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Information on EC 2.7.1.35 - pyridoxal kinase and Organism(s) Homo sapiens and UniProt Accession O00764

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IUBMB Comments
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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This record set is specific for:
Homo sapiens
UNIPROT: O00764
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxal kinase, pyridoxine kinase, pl kinase, ldpdxk, pyridoxal phosphokinase, stplk, hpl kinase, epl kinase 1, pn kinase, pyridoxamine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hPL kinase
-
pyridoxal kinase
-
kinase (phosphorylating), pyridoxal
-
-
-
-
kinase, pyridoxal (phosphorylating)
-
-
-
-
PL kinase
-
-
-
-
PM kinase
-
-
-
-
PN kinase
-
-
-
-
PN/PL/PM kinase
-
-
-
-
pyridoxal 5-phosphate-kinase
-
-
-
-
pyridoxal kinase
-
-
-
-
pyridoxal kinase-like protein SOS4
-
-
-
-
pyridoxal phosphokinase
-
-
-
-
pyridoxamine kinase
-
-
-
-
pyridoxine kinase
-
-
-
-
pyridoxine/pyridoxal/pyridoxamine kinase
-
-
-
-
vitamin B6 kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyridoxal 5'-phosphotransferase
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-42-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4'-deoxypyridoxine
ADP + 4'-deoxypyridoxine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 4'-O-methylpyridoxine
ADP + 4'-O-methylpyridoxine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + ginkgotoxin
ADP + ginkgotoxin 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
show the reaction diagram
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
show the reaction diagram
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
show the reaction diagram
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
show the reaction diagram
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
in complex with ATP preferred substrate in vitro
Ca2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Fe2+
-
cations activate in decreaseing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Li+
-
poor activator which seems to modify the enzymatic mechanism from a random to an ordered sequential pattern with ATP bound before pyridoxal. Km: 37 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-deoxypyridoxine
-
4'-O-methylpyridoxine
i.e. ginkgotoxin. Treatment leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
Caffeine
21% inhibition at 0.1 mM
enprofylline
33% inhibition at 0.1 mM
ginkgotoxin
lamotrigine
45% inhibition at 0.1 mM
Na+
inhibits above 50 mM
Theobromine
22% inhibition at 0.1 mM
theophylline
60% inhibition at 0.1 mM
(R)-roscovitine
-
-
1,4-diaminobutane
-
-
1,6-diaminohexane
-
-
1,8-diaminooctane
-
-
4-deoxypyridoxine
-
-
Cr2+
-
-
cycloserine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 42% inhibition
D-penicillamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 20% inhibition
dopamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% inhibition
gamma-aminobutyric acid
-
-
isoniazid
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 81% inhibition
levodopa
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 16% inhibition
muzolimine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 27% inhibition
N-Dansyl-1,8-diaminooctane
-
-
primaquine
-
competitive inhibition, complete inhibition at 0.75 mM
progabide
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate
pyridoxal
pyridoxamine
theophylline
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate, 86% inhibition of reaction with pyridoxal, 88% inhibition of reaction with pyridoxamine
Thiamphenicol
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 31% inhibition
ZnATP2-
-
weak substrate inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
-
slightly less effective in activation than K+
phosphate
-
optimal concentration is 80-100 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0216
4'-deoxypyridoxine
0.00495
4'-O-methylpyridoxine
pH 6.2, 37°C
0.025 - 3.096
ATP
0.00495
ginkgotoxin
in 70 mM potassium phosphate buffer, pH 6.2
0.0028 - 3.839
pyridoxal
0.035 - 0.126
pyridoxamine
0.00987 - 0.02
pyridoxine
0.012 - 0.02
ATP
0.00122 - 0.49
pyridoxal
0.0062
pyridoxamine
-
-
0.00172 - 0.016
pyridoxine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.535 - 2.94
4'-deoxypyridoxine
0.46
4'-O-methylpyridoxine
pH 6.2, 37°C
0.47 - 1.12
ATP
0.46
ginkgotoxin
in 70 mM potassium phosphate buffer, pH 6.2
0.03 - 6.08
pyridoxal
0.3 - 0.79
pyridoxamine
0.1 - 6.08
pyridoxine
1.9
ATP
-
in the presence of Zn2+, at pH 6.5 and 37°C
0.12 - 3.2
pyridoxal
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 2.38
ATP
0.29 - 5.13
pyridoxal
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0574
4'-deoxypyridoxine
0.000414
4'-O-methylpyridoxine
pH 6.2, 37°C
0.228
enprofylline
in 20 mM sodium BES buffer, pH 7.2, at 37°C
0.000414 - 0.003
ginkgotoxin
0.056
lamotrigine
in 20 mM sodium BES buffer, pH 7.2, at 37°C
0.05
theophylline
in 20 mM sodium BES buffer, pH 7.2, at 37°C
0.0572
primaquine
-
at pH 7.0 and 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
Zn2+
Homo sapiens
-
at pH 6.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
purified enzyme, pH 6.1, 37°C
2.47
-
-
additional information
-
accurate and rapid assay method
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 6.3
-
7.3
assay at
5.5 - 6
-
-
8.8
-
enzyme from leukocytes
9.1
-
enzyme from erythrocytes
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
pH 5.0: about 70% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
40
-
Zn2+ as activating anion
50
-
Mg2+ as activating anion
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.75
calculated from the deduced amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the four PDXK human variants, D87H, V128I, H246Q, and A243Gf D87H, V128I, H246Q and A243G proteins show reduced catalytic activity and/or reduced affinity for PLP precursors. Although these variants are rare in population and carried in heterozygous condition, it is suggested that in certain metabolic contexts and diseases in which PLP levels are reduced, the presence of these PDXK variants might threaten genome integrity and increase cancer risk
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDXK_HUMAN
312
0
35102
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
x * 35000, SDS-PAGE
37000
-
SDS-PAGE
40000
-
gel filtration
65000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
homodimer
?
