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ATP + 4'-deoxypyridoxine
ADP + 4'-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4'-O-methylpyridoxine
ADP + 4'-O-methylpyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
ATP + 5-deoxypyridoxal
ADP + ?
ATP + ginkgotoxin
?
-
ginkgotoxin is an effective pseudosubstrate
-
-
?
ATP + ginkgotoxin
ADP + ginkgotoxin 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate + ATP
methyl (1S)-1-[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate + ADP
-
-
very probably: methyl (1S)-1-[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate is an inhibitor of Plasmodium falciparum ornithine decarboxylase
-
?
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate + ATP
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)histidinate + ADP
-
-
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)histidinate is an inhibitor of Plasmodium falciparum ornithine decarboxylase: IC50 = 0.058 mM
-
?
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate + ATP
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)tryptophanate + ADP
-
-
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)tryptophanate is an inhibitor of Plasmodium falciparum ornithine decarboxylase: IC50 = 0.064 mM
-
?
pyridoxal + ATP
pyridoxal 5'-phosphate
-
-
-
-
?
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
-
-
-
-
?
pyridoxamine + ATP
pyridoxamine 5'-phosphate
-
-
-
-
?
pyridoxine + ATP
pyridoxine 5'-phosphate
-
-
-
-
?
additional information
?
-
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine

ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
reaction of EC 2.7.1.49
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
reaction of EC 2.7.1.49
-
-
?
ATP + 4-deoxypyridoxine

ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 5-deoxypyridoxal

ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + omega-methylpyridoxal

ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal

ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
the SOS4 gene encodes a pyridoxal kinase that functions upstream of ethylene and auxin in root hair development, SOS4 is required for the initiation and tip growth of root hairs
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
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 + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
the pdxY gene encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. The pyridoxal kinase PdxY and the pyridoxine/pyridoxal/pyridoxamine kinase PdxK are the only physiologically important B6 vitamer kinases in Escherichia coli and their function is confined to the pyridoxal 5'-phosphate salvage pathway
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
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 + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
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 + 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
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes, increased enzyme activity detected 12-24 h after ischemia, pyridoxal 5'-phosphate essential for the synthesis of some neurotransmitters
-
-
?
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 + 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
-
key enzyme in transformation of vitamin B6 to pyridoxal 5'-phosphate. Pyridoxal 5'-phosphate is the crucial cofactor required by numerous enzymes involved in the metabolism of amino acids and the synthesis of many neurotransmitters
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
A0A0G5TGA8
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
A0A0G5TGA8
-
-
-
?
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 + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
important enzyme involved in bioactivation of vitamin B6
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes, interaction of pyridoxal kinase with pyridoxal 5'-phosphate dependent enzymes seems to be important for providing sufficient amounts of enzyme cofactor
-
-
?
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 + pyridoxamine

ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
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
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
33% of the activity with pyridoxal
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
not a substrate of the purified enzyme
-
-
-
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine

ADP + pyridoxine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 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
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
-
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
-
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
40% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
46% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
additional information

?
-
-
the enzyme possesses also a 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase activity
-
-
-
additional information
?
-
-
no activity with GTP
-
-
-
additional information
?
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
-
additional information
?
-
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
-
additional information
?
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
-
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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
Rb+
-
Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Ca2+

-
-
Ca2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+

-
-
Co2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Co2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
-
0.2 mM, partial activation
Cu2+

-
-
Cu2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Cu2+
-
0.2 mM, partial activation
Fe2+

-
-
Fe2+
-
cations activate in decreaseing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
K+

-
when only triethanolamine is present as the cation, K+ is an activator of the enzyme
K+
-
activates in presence of optimal concentrations of Zn2+
K+
-
in the absence of any potassium ion, the activity is less than 5% of the maximum activity
K+
-
most effective activator of the monovalent cations
K+
-
most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM
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; affinity to pyridoxal and ATP is increased manifold in the presence of K+ compared to Na+, 2.5fold increase of activity
K+
-
Km: 8.9 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Mg2+

