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Information on EC 2.7.1.35 - pyridoxal kinase
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2.7.1.35 pyridoxal kinaseIUBMB Comments
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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Word Map
- 2.7.1.35
- 5'-phosphate
-
vitamers
- pyridoxal-5'-phosphate
- plk
-
plp-dependent
- ribokinase
-
4-pyridoxic
- medicine
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
ePL kinase, ePL kinase 1, hPL kinase, HPLK, kinase (phosphorylating), pyridoxal, kinase, pyridoxal (phosphorylating), PdxK, PKH, PL kinase, PLK, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ePL kinase
-
two different forms encoded by genes PdxK and PdxY yielding kinase 1 and kinase 2, low activity of kinase 2 suggests that this kinase originally has another substrate but can also utilize pyridoxal
kinase (phosphorylating), pyridoxal
-
-
-
-
kinase, pyridoxal (phosphorylating)
-
-
-
-
PdxK
PL kinase
PLK
Plk1
PM kinase
-
-
-
-
PN kinase
-
-
-
-
PN/PL/PM kinase
-
-
-
-
pyridoxal 5-phosphate-kinase
-
-
-
-
pyridoxal kinase
pyridoxal kinase PKL
pyridoxal kinase-like protein SOS4
-
-
-
-
pyridoxal phosphokinase
-
-
-
-
pyridoxamine kinase
-
-
-
-
pyridoxine kinase
-
-
-
-
pyridoxine/pyridoxal/pyridoxamine kinase
-
-
-
-
SAV0580
Sos4
vitamin B6 kinase
-
-
-
-
PL kinase
-
-
-
-
PLK
-
-
-
-
pyridoxal kinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyridoxal = ADP + pyridoxal 5'-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:pyridoxal 5'-phosphotransferase
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
9026-42-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
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
-
?
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 + 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
-
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
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
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
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
-
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
-
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
-
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
-
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 + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
33% of the activity with pyridoxal
-
-
?
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 + pyridoxine
ADP + pyridoxine 5'-phosphate
-
40% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
46% of the activity with pyridoxal
-
-
?
additional information
?
-
-
the enzyme possesses also a 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase activity
-
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 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
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
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
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, 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
-
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
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Fe2+
K+
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
Mg2+
Mn2+
Na+
Ni2+
Rb+
-
Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Zn2+
additional information
Ca2+
-
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+
Co2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Cu2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, 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+
-
in the absence of any potassium ion, the activity is less than 5% of the maximum activity
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+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mg2+
-
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+
Mn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
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+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
-
Zn2+ is the most effective cation for catalysis under saturating substrate concentrations
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+
-
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+
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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-O-methylpyridoxine
-
i.e. ginkgotoxin. Treatment leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
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
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
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
NADH
-
0.5 mM, 14% inhibition of activity with pyridoxine, 11% inhibition of activity with pyridoxal
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
quinolinate
-
0.5 mM, 82% inhibition of activity with pyridoxine, 82% inhibition of activity with pyridoxal
rugulactone
selectively modifies the enzyme not at the active site cysteine, but on a remote cysteine residue
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
dopamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% 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
tryptamine
-
no inhibition of activity with pyridoxine, 72% inhibition of activity with pyridoxal
additional information
-
ATP4- and HATP3- do not affect the enzyme activity. Free Mg2+ does not inhibit enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
-
Km: 3.7 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Carcinoma
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.
Leishmaniasis, Visceral
Evaluation of Leishmania infantum pyridoxal kinase protein for the diagnosis of human and canine visceral leishmaniasis.
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.
Parkinson Disease
A loss of Pdxk model of Parkinson disease in Drosophila can be suppressed by Buffy.