-
x * 35000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A243G
naturally occuring mutation from a patient with diabetes, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant A243G displays a damaging score of 0.72. The A243Q mutation somewhat reduces the affinity for ATP when using PL as substrate and the affinity for PM, while it does not affect KM for PL and PN. In addition, it has the effect to halve kcat with PL
D235A
active site residue
D235N
active site residue
D87H
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant D87H displays the highest damaging score (1.0). The D87H mutation strongly increases KM for PL, and to a lesser extent also increases KM for PN and PM, leaving KM for ATP and kcat almost unaltered
H246Q
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant H246Q displays a damaging score of 0.98. The H246Q mutation somewhat reduces the affinity for ATP when using PL as substrate and the affinity for PM, while it does not affect KM for PL and PN. In addition, it has the effect to halve kcat with PL
V128I
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant V128I isplays a damaging score of 0.99. The V128I mutation drastically increases KM for PL and KM for ATP with this vitamer, whereas it does not affect kcat
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 11
-
25°C, 3 h, stable. Gradual irreversible inactivation below pH 5.5
641425
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
stable at -20°C for approximately 21 days
25
-
pH 5.5-11, 3 h, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
3 M guanidine hydrochloride, enzyme loses more than 90% of the alpha-helix content
-
stable for 48 h when transduced into PC-12 cells
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, recombinant enzyme, stable for 21 days
-80°C, 20 mM phosphate buffer, pH 7.3, stable for at least some weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion adsorption chromatography (Ni2+)
Ni-NTA agarose column chromatography and HiLoad 26/60 Superdex 200 gel filtration
pyridoxyl-EAH-Sepharose 4B column chromatography
recombinant enzyme
TMAE column chromatography, Phenyl Sepharose column chromatography, and hydroxyapatite column chromatography
Ni-NTA agarose column chromatography
-
Ni-NTA column chromatography
-
Ni-NTA Sepharose column chromatography
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli HMS174(DE3)
expressed in Escherichia coli Rosetta (DE3)pLysS cells
expressed in Escherichia coli strain BL21 (DE3)
expressed in Escherichia coli strain BL21 (DE3) plysS
expression in Escherichia coli
gene PDXK, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta(lambdaDE3) pLysS
His-tag, expressed in Escherichia coli Rosetta (lambdaDE3)
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
recombinant enzyme is overexpressed in Escherichia coli as a fusion protein with maltose binding protein
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McCormick, D.B.; Gregory, M.E.; Snell, E.E.
Pyridoxal phosphokinases. I. Assay, distribution, purification, and properties
J. Biol. Chem.
236
2076-2084
1961
Bos taurus, Enterococcus faecalis, Homo sapiens, Lacticaseibacillus casei, Lactobacillus delbrueckii subsp. bulgaricus, Meleagris gallopavo, Mus musculus, Neurospora crassa, Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kerry, J.A.; Kwok, F.
Purification and characterization of pyridoxal kinase from human erythrocytes
Prep. Biochem.
16
199-216
1986
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chern, C.J.; Beutler, E.
Purification and characterization of human erythrocyte pyridoxine kinase
Clin. Chim. Acta
61
353-365
1975
Homo sapiens
Manually annotated by BRENDA team
Chern, C.J.; Beutler, E.
Assay for human erythrocyte pyridoxine kinase
Anal. Biochem.
67
97-109
1975
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
di Salvo, M.L.; Hunt, S.; Schirch, V.
Expression, purification, and kinetic constants for human and Escherichia coli pyridoxal kinases
Protein Expr. Purif.
36
300-306
2004
Escherichia coli, Homo sapiens (O00764), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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 (O00764), Homo sapiens
Manually annotated by BRENDA team
Flanagan, J.M.; Beutler, E.
The genetic basis of human erythrocyte pyridoxal kinase activity variation
Haematologica
91
801-804
2006
Homo sapiens
Manually annotated by BRENDA team
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
Ovis aries, Homo sapiens
Manually annotated by BRENDA team
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 (O00764), Homo sapiens
Manually annotated by BRENDA team
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 (O00764), Homo sapiens
Manually annotated by BRENDA team
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 (O00764), Homo sapiens
Manually annotated by BRENDA team
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 (O00764), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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), Trypanosoma cruzi (Q4D946), Plasmodium vivax Salvador I (A5K1Z8), Trypanosoma cruzi CL Brener (Q4D946)
Manually annotated by BRENDA team
Ramos, R.J.; Albersen, M.; Vringer, E.; Bosma, M.; Zwakenberg, S.; Zwartkruis, F.; Jans, J.J.M.; Verhoeven-Duif, N.M.
Discovery of pyridoxal reductase activity as part of human vitamin B6 metabolism
Biochim. Biophys. Acta
1863
1088-1097
2019
Homo sapiens (O00764), Homo sapiens
Manually annotated by BRENDA team
Mascolo, E.; Barile, A.; Mecarelli, L.S.; Amoroso, N.; Merigliano, C.; Massimi, A.; Saggio, I.; Hansen, T.; Tramonti, A.; Di Salvo, M.L.; Barbetti, F.; Contestabile, R.; Verni, F.
The expression of four pyridoxal kinase (PDXK) human variants in Drosophila impacts on genome integrity
Sci. Rep.
9
14188
2019
Homo sapiens (O00764), Homo sapiens, Drosophila melanogaster (Q7KUC2)
Manually annotated by BRENDA team