-
-
Mg2+
-
active in the presence of Mg2+
Mg2+
-
in complex with ATP most likely preferred substrate in vivo
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
Mg2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mg2+
-
in complex with ATP most likely preferred substrate in vivo
Mg2+
-
acts in complex with ATP
Mg2+
-
best activator, optimum activity at 0.25 mM Mn2+
Mn2+

-
-
Mn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mn2+
-
0.2 mM, partial activation
Mn2+
-
0.2 mM, partial activation
Mn2+
-
0.2 mM, partial activation
Mn2+
-
optimum activity at 0.05 mM Mn2+
Na+

-
increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal
Na+
-
6fold increase of activity; 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
Ni2+

-
-
Ni2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Ni2+
-
0.2 mM, partial activation
Zn2+

-
Zn2+ is the most effective cation for catalysis under saturating substrate concentrations
Zn2+
-
in complex with ATP preferred substrate in vitro
Zn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
-
divalent cation required, optimal concentration is 0.33 mM. Zn2+ is superior to Mg2+ below the optimum concentration of Zn2+
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+
-
in complex with ATP preferred substrate in vitro
Zn2+
-
activator at low concentrations (0.019 mM optimal concentration), most effective divalent cation for catalysis
Zn2+
-
the enzyme requires divalent cations for activity. At 0.08 mM the cations activate in order of decreasing efficiency: Mn2+, Zn2+, Mg2+. At 0.4 mM the cations activate in the order of decreasing efficiency: Mn2+, Zn2+, Mg2+
Zn2+
-
0.2 mM, activates; half-maximal activation at 0.01 mM
additional information

-
the presence of 100 mM NaCl does not alter the potassium activation profile
additional information
-
Li+, Cs+, and Rb+ show no significant activity enhancement; no singnificant activity with Li+, Cs+, Rb+
additional information
-
ZnCl2 and Ca2+ do not activate the enzyme
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(2-Diethylaminoethyl)hydrazine
-
0.005 mM, 20% inhibition
1,1-Bis(2-diethylaminoethyl)hydrazine
-
0.005 mM, 51% inhibition
1,4-Diaminopiperazine
-
0.005 mM, 59% inhibition
1-(2-Hydrazinopropyl)piperidine
-
0.005 mM, 31% inhibition
1-(3-Dimethylamino-2-methylpropyl)hydrazine
-
0.005 mM, 39% inhibition
1-Aminopiperidine
-
0.005 mM, 58% inhibition
1-Cyclohexyl-1-methylhydrazine
-
0.005 mM, 29% inhibition
2,2'-hydrazinediethanol
-
0.005 mM, 47% inhibition
2,6-Dimethyl-3,4-bis(hydroxymethyl)pyridine
-
-
2-Methyl-3-amino-4,5,6-tris(hydroxymethyl)pyridine
-
-
2-Methyl-3-amino-4,5-bis(hydroxymethyl)pyridine
-
-
2-Methyl-3-hydroxy-5,6-bis(hydroxymethyl)pyridine
-
-
2-Methyl-4,5-bis(hydroxymethyl)pyridine
-
-
2-[1-(2-Diethylaminoethyl)hydrazine]ethanol
-
0.005 mM, 44% inhibition
3,4-dihydroxyphenylalanine
-
-
3-hydroxyanthranilic acid
-
IC50: 0.12 mM
3-hydroxykynurenine
-
IC50: 0.1 mM
4'-O-methylpyridoxine
-
i.e. ginkgotoxin. Treatment leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
4-Aminomorpholine
-
0.005 mM, 52% inhibition
5-dimethylaminonaphthalene-1-sulfonyl-4-aminobutyrate
-
competitive with respect to pyridoxal
5-hydroxytryptamine
-
0.5 mM, 11% inhibition of activity with pyridoxine, 81% inhibition of activity with pyridoxal
alpha-Methylphenethylhydrazine
alpha-Methylphenethylhydrazone
aminooxyacetic acid
-
0.002 mM, 50% inhibition
Ca2+
-
low substrate inhibition
Caffeine
-
21% inhibition at 0.1 mM
Chloroquine
about 40% inhibition at 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
enprofylline
-
33% inhibition at 0.1 mM
gamma-aminobutyric acid
-
-
isoniazid
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 81% inhibition
K+
-
at high concentrations
L-canaline
-
0.01 mM, 50% inhibition
lamotrigine
-
45% inhibition at 0.1 mM
levodopa
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 16% inhibition
Li+
-
at high concentrations
Mn2+
-
excess free divalent cations inhibit the enzyme
muzolimine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 27% inhibition
N,N'-Bis(pyridoxyl)hydrazine
-
0.0005 mM, 50% inhibition
N-Dansyl-1,8-diaminooctane
NADH
-
0.5 mM, 14% inhibition of activity with pyridoxine, 11% inhibition of activity with pyridoxal
Octylhydrazine
-
0.005 mM, 53% inhibition
picolinate
-
0.5 mM, 95% inhibition of activity with pyridoxine, 97% inhibition of activity with pyridoxal
progabide
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate
pyridoxal 5'-phosphate
-
-
pyridoxal semicarbazone
-
0.00005 mM, 50% inhibition
pyridoxal-gamma-aminobutyrate
-
-
pyridoxine
-
substrate inhibition above 0.2 mM
quinolinate
-
0.5 mM, 82% inhibition of activity with pyridoxine, 82% inhibition of activity with pyridoxal
quinolinic acid
-
IC50: 0.42 mM
rugulactone
selectively modifies the enzyme not at the active site cysteine, but on a remote cysteine residue
Semicarbazine
-
0.0005 mM, 50% inhibition
Theobromine
-
22% inhibition at 0.1 mM
Thiamphenicol
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 31% inhibition
xanthurenate
-
0.5 mM, 19% inhibition of activity with pyridoxine, 18% inhibition of activity with pyridoxal
xanthurenic acid
-
IC50: 0.36 mM
ZnATP2-
-
weak substrate inhibition
(R)-roscovitine

