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ADP + NADH
AMP + NADPH
13% activity compared to ATP
-
-
?
ATP + 3-acetyl pyridineadenine dinucleotide
?
-
-
-
-
?
dATP + NADH
dADP + NADPH
103% activity compared to ATP
-
-
?
di-adenosine diphosphate
?
-
-
-
-
?
diphosphate + NAD+
phosphate + NADP+
-
10% of the activity with ATP
-
-
?
dITP + NAD+
dIDP + NADP+
-
141% activity compared to ATP
-
-
?
dTTP + NAD+
dTDP + NADP+
-
35% of the activity with ATP
-
-
?
fructose-1,6-bisphosphate + ?
?
-
-
-
?
GTP + NADH
GDP + NADPH
102% activity compared to ATP
-
-
?
hexametaphosphate + NAD+
? + NADP+
-
194% activity compared to ATP
-
-
?
hexametaphosphate + NAD+
NADP+ + ?
-
47% of the activity with ATP
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
hexapolyphosphate + NAD+
pentapolyphosphate + NADP+
metaphosphate + NAD+
? + NADP+
-
280% activity compared to ATP
-
-
?
NAD+ + poly(P)4
NADP+ + poly(P)3
-
-
-
-
?
NADH + ATP
NADPH + ADP
-
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
polyphosphate + NAD+
(phosphate)n-1 + NADP+
polyphosphate(20) + NAD+
polyphosphate(19) + NADP+
polyphosphate(25) + NAD+
polyphosphate(24) + NADP+
polyphosphate(45) + NAD+
polyphosphate(44) + NADP+
polyphosphate(65) + NAD+
polyphosphate(64) + NADP+
-
-
-
-
?
polyphosphate(75) + NAD+
polyphosphate(74) + NADP+
-
-
-
-
?
tetraphosphate + NAD+
triphosphate + NADP+
-
-
-
-
?
tetrapolyphosphate + NAD+
tripolyphosphate + NADP+
-
84% activity compared to ATP
-
-
?
triphosphate + NAD+
diphosphate + NADP+
-
-
-
-
?
TTP + NADH
TDP + NADPH
50% activity compared to ATP
-
-
?
additional information
?
-
ADP + NAD+
AMP + NADP+
-
-
-
-
?
ADP + NAD+
AMP + NADP+
-
-
-
-
?
ADP + NADP+
ATP + NAD+
-
-
-
?
ADP + NADP+
ATP + NAD+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
100% activity
-
-
?
ATP + NAD+
ADP + NADP+
-
UTP also may be used as phosphoryl donor
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
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+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
key enzyme for NADP+ metabolism and quinolinic acid metabolism
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
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+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
50% activity compared to NADH
-
-
?
ATP + NAD+
ADP + NADP+
50% activity compared to NADH
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
100% activity
-
-
?
ATP + NAD+
ADP + NADP+
synthesis of NADP+
-
-
?
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+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
Asp-45 is a key residue for the catalytic activity of NADK1
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
most effective phosphate donor
-
-
?
ATP + NAD+
ADP + NADP+
-
NAD kinase is responsible for the light-induced conversion of NAD to NADP in the chloroplast
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
75% of the activity with polyP27
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
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+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme exhibits very high affinity for NAD+ compared to adenosine triphosphate
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme exhibits very high affinity for NAD+ compared to adenosine triphosphate
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NAD+
ADP + NADP+
-
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
ATP + NADH
ADP + NADPH
100% activity
-
-
?
ATP + NADH
ADP + NADPH
100% activity
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
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
-
10% activity compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
ATP + NADH
ADP + NADPH
-
14% of the activity NAD+
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
ATP + NADH
ADP + NADPH
low activity
-
-
?
ATP + NADH
ADP + NADPH
low activity
-
-
?
ATP + NADH
ADP + NADPH
-
-
-
?
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+
-
-
-
?
CTP + NAD+
CDP + NADP+
-
-
-
?
CTP + NAD+
CDP + NADP+
-
60% of activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
60% of activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
56% activity compared to ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
102% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
-
-
-
?
CTP + NAD+
CDP + NADP+
76% of the activity with polyP27
-
-
?
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 + NAD+
CDP + NADP+
37% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
-
11% of the activity with ATP
-
-
?
CTP + NADH
CDP + NADPH
74% activity compared to 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+
-
77% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
-
42% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
-
42% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
-
99% activity compared to ATP
-
-
?
dATP + NAD+
dADP + NADP+
-
73% of the activity with 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+
-
-
?
dATP + NAD+
dADP + NADP+
58% of the activity with ATP
-
-
?
dCTP + NAD+
dCDP + NADP+
-
30% of the activity with ATP
-
-
?
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+
-
77% of the activity with ATP
-
-
?
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+
-
-
-
?
GTP + NAD+
GDP + NADP+
-
-
-
?
GTP + NAD+
GDP + NADP+
-
69% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
56% of activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
56% of activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
-
-
-
?
GTP + NAD+
GDP + NADP+
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
?
GTP + NAD+
GDP + NADP+
-
-
-
-
?
GTP + NAD+
GDP + NADP+
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
?
GTP + NAD+
GDP + NADP+
7% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
162% activity compared to ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
66% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
-
-
-
?
