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Information on EC 2.7.1.23 - NAD+ kinase
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2.7.1.23 NAD+ kinaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Synonyms
Afnk, AtNADK1, AtNADK2, AtNADK3, ATP: NAD(H) 2'-phosphotransferase, ATP:NAD 2'-phosphotransferase, ATP:NAD+ 2'-phosphotransferase, BsNADK, C5orf33, C5orf33 protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP: NAD(H) 2'-phosphotransferase
ATP:NAD 2'-phosphotransferase
-
-
-
-
DPN kinase
-
-
-
-
kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
-
kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
MJ0917
NAD kinase
NAD kinase 1
NAD(H) kinase
NADHK
NADK
NADK1
NADK2
nicotinamide adenine dinucleotide kinase
-
-
-
-
PH1074
Poly(P)/ATP NAD kinase
-
-
-
-
poly(P)/ATP-NAD kinase
poly(P)/ATPdependent NAD kinase
polyP/ATP-dependent NAD kinase
polyphosphate/ATP-NAD kinase
-
-
-
-
Ppnk
sll1415
Yef1p
YfjB
YjbN
NAD kinase
-
-
-
-
NAD kinase
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
NADK
-
-
-
-
poly(P)/ATPdependent NAD kinase
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
Ppnk
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + NAD+ = ADP + NADP+
isoenzyme 1: ping-pong mechanism. Isoenzyme 2: sequential mechanism
-
ATP + NAD+ = ADP + NADP+
AMP portion of ATP uses the same binding site as the nicotinamide ribose portion of NAD/NADP, proposal for phosphate transfer mechanism
ATP + NAD+ = ADP + NADP+
NAD+-binding mode and intersubunit contact
ATP + NAD+ = ADP + NADP+
isoenzyme 1: ping-pong mechanism. Isoenzyme 2: sequential mechanism
-
-
ATP + NAD+ = ADP + NADP+
NAD+-binding mode and intersubunit contact
-
-
ATP + NAD+ = ADP + NADP+
-
-
-
-
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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:NAD+ 2'-phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9032-66-0
-
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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
hexametaphosphate + NAD+
NADP+ + ?
-
47% of the activity with ATP
-
-
?
tetrapolyphosphate + NAD+
tripolyphosphate + NADP+
-
84% activity compared to ATP
-
-
?
ATP + NAD+
ADP + NADP+
-
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
-
-
?
ATP + NAD+
ADP + NADP+
-
the 410000 Da isoenzyme could be a housekeeping enzyme, the 63000 Da isoenzyme could be mainly involved in the adaption and response of Avena sativa to environmental signals or stress through changes of redox potential and/or calcium signalling pathways
-
-
?
ATP + NAD+
ADP + NADP+
-
key enzyme for NADP+ metabolism and quinolinic acid metabolism
-
-
?
ATP + NAD+
ADP + NADP+
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
-
the catalytic efficiency with ATP as phosphate donor for phosphorylation of NAD is higher than with polyphosphate. The enzyme prefers ATP over ADP and polyphosphate(20)
-
-
?
ATP + NAD+
ADP + NADP+
-
the catalytic efficiency with ATP as phosphate donor for phosphorylation of NAD is higher than with polyphosphate. The enzyme prefers ATP over ADP and polyphosphate(20)
-
-
?
ATP + NAD+
ADP + NADP+
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
50% activity compared to NADH
-
-
?
ATP + NAD+
ADP + NADP+
-
isoenzyme 1: most effective phosphate donor. Isoenzyme 2: 35% of the activity with GTP
-
-
?
ATP + NAD+
ADP + NADP+
-
treatment with AlCl3 of cell grown heterotrophically grown in darkness at pH 3.5 in the presence of lactate as sole carbon source, slows down the culture growth and suppresses the peak of NAD+ kinase activity, which characterizes the beginning of the exponential phase of growth of the control cultures, possible explanations
-
-
?
ATP + NAD+
ADP + NADP+
-
treatment with AlCl3 of cell grown heterotrophically grown in darkness at pH 3.5 in the presence of lactate as sole carbon source, slows down the culture growth and suppresses the peak of NAD+ kinase activity, which characterizes the beginning of the exponential phase of growth of the control cultures, possible explanations
-
-
?