-
-
(R)-roscovitine
binds to the pyridoxal binding site
4-deoxypyridoxine

-
-
4-deoxypyridoxine
-
competitive with respect to pyridoxal
alpha-Methylphenethylhydrazine

-
0.001 mM, 50% inhibition
alpha-Methylphenethylhydrazine
-
0.015 mM, 50% inhibition
alpha-Methylphenethylhydrazone

-
0.001 mM, 50% inhibition
alpha-Methylphenethylhydrazone
-
0.015 mM, 50% inhibition
azine

-
0.000065 mM, 50% inhibition
azine
-
0.0004 mM, 50% inhibition
dopamine

-
-
dopamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% inhibition
ginkgotoxin

-
-
ginkgotoxin
-
i.e. 4'-O-methylpyridoxine, complete inhibition at 0.1 mM
ginkgotoxin
-
i.e.4'-O-methylpyridoxine
hydrazine

-
0.00055 mM, 50% inhibition
hydrazine
-
0.05 mM, 50% inhibition
hydroxylamine

-
0.0005 mM, 50% inhibition
hydroxylamine
-
0.01 mM, 50% inhibition
Mg2+

-
excess free divalent cations inhibit the enzyme
Mg2+
-
low substrate inhibition
N-Dansyl-1,8-diaminooctane

-
-
N-Dansyl-1,8-diaminooctane
-
-
Na+

-
at high concentrations
Na+
-
inhibits above 50 mM
Oxime

-
0.0025 mM, 50% inhibition
Oxime
-
0.008 mM, 50% inhibition
primaquine

-
competitive inhibition, complete inhibition at 0.75 mM
primaquine
competitive inhibition, complete inhibition at 1 mM
primaquine
competitive inhibition, about 70% inhibition at 1 mM
pyridoxal

-
-
pyridoxal
-
effective competitive inhibitor
pyridoxal
-
substrate inhibition
pyridoxal
-
0.1 mM, substrate inhibition
pyridoxaloxime

