2.7.1.23: NAD+ kinase
This is an abbreviated version!
For detailed information about NAD+ kinase, go to the full flat file.
Reaction
Synonyms
Afnk, AtNADK1, AtNADK2, AtNADK3, ATP: NAD(H) 2'-phosphotransferase, ATP:NAD 2'-phosphotransferase, ATP:NAD+ 2'-phosphotransferase, BsNADK, C5orf33, C5orf33 protein, diphosphopyridine nucleotide kinase, diphosphppyridine kinase, DPN kinase, EC 2.7.1.23, GmNADK1, GmNADK2, GmNADK3, GmNADK4, GmNADK5, HsNADK, kinase (phosphorylating), nicotinamide adenine dinucleotide, kinase, nicotinamide adenine dinucleotide (phosphorylating), MJ0917, NAD kinase, NAD kinase 1, NAD kinase 2, NAD kinase2, NAD(H) kinase, NadF, NADHK, NADK, NADK1, NADK2, NADK3, NADP phosphatase/NAD kinase, native plant calcium- and calmodulin-dependent NAD+-kinase, nicotinamide adenine dinucleotide kinase, OsNADK1, PH1074, Poly(P)/ATP NAD kinase
ECTree
2.7.1.23 NAD+ kinaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 2.7.1.23 - NAD+ kinase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
CaCl2
Co2+
Cu2+
CuCl2
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
Fe2+
Mg2+
MgCl2
Mn2+
MnCl2
NiCl2
5 mM, substrate polyP27, 80% activity, substrate ATP, 36% activity
Zn2+
ZnCl2
additional information
Ca2+
-
a 410000 Da Ca2+-calmodulin-independent isoform and a 63000 Da Ca2+-calmodulin-dependent isoform
Ca2+
-
the Ca2+-calmodulin-dependent NAD+ kinase isoforms, amongst which is the isoform bound to mitochondrial membranes play an important role at the end of sensu stricto germination and during the following growth of Avena sativa
Ca2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+. Most effective are Mn2+, Mg2+ and Ca2+. Maximal activity with Ca2+ at 9.0 mM
Ca2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Ca2+
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
Ca2+
-
five forms of NAD+ kianse: 1. a solvent Ca2+ sensitive form, 2. and 3. two Ca2+-calmodulin independent forms, one solvent and one membranal, 4. and 5. two Ca2+-calmodulin dependent forms, one solvent and one membranal.In dry seeds the membranal-Ca2+-calmodulin-dependent form represents 100% of the total pelletable activity
Ca2+
-
five forms of NAD+ kianse: 1. a solvent Ca2+ sensitive form, 2. and 3. two Ca2+-calmodulin independent forms, one solvent and one membranal, 4. and 5. two Ca2+-calmodulin dependent forms, one solvent and one membranal.In dry seeds the membranal-Ca2+-calmodulin-dependent form represents 100% of the total pelletable activity
Ca2+
-
Ca2+-calmodulin-dependent enzyme. Half-saturating concentration of Ca2+ is 0.07 mM
Ca2+
-
optimal Ca2+ concentration is 0.0001 mM for enzyme activated by type II calmodulin, 0.001-0.005 mM for enzyme activated by type I calmodulin. Activation is highest at pH 6.8-7.1. No activation by type III calmodulin
CaCl2
5 mM, substrate polyP27, 57% activity, substrate ATP, 65% activity
Co2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Cu2+
POS5 is upregulated 3.4fold after treatment for 10 to 12 min with 2.5 mM
Fe2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Mg2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+. Most effective are Mn2+, Mg2+ and Ca2+. Maximal activity with Mg2+ at 7.5 mM
Mg2+
-
enzyme activity is enhanced by Mg2+. The highest activity for ATP is reached with 20 mM Mg2+ (2.6fold higher than with ATP, but without addition of bivalent cations)
Mg2+
optimal concentration is 10 mM. At 1 mM, 29% of the activation with 1 mM Zn2+
Mg2+
-
activity is dependent on Mg2+, maximal activity at 50 mM
Mg2+
-
Mg2+ at 1 mM gives 60% of the maximum activity obtained with Mn2+
MgCl2
5 mM, substrate polyP27, 100% activity, substrate ATP, 100% activity
Mn2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+. Most effective are Mn2+, Mg2+ and Ca2+. Maximal activity with Mn2+ at 6.0 mM
Mn2+
-
enzyme activity is enhanced by Mn2+. When using polyphosphate, the enzyme requires bivalent cations, preferably manganese ions, for activity. With polyphosphate, the enzyme is most active in the presence of 15 mM Mn2+ (60% activity compared to ATP with 20 mM Mg2+). 20 mM Mn2+ increases ATP-dependent activity 1.9fold
Mn2+
-
at pH 6.5, with 2.0 mM NAD+ and 1.0 mM ATP maximal activity is observed with Mn2+ at 0.5 to 1.0 mM
MnCl2
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
Zn2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
ZnCl2
5 mM, substrate polyP27, 56% activity, substrate ATP, 78% activity
additional information
-
NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
-
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
-
NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
-
addition of NaCl or KCl does not alter ATP-dependent activity
additional information
-
enzyme activity is independent of bivalent cations when using ATP
additional information
no activity is detected in presence of Li+, Na+, and K+
additional information
-
no activity is detected in presence of Li+, Na+, and K+