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
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
Seizure susceptibility in the developing mouse and its relationship to glutamate decarboxylase and pyridoxal phosphate in brain.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0216
4'-deoxypyridoxine
-
in 70 mM potassium phosphate buffer, pH 6.2; pH 6.2, 37°C
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
0.025
ATP
-
in the presence of K+, and in complex with Mg2+; presence of 40 mM Na+, pH 7.3, 37°C
0.5
ATP
-
in the presence of Na+, and in complex with Mg2+; presence of 40 mM Na+, pH 7.3, 37°C
0.0466
ginkgotoxin
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.00165
pyridoxal
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.038
pyridoxal
-
recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C
0.111
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
0.26
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
0.0594
pyridoxamine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.048
pyridoxine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.044
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
0.045
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
106
ginkgotoxin
-
recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.165
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
0.328
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
131
pyridoxal
-
recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
127
pyridoxamine
-
recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.015
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
0.016
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
122
pyridoxine
-
recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000228
ginkgotoxin
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.000214
pyridoxamine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.000254
pyridoxine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.0009
pyridoxal
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.54
Mg2+
-
recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C
0.0398
Zn2+
-
recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0125
0.02
-
substrate: methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate
0.03
0.038
-
substrate: methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate
0.05
0.064
-
substrate: methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate
0.07
-
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C
0.112
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
-
the enzyme is inactive below pH 4.5. Enzyme activity decreases slowly above pH 6.0, to approximately 35% at pH 8.5
4.7 - 5.3
-
pH 4.7: about 60% of maximal activity, pH 5.3: about 40% of maximal activity
5 - 5.7
-
pH 5.0: about 90% of maximal activity, pH 5.7: about 45% of maximal activity
5 - 8
-
pH 5.0: about 70% of maximal activity, pH 8.0: about 50% of maximal activity
6 - 7
-
pH 6.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
641403, 641406, 641407, 641408, 641415, 641424, 641425, 641428, 672438, 673904, 674472, 737809, 738236
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
dentate granule cell. Pyridoxal kinase immunoreactivity is not increased after induction of long-term potentiation and not involved in increase in the efficiency of high frequency stimulus-induced potentiation of populations spike amplitude when compared with saline-, or Tat-protein-treated animals
brenda
-
from CA1 region, strong immunoreactivity
brenda
-
regions CA1, CA2/3 and dentate gyrus, increased enzyme activity detected 12-24 h after ischemia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
splice variant SOS4.1 (but not SOS4.2) is localized in chloroplasts
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
root growth of a sos4 mutant is significantly decreased when grown on either 100 mM or 200 mM sucrose as compared to root growth on10 mM sucrose. The sos4 mutant plant accumulates phytoglycogen
physiological function
additional information
-
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor
physiological function
-
pyridoxal kinase is a key enzyme in the metabolism of vitamin B6
physiological function
-
the enzyme is essential for growth of Trypanosoma brucei in vitro and for infectivity in mice
physiological function
-
the SOS4 pyridoxal kinase is required for maintenance of vitamin B6-mediated processes in chloroplasts. SOS4 is required for maintenance of phosphorylated B6 vitamer concentrations in chloroplasts
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Burkholderia multivorans (strain ATCC 17616 / 249)
Escherichia coli (strain K12)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
37000
40000
57200
-
2 * 57200, calculated from the deduced amino acid sequence, 2 * 58000, SDS-PAGE, native mass by gel filtration
58000
-
2 * 57200, calculated from the deduced amino acid sequence, 2 * 58000, SDS-PAGE, native mass by gel filtration
80000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
dimer
-
2 * 57200, calculated from the deduced amino acid sequence, 2 * 58000, SDS-PAGE, native mass by gel filtration
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 28% PEG 4000, 0.17 M sodium acetate trihydrate, and 0.1 M Tris-HCl (pH 8.5)
-
with 28% (w/v) PEG 4000, 0.17 M sodium acetate trihydrate, 0.1 M Tris-HCl (pH 8.5) as the precipitant in the presence of 10 mM ADP and 10 mM MgCl
-
hanging drop vapour diffusion method using 20 mM potassium phosphate, pH 7.5, 5 mM beta-mercaptoethanol, 0.2 mM EDTA, and 21% PEG 4K, 100 mM Tris-HCl, pH 8.5, 200 mM Na acetate, 40 mM MgSO4, and 10% glycerol
-
hanging drop vapour diffusion method using 0.1 mM Tris-HCl pH 8.0, 1.8 M NH4Ac, and 3% glycol
-
hanging drop vapour diffusion method using 100 mM Tris-HCl pH 8.0 and 50% 2-methyl-2,4-pentanediol; unliganded enzyme and in complex with MgATP, diffraction to 2.0 and 2.2 A rsolution, respectively. both Structures show similar open conformations. Mg2+ and Na+ act in tandem to anchor the ATP at the active site, which itself acts as a sink to bind several molecules of 2-methyl-2,4-pentanediol