ATP + NAD+
ADP + NADP+
-
isoenzyme 1: most effective phosphate donor. Isoenzyme 2: 35% of the activity with GTP
-
-
?
ATP + NAD+
ADP + NADP+
-
preferentially accepts NAD+ as substrate. At 100 micromol, NAD+ is 10fold faster phosphorylated than NADH
-
-
?
ATP + NAD+
ADP + NADP+
NAD+ kinase is the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme is required for the de novo synthesis of NADP+ from NAD+
-
-
?
ATP + NAD+
ADP + NADP+
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Asp-45 is a key residue for the catalytic activity of NADK1
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
-
the membranal Ca2+-calmodulin-dependent enzyme might be important for early growth metabolism. Except for drought-stressed Phaseolus vulgaris at the stage of radicle protrusion in which NAD+ kinase activities are not perturbed, in both Phaseolus vulgaris and Phaseolus acutifolius NAD+ kinase activities temporarily decrease in response to drought stress, these being restored after subsequent rehydration
-
-
?
ATP + NAD+
ADP + NADP+
-
the membranal Ca2+-calmodulin-dependent enzyme might be important for early growth metabolism. Except for drought-stressed Phaseolus vulgaris at the stage of radicle protrusion in which NAD+ kinase activities are not perturbed, in both Phaseolus vulgaris and Phaseolus acutifolius NAD+ kinase activities temporarily decrease in response to drought stress, these being restored after subsequent rehydration
-
-
?
ATP + NAD+
ADP + NADP+
-
NAD kinase is responsible for the light-induced conversion of NAD to NADP in the chloroplast
-
-
?
ATP + NAD+
ADP + NADP+
Utr1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm
-
-
?
ATP + NAD+
ADP + NADP+
Yef1 contributes very slightly to total NAD and NADH kinase activities in vivo
-
-
?
ATP + NAD+
ADP + NADP+
specific activity is 43fold higher than with NADH and ATP
-
-
?
ATP + NAD+
ADP + NADP+
specific activity is about 3fold higher than with NADH
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme exhibits very high affinity for NAD+ compared to adenosine triphosphate
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme exhibits very high affinity for NAD+ compared to adenosine triphosphate
-
-
?
ATP + NADH
ADP + NADPH
-
conversion is slow at a NADH concentration of 5 mM. At lower concentrations (50-150 micromol) and particularly when NAD+ is concomitantly present as substrate, NADH becomes farmore efficiently phosphorylated
-
-
?
ATP + NADH
ADP + NADPH
specific activity is 43fold lower than with NAD+ and ATP
-
-
?
ATP + NADH
ADP + NADPH
specific activity is about 3fold lower than with NAD+ and ATP
-
-
?
ATP + NADH
ADP + NADPH
higher activity with NADH than with NAD+
-
-
?
ATP + NADH
ADP + NADPH
low activity with NADH
-
-
?
ATP + NADH
ADP + NADPH
isoform Utr1p displays 15% activity with NADH compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
while isoform Yef1p displays 15% activity with NADH compared to NAD+
-
-
?
CTP + NAD+
CDP + NADP+
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isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
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isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
specific activity is 16.5fold lower than with NAD+ and ATP
-
-
?
CTP + NAD+
CDP + NADP+
specific activity is 7fold lower than with NAD+ and ATP
-
-
?
CTP + NADH
CDP + NADPH
74% activity compared to ATP
-
-
?
CTP + NADH
CDP + NADPH
specific activity is 13.2fold lower than with NADH and ATP
-
-
?
CTP + NADH
CDP + NADPH
specific activity is 2.4fold lower than with NADH and ATP
-
-
?
dATP + NAD+
dADP + NADP+
specific activity is 2.6fold lower than with ATP and NAD+
-
-
?
dATP + NAD+
dADP + NADP+
specific activity is similar to reaction with ATP and NAD+
-
-
?
dCTP + NAD+
dCDP + NADP+
specific activity is 11fold lower than with ATP and NAD+
-
-
?
dCTP + NAD+
dCDP + NADP+
specific activity is 3.3fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
specific activity is 11fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
specific activity is 13.2fold lower than with ATP and NAD+
-
-
?
GTP + NAD+
GDP + NADP+
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
?
