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IUBMB Comments Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
The taxonomic range for the selected organisms is: Ovis aries The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxal kinase, pyridoxine kinase, pl kinase, ldpdxk, pyridoxal phosphokinase, stplk, pn kinase, hpl kinase, epl kinase 1, pn/pl/pm kinase,
more
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kinase (phosphorylating), pyridoxal
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kinase, pyridoxal (phosphorylating)
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pyridoxal 5-phosphate-kinase
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pyridoxal kinase-like protein SOS4
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pyridoxal phosphokinase
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pyridoxamine kinase
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pyridoxine kinase
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pyridoxine/pyridoxal/pyridoxamine kinase
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vitamin B6 kinase
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ATP + pyridoxal = ADP + pyridoxal 5'-phosphate
mechanism
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phospho group transfer
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ATP:pyridoxal 5'-phosphotransferase
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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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
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes
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ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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33% of the activity with pyridoxal
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ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
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ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
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40% of the activity with pyridoxal
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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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
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ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes
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K+
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Km: 8.9 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Rb+
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Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Zn2+
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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+
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(R)-roscovitine
binds to the pyridoxal binding site
3-hydroxyanthranilic acid
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IC50: 0.12 mM
3-hydroxykynurenine
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IC50: 0.1 mM
Mg2+
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excess free divalent cations inhibit the enzyme
Mn2+
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excess free divalent cations inhibit the enzyme
N-Dansyl-1,8-diaminooctane
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pyridoxaloxime
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strong competitive inhibitor
quinolinic acid
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IC50: 0.42 mM
xanthurenic acid
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IC50: 0.36 mM
Zn2+
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excess free divalent cations inhibit the enzyme
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NH4+
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Km: 3.7 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
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0.006
pyridoxamine
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pH 6.5
additional information
additional information
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effect of KCl on Km-values
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0.02
ATP
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pH 6.5
0.06
ATP
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ATP in form of ZnATP2-
0.101
ATP
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ATP in form of MgATP2-
0.194
ATP
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ATP in form of MnATP2-
0.026
pyridoxine
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pH 6.5
0.06
pyridoxine
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pH 5.8, 37°C, with MnATP2- as the second substrate
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0.0001
pyridoxal oxime
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pH 7, 25°C
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0.12
3-hydroxyanthranilic acid
Ovis aries
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IC50: 0.12 mM
0.1
3-hydroxykynurenine
Ovis aries
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IC50: 0.1 mM
0.42
quinolinic acid
Ovis aries
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IC50: 0.42 mM
0.36
xanthurenic acid
Ovis aries
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IC50: 0.36 mM
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additional information
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Uniprot
brenda
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brenda
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brenda
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brenda
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PDXK_SHEEP
312
0
34819
Swiss-Prot
other Location (Reliability: 2 )
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34861
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x * 34861, calculation from nucleotide sequence
40000
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2 * 40000, SDS-PAGE
60000
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gel filtration, equilibrium sedimentation
80000
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gel filtration, gradient PAGE
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?
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x * 34861, calculation from nucleotide sequence
monomer
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1 * 60000, SDS-PAGE
dimer
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2 * 40000, SDS-PAGE
dimer
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crystal structure analysis
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hanging drop vapor diffusion method, in complex with (R)-roscovitine and N6-methyl-(R)-roscovitine
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
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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
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hanging drop vapor diffusion method in complex with adenosine 5-(beta, gamma-methylenetriphosphate)-pyridoxamine, ADP-pyriodoxal 5-phosphate, and ADP
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impure enzyme is stabilized by Zn2+
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the enzyme is digested by chymotrypsin to proteolytic fragments of 24000 Da and 16000 Da
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-18°C, stable for 20 weeks
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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
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
Kerry, J.A.; Rohde, M.; Kwok, F.
Brain pyridoxal kinase. Purification and characterization
Eur. J. Biochem.
158
581-585
1986
Ovis aries
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
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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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
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
brenda