Homo sapiens
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Mascolo, E.; Barile, A.; Mecarelli, L.S.; Amoroso, N.; Merigliano, C.; Massimi, A.; Saggio, I.; Hansen, T.; Tramonti, A.; Di Salvo, M.L.; Barbetti, F.; Contestabile, R.; Verni, F.
The expression of four pyridoxal kinase (PDXK) human variants in Drosophila impacts on genome integrity
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Homo sapiens (O00764), Homo sapiens, Drosophila melanogaster (Q7KUC2)
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