GTP + NAD+
GDP + NADP+
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
-
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
-
?
hexapolyphosphate + NAD+
pentapolyphosphate + NADP+
-
-
-
-
?
polyphosphate + NAD+
(phosphate)n-1 + NADP+
activity with polyphosphates in decreasing order: polyP27, polyP32, polyP18, polyP46, polyP62, polyP5, no activity with orthophosphate or diphosphate
-
-
?
polyphosphate(20) + NAD+
polyphosphate(19) + NADP+
-
-
-
-
?
polyphosphate(25) + NAD+
polyphosphate(24) + NADP+
-
-
-
-
?
polyphosphate(45) + NAD+
polyphosphate(44) + NADP+
-
-
-
-
?
UTP + NAD+
UDP + NADP+
-
isoenzyme 1: 12% of the activity with ATP. Isoenzyme 2: 19% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
isoenzyme 1: 12% of the activity with ATP. Isoenzyme 2: 19% of the activity with ATP
-
-
?
UTP + NADH
UDP + NADPH
69% activity compared to ATP
-
-
?
additional information
?
-
-
NADP is not phosphorylated, tetrapolyphosphate or diphosphate are not used as phosphoryl donors
-
-
?
additional information
?
-
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
-
the enzyme also catalyzes an exchange reaction between ADP and ATP
-
-
?
additional information
?
-
the enzyme does not use AMP, CMP or inorganic polyphosphates (diphosphate, tripolyphosphate, trimetaphosphate, hexametaphosphate, metaphosphate, and polyphosphate) as the phosphoryl donor. Glucose 6-phosphate and phosphoenolpyruvate are also inert as phosphoryl donors
-
-
?
additional information
?
-
-
the enzyme does not use AMP, CMP or inorganic polyphosphates (diphosphate, tripolyphosphate, trimetaphosphate, hexametaphosphate, metaphosphate, and polyphosphate) as the phosphoryl donor. Glucose 6-phosphate and phosphoenolpyruvate are also inert as phosphoryl donors
-
-
?
additional information
?
-
the enzyme does not use AMP, CMP or inorganic polyphosphates (diphosphate, tripolyphosphate, trimetaphosphate, hexametaphosphate, metaphosphate, and polyphosphate) as the phosphoryl donor. Glucose 6-phosphate and phosphoenolpyruvate are also inert as phosphoryl donors
-
-
?
additional information
?
-
-
no activity with NAAD, ADP-ribose, adenosine, 5'-AMP, ADP, sphingosine, diacylglycerol, fructose 6-phosphate, trimetaphosphate, tripolyphosphate, phosphoenolpyruvate, and phosphocreatine
-
-
?
additional information
?
-
the NAD kinase from Listeria monocytogenes can promote amide formation between 5'-amino-5'-deoxyadenosine and carboxylic acid groups
-
-
?
additional information
?
-
-
the NAD kinase from Listeria monocytogenes can promote amide formation between 5'-amino-5'-deoxyadenosine and carboxylic acid groups
-
-
?
additional information
?
-
-
the enzyme also shows phosphatase activity
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
-
absence of any NADH-phosphorylating (NADH kinase) activity of NAD kinase
-
-
?
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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 + NAD+
ADP + NADP+
-
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
-
-
?
ATP + NAD+
ADP + NADP+
-
the 410000 Da isoenzyme could be a housekeeping enzyme, the 63000 Da isoenzyme could be mainly involved in the adaption and response of Avena sativa to environmental signals or stress through changes of redox potential and/or calcium signalling pathways
-
-
?
ATP + NAD+
ADP + NADP+
-
key enzyme for NADP+ metabolism and quinolinic acid metabolism
-
-
?
ATP + NAD+
ADP + NADP+
-
treatment with AlCl3 of cell grown heterotrophically grown in darkness at pH 3.5 in the presence of lactate as sole carbon source, slows down the culture growth and suppresses the peak of NAD+ kinase activity, which characterizes the beginning of the exponential phase of growth of the control cultures, possible explanations
-
-
?
ATP + NAD+
ADP + NADP+
-
treatment with AlCl3 of cell grown heterotrophically grown in darkness at pH 3.5 in the presence of lactate as sole carbon source, slows down the culture growth and suppresses the peak of NAD+ kinase activity, which characterizes the beginning of the exponential phase of growth of the control cultures, possible explanations
-
-
?