-
in complex with ginkgotoxin and theophylline, hanging drop vapor diffusion method, using 48-50% (w/v) 2-methyl-1,3 propanediol as precipitant, at 22°C
-
crystallized in the orthorhombic form using the hanging-drop vapour-diffusion method with sodium citrate as the precipitant, crystals are transferred into a soaking liquid without citrate and two-heavy-atom derivatives are prepared
-
crystals are grown in the presence of 100 mM potassium phosphate, pH 7.2, and 120 mM ammonium sulfate and crystals grown in the presence of 600 mM potassium phosphate, pH 7.2, and in the absence of ammonium sulfate. The crystals are quite stable to X-rays and diffract at 2.2 A resolution
-
hanging drop vapor diffusion method in complex with adenosine 5’-(beta, gamma-methylenetriphosphate)-pyridoxamine, ADP-pyriodoxal 5’-phosphate, and ADP
-
hanging drop vapor diffusion method, in complex with (R)-roscovitine and N6-methyl-(R)-roscovitine
sitting drop vapor diffusion method, using 0.1 M Tris, pH 8.5, 1 M LiCl2, and 15% (w/v) PEG 6000
A0A0G5TGA8
native protein and in complex with its substrates to 1.4?1.85 A resolution. The protein shows a typical ribokinase fold with a central large beta-sheet consisting of nine strands, flanked by three and five structurally conserved alpha-helices
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K229Q
C124A
A0A0G5TGA8
the mutant shows about 2fold increased catalytic efficiency compared to the wild type enzyme
C124A
-
the mutant shows about 2fold increased catalytic efficiency compared to the wild type enzyme
-
C110A
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
C214A
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
C110A
-
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
-
C214A
-
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
-
additional information
plants lacking enzyme activity display chlorosis and reduced plant size, and hypersensitivity to NaCl and sucrose. Mutant has higher level of pyridoxine, pyridoxamine, and pyridoxal 5'-phosphate. Mutant shows higher activity of pyridoxine/pyridoxamine 5'-phosphate oxidase as well as of the vitamin B6 de novo pathway enzyme Pdx1 and increased total vitamin B6 levels
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3 M guanidine hydrochloride, enzyme loses more than 90% of the alpha-helix content
-
if instead of the phosphate buffer an acetate buffer is used, enzymatic activity is reduced to 74% and almost no activity is recorded when a citrate buffer is used
-
the enzyme is digested by chymotrypsin to proteolytic fragments of 24000 Da and 16000 Da
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM phosphate buffer, pH 7.3, stable for at least some weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
Ni-NTA agarose column chromatography and HiLoad 26/60 Superdex 200 gel filtration
-
Ni-NTA column chromatography and Mono Q column chromatography
A0A0G5TGA8
Phenyl ToyoPearl 650S column chromatography and Hi-Load Superdex 200 column gel filtration
-
recombinant enzyme
TMAE column chromatography, Phenyl Sepharose column chromatography, and hydroxyapatite column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta (DE3)pLysS cells; expression in Escherichia coli
-
expression in Escherichia coli
kinase 1 and 2 expressed in Escherichia coli HMS174(DE3), kinase 2 additionally expressed as His-tag fusion protein
-
recombinant enzyme is overexpressed in Escherichia coli as a fusion protein with maltose binding protein
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression patterns show that the gene is involved in abiotic stress and phytohormone regulation; expression patterns show that the gene is involved in abiotic stress and phytohormone regulation
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the enzyme which has lost more than 90% of the alpha-helix content after treatment with 3 M guanidine hydrochloride regains more than 90% of the original catalytic activity after overnight dialysis against 10 mM potassium phosphate, pH 7 at 4°C
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
plants lacking enzyme activity display chlorosis and reduced plant size, and hypersensitivity to NaCl and sucrose. Mutant has higher level of pyridoxine, pyridoxamine, and pyridoxal 5'-phosphate. Mutant shows higher activity of pyridoxine/pyridoxamine 5'-phosphate oxidase as well as of the vitamin B6 de novo pathway enzyme Pdx1 and increased total vitamin B6 levels
medicine
medicine
-
ingestion of 4'-O-methylpyridoxine, i.e. ginkgotoxin, triggers epileptic convulsions and other neuronal symptoms. 4'-O-Methylpyridoxine is an competitive inhibitor of pyridoxal kinase and leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
236
2076-2084
1961
Bos taurus, Enterococcus faecalis, Homo sapiens, Lactobacillus casei, Lactobacillus delbrueckii subsp. bulgaricus, Meleagris gallopavo, Mus musculus, Neurospora crassa, Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae
brenda
McCormick, D.B.; Snell, E.E.
Pyridoxal phosphokinase. II. Effects of inhibitors
J. Biol. Chem.
236
2085-2088
1961
Bos taurus, Enterococcus faecalis, Lactobacillus casei, Rattus norvegicus, Saccharomyces pastorianus
brenda
Hirakawa-Sakurai, T.; Ohkawa, K.; Matsuda, M.
Purification and properties of pyridoxal kinase from bovine brain
Mol. Cell. Biochem.
119
203-207
1993
Bos taurus
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
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
318-323
1973
Rattus norvegicus
brenda
Arone, A.; Rogers, P.; Scholz, G.; Kwok, F.
Crystallization and preliminary X-ray studies of pyridoxal kinase from sheep brain
J. Biol. Chem.
264
4322-4323
1989
Ovis aries
brenda
Abercrombie, D.M.; Martin, D.L.
Inhibition of pyridoxal kinase by the pyridoxal-gamma-aminobutyrate imine
J. Biol. Chem.
255
79-84
1980
Bos taurus
brenda
Karawya, E.; Mostafa, M.H.; Osman, N.