-
strong competitive inhibitor
pyridoxaloxime
-
competitive with respect to pyridoxal
pyridoxamine

-
effective competitive inhibitor
serotonin

-
-
serotonin
-
0.08 mM, 50% inhibition
theophylline

-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate, 86% inhibition of reaction with pyridoxal, 88% inhibition of reaction with pyridoxamine
theophylline
-
60% inhibition at 0.1 mM
tryptamine

-
no inhibition of activity with pyridoxine, 72% inhibition of activity with pyridoxal
Zn2+

-
slight inhibition above the optimum of 0.33 mM
Zn2+
-
excess free divalent cations inhibit the enzyme
Zn2+
-
ZnCl2 shows pronounced high substrate inhibition
additional information

-
no inhibition by Tyr, Trp and 5-hydroxytryptophan
-
additional information
-
ATP4- and HATP3- do not affect the enzyme activity. Free Mg2+ does not inhibit enzyme activity
-
additional information
-
not inhibited by chloroquine
-
additional information
not inhibited by chloroquine
-
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0.0216
4'-deoxypyridoxine
-
in 70 mM potassium phosphate buffer, pH 6.2; pH 6.2, 37°C
0.00495
4'-O-methylpyridoxine
-
pH 6.2, 37°C
1.85 - 2.03
4-Amino-5-hydroxymethyl-2-methylpyrimidine
0.00495 - 0.0466
ginkgotoxin
0.194
MnATP2-
-
pH 5.8, 37°C
0.006 - 0.126
pyridoxamine
0.00172 - 2.07
pyridoxine
additional information
additional information
-
effect of KCl on Km-values
-
1.85
4-Amino-5-hydroxymethyl-2-methylpyrimidine

mutant C110A, pH not specified in the publication, temperature not specified in the publication
1.99
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
2.03
4-Amino-5-hydroxymethyl-2-methylpyrimidine
-
pH 8, 37°C
0.0091
ATP

-
pH 7, 37°C
0.012
ATP
-
pH 6.0, 37°C
0.02
ATP
-
in the presence of Zn2+, at pH 6.5 and 37°C
0.025
ATP
-
in the presence of K+, and in complex with Mg2+; presence of 40 mM Na+, pH 7.3, 37°C
0.0579
ATP
-
in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C
0.078
ATP
A0A0G5TGA8
mutant enzyme C124A, at pH 7.4 and 37°C
0.082
ATP
-
pH 6.5, 30°C
0.102
ATP
A0A0G5TGA8
wild type enzyme, at pH 7.4 and 37°C
0.127
ATP
-
pH 7, 37°C, recombinant enzyme
0.5
ATP
-
in the presence of Na+, and in complex with Mg2+; presence of 40 mM Na+, pH 7.3, 37°C
0.00495
ginkgotoxin

-
in 70 mM potassium phosphate buffer, pH 6.2
0.0466
ginkgotoxin
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.17
MgATP

-
D235A mutant protein
0.18
MgATP
-
D235N mutant protein
0.19
MgATP
-
wild-type protein
0.42
MgATP
-
with pyridoxal as substrate, pH 7.3, 37°C
0.101
MgATP2-

-
pH 5.8, 37°C
0.6
MgATP2-
-
kinase 1 with pyridoxal as substrate, pH 7.3, 37°C
0.00122
pyridoxal