ATP + NAD+
ADP + NADP+
NAD+ kinase is the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme is required for the de novo synthesis of NADP+ from NAD+
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
-
the membranal Ca2+-calmodulin-dependent enzyme might be important for early growth metabolism. Except for drought-stressed Phaseolus vulgaris at the stage of radicle protrusion in which NAD+ kinase activities are not perturbed, in both Phaseolus vulgaris and Phaseolus acutifolius NAD+ kinase activities temporarily decrease in response to drought stress, these being restored after subsequent rehydration
-
-
?
ATP + NAD+
ADP + NADP+
-
the membranal Ca2+-calmodulin-dependent enzyme might be important for early growth metabolism. Except for drought-stressed Phaseolus vulgaris at the stage of radicle protrusion in which NAD+ kinase activities are not perturbed, in both Phaseolus vulgaris and Phaseolus acutifolius NAD+ kinase activities temporarily decrease in response to drought stress, these being restored after subsequent rehydration
-
-
?
ATP + NAD+
ADP + NADP+
-
NAD kinase is responsible for the light-induced conversion of NAD to NADP in the chloroplast
-
-
?
ATP + NAD+
ADP + NADP+
Utr1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm
-
-
?
ATP + NAD+
ADP + NADP+
Yef1 contributes very slightly to total NAD and NADH kinase activities in vivo
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3R)-5-hydroxy-6,8,10-trimethoxy-2,3-dimethyl-2,3-dihydro-4H-naphtho-(2,3-b)-pyran-4-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.0243 mM
(2S,3R)-5-hydroxy-6,8-dimethoxy-2,3-dimethyl-2,3-dihydro-4H-naphtho-(2,3-b)-pyran-4-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.0422 mM
(2S,3S)-5-hydroxy-6,8,10-trimethoxy-2,3-dimethyl-4H-2,3-dihydronaphtho-(2,3-b)-pyran-4-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.022 mM
(2S,3S)-5-hydroxy-6,8-dimethoxy-2,3-dimethyl-4H-2,3-dihydronaphtho-(2,3-b)-pyran-4-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.0401 mM
2-(adenosine-8-thio)-N-[(4-trifluoromethyl)phenethyl]acetamide
-
2-(adenosine-8-thio)-N-[(5-methoxy-3-indoyl)ethyl]acetamide
-
2-([6-amino-9-[(2R,3R,4S,5R)-5-(aminomethyl)-3,4-dihydroxytetrahydrofuran-2-yl]-9H-purin-8-yl]sulfanyl)-N-[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl]acetamide
-
3-acetylpyridine-adenine-dinucleotide (oxidized form)
-
0.5 mM, 10% inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
0.5 mM, 62% inhibition of isoenzyme 1 and 33% inhibition of isoenzyme 2
5-hydroxy-6,8-dimethoxy-2,3-dimethyl-4H-naphtho-(2,3-b)-pyran-4-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.0171 mM
chlorpromazin
-
5 mM, 11% inhibition of the 410000 Da isoform, 80% inhibition of the 63000 Da isoform
diphosphate
-
5 mM, 46% inhibition of the 410000 Da isoform, 69% inhibition of the 63000 Da isoform
dithiothreitol
-
0.1 mM, 81% inhibition, irreversible for isoenzyme 1 and reversible for isoenzyme 2
EGTA
-
5 mM, 20% inhibition of the 410000 Da isoform, 85% inhibition of the 63000 Da isoform
ergosta-4,6,8(14),22-tetraen-3-one
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.090 mM
iodoacetic acid
-
1 mM, 56% inhibition of the 63000 Da isoform, no inhibition of the 410000 Da isoform
KCl
-
200 mM KCl decreases the polyphosphate-dependent activity to 75%
NaCl
-
200 mM NaCl decreases the polyphosphate-dependent activity to 75%
NEM
-
1 mM, 92% inhibition of the 63000 Da isoform, 34% inhibition of the 410000 Da isoform
Ni2+
-
ATP-dependent activity is reduced to 60% or 7% in the presence of 5 or 20 mM Ni2+
R24571
-
1 mM, 46% inhibition of the 410000 Da isoform, 89% inhibition of the 63000 da isoform
rubrofusarin B
-
phytotoxin from Guanomyces polythrix, 50% inhibition at 0.0133 mM
shRNA
-
shRNA1-NADK exhibits a notably higher efficiency compared with a shRNA2-NADK construct. About 70% decrease of both NADK expression, activity, and the NADPH concentration, accompanied by increased sensitivity toward H2O2
-
2-(adenosine-8-thio)-N-(3,4-dichlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(3-bromophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(3-chlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(4-bromophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(4-chlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-[(3-indoyl)ethyl]acetamide
-
2-(adenosine-8-thio)-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-benzimidazolylethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-chloro-5-pyridyl)acetamide
10% inhibition at 0.3 mM
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-naphthylethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromobenzyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-chlorophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-ethynylphenethyl)acetamide