The kinetic mechanism of inhibition of liver pyridoxal kinase with tryptophan metabolites
Biochim. Biophys. Acta
657
153-158
1981
Ovis aries
brenda
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
Neary, J.T.; Meneely, R.L.; Grever, M.R.; Diven, W.F.
The interactions between biogenic amines and pyridoxal, pyridoxal phosphate, and pyridoxal kinase
Arch. Biochem. Biophys.
151
42-47
1972
Bos taurus
brenda
Chern, C.J.; Beutler, E.
Assay for human erythrocyte pyridoxine kinase
Anal. Biochem.
67
97-109
1975
Homo sapiens
brenda
Kerry, J.A.; Rohde, M.; Kwok, F.
Brain pyridoxal kinase. Purification and characterization
Eur. J. Biochem.
158
581-585
1986
Ovis aries
brenda
Kwok, F.; Churchich, J.E.
Brain pyridoxal kinase. Purification, substrate specificities, and sensitized photodestruction of an essential histidine
J. Biol. Chem.
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
170-177
1982
Ovis aries
brenda
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
brenda
Maras, B.; Valiante, S.; Orru, S.; Simmaco, M.; Barra, D.; Churchich, J.E.
Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues
J. Protein Chem.
18
259-268
1999
Ovis aries
brenda
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.
brenda
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
J. Bacteriol.
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
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
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
-
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
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
brenda
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
brenda
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
brenda
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)
brenda
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
J. Biol. Chem.
280
5242-5248
2005
Plasmodium falciparum
brenda
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
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, Homo sapiens (O00764)
brenda
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
F62
1006-1009
2006
Bacillus subtilis
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.
Tat-mediated protein transduction of human brain pyridoxal kinase into PC12 cells
Biochimie
87
481-487
2005
Homo sapiens
brenda
Kaestner, U.; Hallmen, C.; Wiese, M.; Leistner, E.; Drewke, C.
The human pyridoxal kinase, a plausible target for ginkgotoxin from Ginkgo biloba
FEBS J.
274
1036-1045
2007
Homo sapiens, Homo sapiens (O00764)
brenda
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
J. Bacteriol.
188
4542-4552
2006
Escherichia coli, Escherichia coli (P40191)
brenda
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
J. Biol. Chem.
280
31208-31219
2005
Homo sapiens, Ovis aries
brenda
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
J. Mol. Biol.
363
520-530
2006
Bacillus subtilis
brenda
Cao, P.; Gong, Y.; Tang, L.; Leung, Y.C.; Jiang, T.
Crystal structure of human pyridoxal kinase
J. Struct. Biol.
154
327-332
2006
Homo sapiens, Homo sapiens (O00764)
brenda
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.
16
2184-2194
2007
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
19
45-56
2009
Rattus norvegicus
brenda
Shi, R.; Zhang, J.; Jiang, C.; Huang, L.
Bombyx mori pyridoxal kinase cDNA cloning and enzymatic characterization
J. Genet. Genomics
34
683-690
2007
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.
145
985-996
2007
Arabidopsis thaliana (Q8W1X2)
brenda
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
1005-1014
2008
Brassica napus (A4K866), Brassica napus (A4K867), Brassica napus
brenda
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.
381
12-15
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
1108-1118
2009
Rattus norvegicus (O35331)
brenda
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
4
e4406
2009
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
Eur. J. Entomol.
108
25-34
2011
Bombyx mori (Q1PCB1)
-
brenda
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
Mol. Microbiol.
86
51-64
2012
Trypanosoma brucei
brenda
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
281-291
2013
Arabidopsis thaliana
brenda
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
7
e40954
2012
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
70
1550-1555
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.
478
300-306
2016
Pseudomonas aeruginosa (A0A0G5TGA8), Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO (A0A0G5TGA8)
brenda
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
1854
1160-1166
2015
Escherichia coli, Escherichia coli BW25113
brenda
Navarro, F.; Ramirez-Sarmiento, C.A.; Guixe, V.
Catalytic and regulatory roles of species involved in metal-nucleotide equilibriums in human pyridoxal kinase
Biometals
26
805-812
2013
Homo sapiens
brenda
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
FEBS Lett.
588
3068-3073
2014
Escherichia coli (P40191)
brenda
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
FEBS Lett.
588
3673-3676
2014
Homo sapiens, Plasmodium vivax (A5K1Z8), Plasmodium vivax Salvador I (A5K1Z8), Trypanosoma cruzi (Q4D946), Trypanosoma cruzi CL Brener (Q4D946)
brenda
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
J. Am. Chem. Soc.
136
4992-4999
2014
Staphylococcus aureus (A0A0H3JTP0), Staphylococcus aureus, Staphylococcus aureus ATCC 700699 (A0A0H3JTP0)
brenda
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