-
in the presence of K+, at pH 7.0 and 30°C
0.00165
pyridoxal
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.0028
pyridoxal
-
in 70 mM potassium phosphate buffer, pH 6.2
0.01
pyridoxal
-
in the presence of K+; presence of 40 mM Na+, pH 7.3, 37°C
0.0153
pyridoxal
in the presence of K+, at pH 7.0 and 30°C
0.0216
pyridoxal
in the presence of K+, at pH 7.0 and 30°C
0.022
pyridoxal
-
pH 7, 37°C
0.024
pyridoxal
-
wild-type protein
0.025
pyridoxal
-
pH 6, 37°C
0.03
pyridoxal
-
with MgATP2- as substrate, pH 7.3, 37°C
0.037
pyridoxal
A0A0G5TGA8
mutant enzyme C124A, at pH 7.4 and 37°C
0.038
pyridoxal
-
pH 7, 37°C, recombinant enzyme
0.038
pyridoxal
-
recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C
0.0441
pyridoxal
-
in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C
0.047
pyridoxal
-
pH 8, 37°C
0.053
pyridoxal
A0A0G5TGA8
wild type enzyme, at pH 7.4 and 37°C
0.058
pyridoxal
-
D235N mutant protein
0.0587
pyridoxal
-
pH 6.2, 37°C
0.07
pyridoxal
-
pH 6.5, 30°C
0.0739
pyridoxal
-
in the presence of Na+, at pH 7.0 and 30°C
0.075
pyridoxal
-
in the presence of Na+; presence of 40 mM Na+, pH 7.3, 37°C
0.097
pyridoxal
-
pH 7, 37°C
0.1
pyridoxal
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.111
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
0.17
pyridoxal
-
D235A mutant protein
0.19
pyridoxal
-
kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C
0.26
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
0.35
pyridoxal
-
with ZnATP2- as substrate, pH 7.3, 37°C
0.49
pyridoxal
-
at pH 6.5 and 37°C
0.006
pyridoxamine

-
pH 6.5
0.01
pyridoxamine
-
kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C
0.03
pyridoxamine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.035
pyridoxamine
-
with MgATP2- as substrate, pH 7.3, 37°C
0.0594
pyridoxamine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.126
pyridoxamine
-
in 70 mM potassium phosphate buffer, pH 6.2; pH 6.2, 37°C
0.00172
pyridoxine

-
pH 7.0, 37°C
0.00987
pyridoxine
-
in 70 mM potassium phosphate buffer, pH 6.2; pH 6.2, 37°C
0.015
pyridoxine
-
with ZnATP2- as substrate, pH 7.3, 37°C
0.017
pyridoxine
-
pH 6.0, 37°C
0.02
pyridoxine
-
with MgATP2- as substrate, pH 7.3, 37°C
0.025
pyridoxine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.026
pyridoxine
-
pH 6.5
0.048
pyridoxine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.06
pyridoxine
-
pH 5.8, 37°C, with MnATP2- as the second substrate
0.212
pyridoxine
-
pH 6.5, 30°C
1.51
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
2.07
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.06
ZnATP2-