-
40% inhibition at 0.25 mM
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-ethynylphenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
-
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-chlorophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylacetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylpropanamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-propargylacetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(3-indoyl)ethyl]acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
-
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
-
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
-
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
-
ADP
-
5 mM, 4% inhibition of the 410000 Da isoform, 25% inhibition of the 63000 Da isoform
Ca2+
-
ATP-dependent activity is reduced to 72% in the presence of 20 mM Ca2+
PCMB
-
0.01 mM, 79% inhibition, NAD+ and ATP protect from inactivation
Trifluoperazine
-
calmodulin-dependent isoform, 50% inhibition at 0.057 mM, isoforms NADK1, NADK2, no effect
Trifluoperazine
-
2 mM, 8% inhibition of the 410000 da isoform, 83% inhibition of the 63000 Da isoform
additional information
-
no inhibition by 2-mercaptoethanol, isoenzyme 1 and 2
-
additional information
utr1 shows slow growth in a low-iron medium
-
additional information
utr1 shows slow growth in a low-iron medium
-
additional information
utr1 shows slow growth in a low-iron medium
-
additional information
utr1 shows slow growth in a low-iron medium
-
additional information
-
utr1 shows slow growth in a low-iron medium
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
upregulates NADK1 by 3fold after treatment of plant cells with 5 mM
Calmodulin
-
calmodulin-dependent isoform, full activation in presence of Ca2+
Calmodulin
-
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
Calmodulin
-
a 410000 Da Ca2+-calmodulin-independent isoform and a 63000 Da Ca2+-calmodulin-dependent isoform
Calmodulin
calmodulin-dependent enzyme is stimulated 3.5fold by addition of calmodulin in presence of Ca2+
Calmodulin
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
Calmodulin
-
in dry seeds the membranal-Ca2+-calmodulin-dependent form represents 30% of the total pelletable activity
Calmodulin
-
five forms of NAD+ kinase: 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
Calmodulin
-
five forms of NAD+ kinase: 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
Calmodulin
-
CaM-2 isoform is a significantly more efficient activator of NAD kinase compared with the CaM-4 and CaM-6 isoforma
Calmodulin
-
Ca2+-calmodulin-dependent enzyme. Half-saturating concentration of calmodulin is 19 ng
Calmodulin
-
the enzyme can be activated by soybean CaM-1, but not by the divergent soybean CaM isoform CaM-4
Calmodulin
-
presence of bovine calmodulin, 100% activity, Nicotiana tabacum calmodulin 1, 207% activity, Nicotiana tabacum calmodulin 3, 235% activity, Nicotiana tabacum calmodulin 1, 9% activity
Calmodulin
-
two peaks of calmodulin-dependent NAD+ kinase activity occur at times when the cells are not actively dividing: the first one, a few hours after medium inoculation and the second one, at the end of the exponential growth phase
additional information
-
irradiation upregulates NADK1 by 8fold. NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
-
additional information
irradiation upregulates NADK1 by 8fold. NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
-
additional information
irradiation upregulates NADK1 by 8fold. NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
-
additional information
irradiation upregulates NADK1 by 8fold. NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
-
additional information
-
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin, although recombinant NADK2, which has a calmodulin-binding motif in its N-terminal, is able to bind to calmodulin
-
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin, although recombinant NADK2, which has a calmodulin-binding motif in its N-terminal, is able to bind to calmodulin
-
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin, although recombinant NADK2, which has a calmodulin-binding motif in its N-terminal, is able to bind to calmodulin
-
additional information
NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin, although recombinant NADK2, which has a calmodulin-binding motif in its N-terminal, is able to bind to 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
-
overexpression of NADK results in an almost 200fold increase of both the mRNA level, the protein amount and the catalytic activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
NADK is activated by oncogenic signaling to sustain pancreatic ductal adenocarcinoma.
