2.7.1.35: pyridoxal kinase
This is an abbreviated version!
For detailed information about pyridoxal kinase, go to the full flat file.
Word Map on EC 2.7.1.35
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2.7.1.35
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5'-phosphate
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vitamers
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pyridoxal-5'-phosphate
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plp-dependent
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4-pyridoxic
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ribokinase
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agriculture
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synthesis
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drug development
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medicine
- 2.7.1.35
- 5'-phosphate
-
vitamers
- pyridoxal-5'-phosphate
-
plp-dependent
-
4-pyridoxic
- ribokinase
- agriculture
- synthesis
- drug development
- medicine
Reaction
Synonyms
ePL kinase, ePL kinase 1, hPL kinase, HPLK, kinase (phosphorylating), pyridoxal, kinase, pyridoxal (phosphorylating), LdPdxK, PdxK, pdxY, PKH, PL kinase, PLK, Plk1, PM kinase, PN kinase, PN/PL/PM kinase, pyridoxal 5-phosphate-kinase, pyridoxal kinase, pyridoxal kinase 1, pyridoxal kinase PKL, pyridoxal kinase-like protein SOS4, pyridoxal phosphokinase, pyridoxal/pyridoxine kinase, pyridoxamine kinase, pyridoxine kinase, pyridoxine/pyridoxal/pyridoxamine kinase, salt overly sensitive4, SAV0580, Sos4, StPLK, vitamin B6 kinase
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Metals Ions
Metals Ions on EC 2.7.1.35 - pyridoxal kinase
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Ca2+
Co2+
Cu2+
Fe2+
K+
Li+
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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+
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Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Zn2+
additional information
Ca2+
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divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
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divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Cu2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Fe2+
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cations activate in decreaseing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
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+
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most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM
K+
affinity to pyridoxal and ATP is increased manifold in the presence of K+ compared to Na+, 2.5fold increase of activity
K+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
K+
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Km: 8.9 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Mg2+
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divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mg2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mg2+
required, Mg2+ ion can be located near the bound phosphate, it is coordinated with O3 of the ADP beta-phosphate and four water molecules
Mn2+
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divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mn2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Na+
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increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal
Na+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
Ni2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+ is the most effective cation for catalysis under saturating substrate concentrations
Zn2+
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cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
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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+
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divalent cation required, optimal concentration is 0.33 mM. Zn2+ is superior to Mg2+ below the optimum concentration of Zn2+
Zn2+
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activator at low concentrations (0.019 mM optimal concentration), most effective divalent cation for catalysis
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+
the presence of 100 mM NaCl does not alter the potassium activation profile
additional information
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the presence of 100 mM NaCl does not alter the potassium activation profile
additional information
Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
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Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
the enzyme requires a metal cofactor, very low activity with Li+, Na+, K+, Rb+ and Cs+. Cobalt gives more activity when compared to that of Zn2+, Ca2+, Cu2+ and Ni2+. Cu2+ shows the least enzyme activity. Order of metal ions with increasing effect on enzyme activity is as follows: Co2+, Zn2+, Mn2+, Mg2+, Fe2+, Ca2+, Ni2+, Cu2+
additional information
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the enzyme requires a metal cofactor, very low activity with Li+, Na+, K+, Rb+ and Cs+. Cobalt gives more activity when compared to that of Zn2+, Ca2+, Cu2+ and Ni2+. Cu2+ shows the least enzyme activity. Order of metal ions with increasing effect on enzyme activity is as follows: Co2+, Zn2+, Mn2+, Mg2+, Fe2+, Ca2+, Ni2+, Cu2+