-
pH 5.8, 37°C
0.07
ZnATP2-
-
kinase 1 with pyridoxal as substrate, pH 7.3, 37°C
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Takeuchi, F.; Tsubouchi, R.; Shibata, Y.
Effect of tryptophan metabolites on the activities of rat liver pyridoxal kinase and pyridoxamine 5-phosphate oxidase in vitro
Biochem. J.
227
537-544
1985
Rattus norvegicus
brenda
McCormick, D.B.; Gregory, M.E.; Snell, E.E.
Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties
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2076-2084
1961
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McCormick, D.B.; Snell, E.E.
Pyridoxal phosphokinase. II. Effects of inhibitors
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236
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Purification and properties of pyridoxal kinase from bovine brain
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1993
Bos taurus
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Kerry, J.A.; Kwok, F.
Purification and characterization of pyridoxal kinase from human erythrocytes
Prep. Biochem.
16
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1986
Homo sapiens
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Pyridoxine kinase activity in human erythrocytes and leukocytes: assay and properties
Biochem. Med.
16
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1976
Homo sapiens
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Chern, C.J.; Beutler, E.
Purification and characterization of human erythrocyte pyridoxine kinase
Clin. Chim. Acta
61
353-365
1975
Homo sapiens
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Gaeng, V.; von Collins, E.N.
Inhibition of pyridoxal kinase from rat liver in vitro by aromatic and aliphatic amines
Int. J. Vitam. Nutr. Res.
43
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1973
Rattus norvegicus
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Arone, A.; Rogers, P.; Scholz, G.; Kwok, F.
Crystallization and preliminary X-ray studies of pyridoxal kinase from sheep brain
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264
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Ovis aries
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Abercrombie, D.M.; Martin, D.L.
Inhibition of pyridoxal kinase by the pyridoxal-gamma-aminobutyrate imine
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255
79-84
1980
Bos taurus
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Karawya, E.; Mostafa, M.H.; Osman, N.
The kinetic mechanism of inhibition of liver pyridoxal kinase with tryptophan metabolites
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657
153-158
1981
Ovis aries
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Kwok, F.; Kerry, J.A.; Churchich, J.E.
Sheep brain pyridoxal kinase: fluorescence spectroscopy of the dimeric enzyme
Biochim. Biophys. Acta
874
167-173
1986
Ovis aries
brenda
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The interactions between biogenic amines and pyridoxal, pyridoxal phosphate, and pyridoxal kinase
Arch. Biochem. Biophys.
151
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1972
Bos taurus
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Assay for human erythrocyte pyridoxine kinase
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67
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1975
Homo sapiens
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Brain pyridoxal kinase. Purification and characterization
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158
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Ovis aries
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Brain pyridoxal kinase. Purification, substrate specificities, and sensitized photodestruction of an essential histidine
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254
6489-6495
1979
Sus scrofa
brenda
Karawya, E.; Fonda, M.L.
Physical and kinetic properties of sheep liver pyridoxine kinase
Arch. Biochem. Biophys.
216
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1982
Ovis aries
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Li, M.H.; Kwok, F.; An, X.M.; Chang, W.R.; Lau, C.K.; Zhang, J.P.; Liu, S.Q.; Leung, Y.C.; Jiang, T.; Liang, D.C.
Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain
Acta Crystallogr. Sect. D
58
1479-1481
2002
Ovis aries
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Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues
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18
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1999
Ovis aries
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Shi, H.; Zhu, J.K.
SOS4, a pyridoxal kinase gene, is required for root hair development in Arabidopsis
Plant Physiol.
129
585-593
2002
Arabidopsis sp.
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Yang, Y.; Tsui, H.C.; Man, T.K.; Winkler, M.E.
Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12
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180
1814-1821
1998
Escherichia coli
brenda
Laine-Cessac, P.; Cailleux, A.; Allain, P.
Mechanisms of the inhibition of human erythrocyte pyridoxal kinase by drugs
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54
863-870
1997
Homo sapiens
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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