Endometrial Neoplasms
Distinct clinical and genetic mutation characteristics in sporadic and Lynch syndrome-associated endometrial cancer in a Chinese population.
Hyperlysinemias
Clinical heterogeneity of mitochondrial NAD kinase deficiency caused by a NADK2 start loss variant.
Hyperlysinemias
Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes dienoyl-CoA reductase deficiency with hyperlysinemia.
Hypersensitivity
NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection.
Hypersensitivity
NADK3, a novel cytoplasmic source of NADPH, is required under conditions of oxidative stress and modulates abscisic acid responses in Arabidopsis.
nad+ kinase deficiency
Clinical heterogeneity of mitochondrial NAD kinase deficiency caused by a NADK2 start loss variant.
Neoplasms
Enhanced degradation of dihydrofolate reductase through inhibition of NAD kinase by nicotinamide analogs.
Neoplasms
Extramedullary relapse of multiple myeloma defined as the highest risk group based on deregulated gene expression data.
Nervous System Malformations
Lysine Restriction and Pyridoxal Phosphate Administration in a NADK2 Patient.
Staphylococcal Infections
From Substrate to Fragments to Inhibitor Active In Vivo against Staphylococcus aureus.
Tuberculosis
A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis.
Tuberculosis
Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis.
Tuberculosis
Crystallization and preliminary X-ray analysis of NAD kinase from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Crystallographic studies of Mycobacterium tuberculosis polyphosphate/ATP-NAD kinase complexed with NAD.
Tuberculosis
Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase.
Tuberculosis
First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization.
Tuberculosis
Inorganic Polyphosphate/ATP-NAD kinase of Micrococcus flavus and Mycobacterium tuberculosis H37Rv.
Tuberculosis
NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex.
Tuberculosis
Overexpression, purification, and characterization of ATP-NAD kinase of Sphingomonas sp. A1.
Tuberculosis
Probing binding requirements of NAD kinase with modified substrate (NAD) analogues.
Tuberculosis
Selective inhibition of nicotinamide adenine dinucleotide kinases by dinucleoside disulfide mimics of nicotinamide adenine dinucleotide analogues.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
5.9
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
17.2
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
14.1
polyphosphate(45)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
18.4
polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
3.1
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
2.1
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
2.4
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
additional information
additional information
-
allosteric enzyme, Hill coefficient for ATP 1.5, for polyphosphate 1.4
-
0.062
ATP
pH and temperature not specified in the publication
0.263
ATP
pH and temperature not specified in the publication
0.397
ATP
pH and temperature not specified in the publication
0.4
ATP
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
0.49
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.64
ATP
wild-type enzyme, pH and temperature not specified in the publication
0.66
ATP
recombinant enzyme, pH and temperature not specified in the publication
0.73
ATP
pH and temperature not specified in the publication
0.74
ATP
pH and temperature not specified in the publication
1.07
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
1.74
ATP
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
1.95
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
3.73
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
0.212
NAD+
pH and temperature not specified in the publication
0.43
NAD+
pH and temperature not specified in the publication
0.52
NAD+
pH and temperature not specified in the publication
0.54
NAD+
pH and temperature not specified in the publication
0.67
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
1.1
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
1.41
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
2.11
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
2.39
NAD+
pH and temperature not specified in the publication
4.02
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
0.042
NADH
pH and temperature not specified in the publication
0.99
NADP+
recombinant enzyme, pH and temperature not specified in the publication
1.01
NADP+
wild-type enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
7.8
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
7.3
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
3.4
polyphosphate(45), polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
1.8
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
8.7
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
3
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
additional information
additional information
-
the molecular activity is 360 per min, the activity per active centre is less than 60 per min, pH 7.4, 30°C
-
0.6
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
2.02
ATP
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
2.54
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
2.68
ATP
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
20.51
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
29.2
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.5
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
3.8
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
7.8
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
15.42
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
27.1
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
1.3
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.42
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.24
polyphosphate(45)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
0.19
polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
0.58
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
-
4.1
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
1.2
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.56
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
1.16
ATP
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
1.3
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
5.5
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
6.72
ATP
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
59.6
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.36
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
0.94
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
7.05
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
7.32
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
40.5
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
2-(adenosine-8-thio)-N-(4-chlorophenethyl)acetamide
pH 7.4, 30°C
0.14
2-(adenosine-8-thio)-N-phenethylacetamide
pH 7.4, 30°C
0.002
2-(adenosine-8-thio)-N-[(3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.01
2-(adenosine-8-thio)-N-[(4-trifluoromethyl)phenethyl]acetamide
pH 7.4, 30°C
0.04
2-(adenosine-8-thio)-N-[(5-methoxy-3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.025
2-([6-amino-9-[(2R,3R,4S,5R)-5-(aminomethyl)-3,4-dihydroxytetrahydrofuran-2-yl]-9H-purin-8-yl]sulfanyl)-N-[[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl]acetamide
in 50 mM Tris-HCl, pH 7.4, 10 mM MgCl2, at 30°C
0.22
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-chloro-5-pyridyl)acetamide
-
pH 7.4, 30°C
0.006
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-ethynylphenethyl)acetamide
pH 7.4, 30°C
0.0065 - 0.3
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
0.0075 - 0.23
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
0.0003 - 0.065
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
0.005 - 0.16
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
0.0004 - 0.35
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
0.022
2-(adenosine-8-thio)-N-(3,4-dichlorophenethyl)acetamide
pH 7.4, 30°C
0.002
2-(adenosine-8-thio)-N-(3-bromophenethyl)acetamide
pH 7.4, 30°C
0.03
2-(adenosine-8-thio)-N-(3-chlorophenethyl)acetamide
pH 7.4, 30°C
0.03
2-(adenosine-8-thio)-N-(4-bromophenethyl)acetamide
pH 7.4, 30°C
0.00025
2-(adenosine-8-thio)-N-[(5-chloro-3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.775
2-(adenosine-8-thio)-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.002
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
pH 7.4, 30°C
0.13
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
pH 7.4, 30°C
0.05
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
pH 7.4, 30°C
0.08
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
-
pH 7.4, 30°C
0.055
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
pH 7.4, 30°C
0.13
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.023
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-benzimidazolylethyl)acetamide
pH 7.4, 30°C
0.525
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-benzimidazolylethyl)acetamide
-
pH 7.4, 30°C
0.005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-naphthylethyl)acetamide
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-naphthylethyl)acetamide
-
pH 7.4, 30°C
0.0001
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
pH 7.4, 30°C
0.025
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromobenzyl)acetamide
pH 7.4, 30°C
0.055
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromobenzyl)acetamide
-
pH 7.4, 30°C
0.001
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)acetamide
pH 7.4, 30°C
0.33
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.00075
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-chlorophenethyl)acetamide
pH 7.4, 30°C
0.02
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-chlorophenethyl)acetamide
-
pH 7.4, 30°C
0.0065
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
pH 7.4, 30°C
0.3
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
-
pH 7.4, 30°C
0.0005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
pH 7.4, 30°C
0.08
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.0005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-chlorophenethyl)acetamide
pH 7.4, 30°C
0.21
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-chlorophenethyl)acetamide
-
pH 7.4, 30°C
0.005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylacetamide
pH 7.4, 30°C
0.35
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylacetamide
-
pH 7.4, 30°C
0.055
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylpropanamide
pH 7.4, 30°C
0.15
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylpropanamide
-
pH 7.4, 30°C
0.03
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-propargylacetamide
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-propargylacetamide
-
pH 7.4, 30°C
0.0005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.0075
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
pH 7.4, 30°C
0.23
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
-
pH 7.4, 30°C
0.0003
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.065
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.005
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
pH 7.4, 30°C
0.16
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.0004
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
pH 7.4, 30°C
0.35
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
-
pH 7.4, 30°C
0.11
NADH
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.34
NADP+
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C