Scott, T.C.; Phillips, M.A.
Characterization of Trypanosoma brucei pyridoxal kinase: purification, gene isolation and expression in Escherichia coli
Mol. Biochem. Parasitol.
88
1-11
1997
Trypanosoma brucei
brenda
Cho, J.J.; Kim, S.K.; Kim, Y.T.
Catalytic and structural properties of pyridoxal kinase
J. Biochem. Mol. Biol.
30
125-131
1997
Ovis aries
-
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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
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Fong, C.C.; Lai, W.P.; Leung, Y.C.; Lo, S.C.; Wong, M.S.; Yang, M.
Study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor
Biochim. Biophys. Acta
1596
95-107
2002
Sus scrofa
brenda
Park, J.H.; Burns, K.; Kinsland, C.; Begley, T.P.
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase
J. Bacteriol.
186
1571-1573
2004
Bacillus subtilis
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Cheung, P.Y.; Fong, C.C.; Ng, K.T.; Lam, W.C.; Leung, Y.C.; Tsang, C.W.; Yang, M.; Wong, M.S.
Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes
J. Biochem.
134
731-738
2003
Sus scrofa
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Li, M.H.; Kwok, F.; Chang, W.R.; Liu, S.Q.; Lo, S.C.; Zhang, J.P.; Jiang, T.; Liang, D.C.
Conformational changes in the reaction of pyridoxal kinase
J. Biol. Chem.
279
17459-17465
2004
Ovis aries
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Tang, L.; Li, M.H.; Cao, P.; Wang, F.; Chang, W.R.; Bach, S.; Reinhardt, J.; Ferandin, Y.; Galons, H.; Wan, Y.; Gray, N.; Meijer, L.; Jiang, T.; Liang, D.C.
Crystal structure of pyridoxal kinase in complex with roscovitine and derivatives
J. Biol. Chem.
280
31220-31229
2005
Ovis aries (P82197)
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Wrenger, C.; Eschbach, M.L.; Muller, I.B.; Warnecke, D.; Walter, R.D.
Analysis of the vitamin B6 biosynthesis pathway in the human malaria parasite Plasmodium falciparum
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280
5242-5248
2005
Plasmodium falciparum
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Hwang, I.K.; Yoo, K.Y.; Kim, D.S.; Eum, W.S.; Park, J.K.; Park, J.; Kwon, O.S.; Kang, T.C.; Choi, S.Y.; Won, M.H.
Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia
Neuroscience
128
511-518
2004
Meriones unguiculatus
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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, Homo sapiens (O00764)
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Newman, J.A.; Das, S.K.; Sedelnikova, S.E.; Rice, D.W.
Cloning, purification and preliminary crystallographic analysis of a putative pyridoxal kinase from Bacillus subtilis
Acta Crystallogr. Sect. F
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2006
Bacillus subtilis
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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.
Tat-mediated protein transduction of human brain pyridoxal kinase into PC12 cells
Biochimie
87
481-487
2005
Homo sapiens
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Kaestner, U.; Hallmen, C.; Wiese, M.; Leistner, E.; Drewke, C.
The human pyridoxal kinase, a plausible target for ginkgotoxin from Ginkgo biloba
FEBS J.
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2007
Homo sapiens, Homo sapiens (O00764)
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Flanagan, J.M.; Beutler, E.
The genetic basis of human erythrocyte pyridoxal kinase activity variation
Haematologica
91
801-804
2006
Homo sapiens
brenda
Safo, M.K.; Musayev, F.N.; di Salvo, M.L.; Hunt, S.; Claude, J.B.; Schirch, V.
Crystal structure of pyridoxal kinase from the Escherichia coli pdxK gene: implications for the classification of pyridoxal kinases
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Escherichia coli, Escherichia coli (P40191)
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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.
Roscovitine targets, protein kinases and pyridoxal kinase
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Homo sapiens, Ovis aries
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Newman, J.A.; Das, S.K.; Sedelnikova, S.E.; Rice, D.W.
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution
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Bacillus subtilis
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Cao, P.; Gong, Y.; Tang, L.; Leung, Y.C.; Jiang, T.
Crystal structure of human pyridoxal kinase
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Homo sapiens, Homo sapiens (O00764)
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Musayev, F.N.; Di Salvo, M.L.; Ko, T.P.; Gandhi, A.K.; Goswami, A.; Schirch, V.; Safo, M.K.
Crystal Structure of human pyridoxal kinase: Structural basis of M+ and M2+ activation
Protein Sci.
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Homo sapiens, Homo sapiens (O00764)
brenda
Kwak, S.E.; Kim, J.E.; Kim, D.W.; Kwon, O.S.; Choi, S.Y.; Kang, T.C.
Pyridoxine 5-phosphate oxidase, not pyridoxal kinase, involves in long-term potentiation induction in the rat dentate gyrus
Hippocampus
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2009
Rattus norvegicus
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Shi, R.; Zhang, J.; Jiang, C.; Huang, L.
Bombyx mori pyridoxal kinase cDNA cloning and enzymatic characterization
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Bombyx mori, Bombyx mori (Q1PCB1)
brenda
Gonzalez, E.; Danehower, D.; Daub, M.E.
Vitamer levels, stress response, enzyme activity, and gene regulation of Arabidopsis lines mutant in the pyridoxine/pyridoxamine 5-phosphate oxidase (PDX3) and the pyridoxal kinase (SOS4) genes involved in the vitamin B6 salvage pathway
Plant Physiol.
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Arabidopsis thaliana (Q8W1X2)
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Yu, S.; Luo, L.
Expression analysis of a novel pyridoxal kinase messenger RNA splice variant, PKL, in oil rape suffering abiotic stress and phytohormones
Acta Biochim. Biophys. Sin. (Shanghai)
40
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2008
Brassica napus (A4K866), Brassica napus (A4K867), Brassica napus
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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.
Kinetic and structural studies of the role of the active site residue Asp235 of human pyridoxal kinase
Biochem. Biophys. Res. Commun.
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2009
Homo sapiens, Homo sapiens (O00764)
brenda
Kwak, S.E.; Kim, J.E.; Kim, D.W.; Kwon, O.S.; Choi, S.Y.; Kang, T.C.
Enhanced pyridoxal 5-phosphate synthetic enzyme immunoreactivities do not contribute to GABAergic inhibition in the rat hippocampus following pilocarpine-induced status epilepticus
Neuroscience
159
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2009
Rattus norvegicus (O35331)
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Mueller, I.B.; Wu, F.; Bergmann, B.; Knoeckel, J.; Walter, R.D.; Gehring, H.; Wrenger, C.
Poisoning pyridoxal 5-phosphate-dependent enzymes: a new strategy to target the malaria parasite Plasmodium falciparum
PLoS ONE
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Plasmodium falciparum
brenda
Huang, S.; Ma, W.; Zhang, P.; Zhang, J.; Xie, Y.; Huang, L.
Recombinant expression, purification and characterization of Bombyx mori (Lepidoptera: Bombycidae) pyridoxal kinase
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Bombyx mori (Q1PCB1)
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Jones, D.C.; Alphey, M.S.; Wyllie, S.; Fairlamb, A.H.
Chemical, genetic and structural assessment of pyridoxal kinase as a drug target in the African trypanosome
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Trypanosoma brucei
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Rueschhoff, E.E.; Gillikin, J.W.; Sederoff, H.W.; Daub, M.E.
The SOS4 pyridoxal kinase is required for maintenance of vitamin B6-mediated processes in chloroplasts
Plant Physiol. Biochem.
63
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2013
Arabidopsis thaliana
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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, Homo sapiens (O00764)
brenda
Kronenberger, T.; Lunev, S.; Wrenger, C.; Groves, M.R.
Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK)
Acta Crystallogr. Sect. F
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2014
Plasmodium falciparum (A0A1C3KUB4), Plasmodium falciparum
brenda
Kim, M.I.; Hong, M.
Crystal structure and catalytic mechanism of pyridoxal kinase from Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
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2016
Pseudomonas aeruginosa (A0A0G5TGA8), Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO (A0A0G5TGA8)
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di Salvo, M.L.; Nogues, I.; Parroni, A.; Tramonti, A.; Milano, T.; Pascarella, S.; Contestabile, R.
On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5-phosphate
Biochim. Biophys. Acta
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2015
Escherichia coli, Escherichia coli BW25113
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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
Biometals
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805-812
2013
Homo sapiens
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Castro-Fernandez, V.; Bravo-Moraga, F.; Ramirez-Sarmiento, C.A.; Guixe, V.
Emergence of pyridoxal phosphorylation through a promiscuous ancestor during the evolution of hydroxymethyl pyrimidine kinases
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2014
Escherichia coli (P40191)
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Kimura, T.; Shirakawa, R.; Yaoita, N.; Hayashi, T.; Nagano, K.; Horiuchi, H.
The antimalarial drugs chloroquine and primaquine inhibit pyridoxal kinase, an essential enzyme for vitamin B6 production
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2014
Homo sapiens, Plasmodium vivax (A5K1Z8), Plasmodium vivax Salvador I (A5K1Z8), Trypanosoma cruzi (Q4D946), Trypanosoma cruzi CL Brener (Q4D946)
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Nodwell, M.B.; Koch, M.F.; Alte, F.; Schneider, S.; Sieber, S.A.
A subfamily of bacterial ribokinases utilizes a hemithioacetal for pyridoxal phosphate salvage
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2014
Staphylococcus aureus (A0A0H3JTP0), Staphylococcus aureus, Staphylococcus aureus ATCC 700699 (A0A0H3JTP0)
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