GTP + NAD+
GDP + NADP+
111% of the activity with polyP27
-
-
?
GTP + NAD+
GDP + NADP+
100% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
-
14% of the activity with ATP
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
-
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
-
?
hexapolyphosphate + NAD+
pentapolyphosphate + NADP+
-
-
-
-
?
hexapolyphosphate + NAD+
pentapolyphosphate + NADP+
-
-
-
-
?
ITP + NAD+
IDP + NADP+
-
-
-
?
ITP + NAD+
IDP + NADP+
-
104% activity compared to ATP
-
-
?
ITP + NAD+
IDP + NADP+
-
-
-
-
?
ITP + NAD+
IDP + NADP+
89% of the activity with polyP27
-
-
?
ITP + NAD+
IDP + NADP+
-
7% of the activity with ATP
-
-
?
NAD+ + ATP
NADP+ + ADP
-
-
-
-
?
NAD+ + ATP
NADP+ + ADP
-
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
-
-
-
?
polyphosphate + NAD+
(phosphate)n-1 + 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 + NAD+
?
-
50% of the activity with ATP
-
-
?
polyphosphate + NAD+
?
-
-
-
-
?
polyphosphate + NAD+
?
-
-
-
-
?
polyphosphate + NAD+
?
-
-
-
-
?
polyphosphate(20) + NAD+
polyphosphate(19) + NADP+
-
-
-
-
?
polyphosphate(20) + NAD+
polyphosphate(19) + NADP+
-
-
-
-
?
polyphosphate(25) + NAD+
polyphosphate(24) + NADP+
-
-
-
-
?
polyphosphate(25) + NAD+
polyphosphate(24) + NADP+
-
-
-
-
?
polyphosphate(45) + NAD+
polyphosphate(44) + NADP+
-
-
-
-
?
polyphosphate(45) + NAD+
polyphosphate(44) + NADP+
-
-
-
-
?
TTP + NAD+
TDP + NADP+
-
40% of maximal activity
-
-
?
TTP + NAD+
TDP + NADP+
-
87% activity compared to ATP
-
-
?
TTP + NAD+
TDP + NADP+
-
71% of the activity with ATP
-
-
?
TTP + NAD+
TDP + NADP+
13% of the activity with polyP27
-
-
?
TTP + NAD+
TDP + NADP+
19% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
-
-
?
UTP + NAD+
UDP + NADP+
-
109% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
109% 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 + NAD+
UDP + NADP+
-
isoenzyme 1: 12% of the activity with ATP. Isoenzyme 2: 19% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
41% activity compared to ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
114% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
-
-
-
?
UTP + NAD+
UDP + NADP+
94% of the activity with polyP27
-
-
?
UTP + NAD+
UDP + NADP+
48% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
-
5% of the activity with ATP
-
-
?
UTP + NADH
UDP + NADPH
69% activity compared to 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
?
-
no activity with poly(P)
-
-
?
additional information
?
-
no activity with poly(P)
-
-
?
additional information
?
-
no activity with poly(P)
-
-
?
additional information
?
-
no activity with poly(P)
-
-
?
additional information
?
-
-
no activity with poly(P)
-
-
?
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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CoCl2
31% of activity with MgCl2
CuCl2
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
Ni2+
6% activity at 5 mM compared to Mg2+
NiCl2
5 mM, substrate polyP27, 80% activity, substrate ATP, 36% activity
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+
43% activity at 5 mM compared to Mg2+
Ca2+
-
Ca2+/calmodulin-binding domain
Ca2+
half-maximal activity at free calcium of approximately 0.0004 mM
Ca2+
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
Ca2+
-
Ca2+/calmodulin-binding domain
Ca2+
-
Ca2+/calmodulin-binding domain
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
Ca2+
Sorghum sp.
-
Ca2+/calmodulin-binding domain
Ca2+
-
5 mM, 33% of the activation obtained with Mn2+
Ca2+
-
Ca2+/calmodulin-binding domain
CaCl2
5 mM, substrate polyP27, 57% activity, substrate ATP, 65% activity
CaCl2
46% of activity with MgCl2
Co2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Co2+
36% activity at 5 mM compared to Mg2+
Cu2+
2% activity at 5 mM compared to Mg2+
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+
Fe2+
83% activity at 5 mM compared to Mg2+
Mg2+
-
-
Mg2+
-
required to stabilize phosphoanhydride bonds to ATP
Mg2+
-
optimal concentration: 5 mM
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+
preferred cation, 100% activity at 5 mM
Mg2+
activity is strictly dependent on Mg2+. Maximal activity above 5 mM
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+
-
divalent cation required
Mg2+
-
maximal activation at a Mg2+:ATP ratio of 1:1
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+
15% activity at 5 mM compared to Mg2+
Mn2+
1 mM, 83% of the activation with 1 mM Zn2+
Mn2+
-
divalent cation required
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
Mn2+
-
maximal activity at 0.5 mM
MnCl2
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
MnCl2
329% of activity with MgCl2
Zn2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Zn2+
10% activity at 5 mM compared to Mg2+
Zn2+
1 mM, highest activation of divalent metal ions tested
ZnCl2
5 mM, substrate polyP27, 56% activity, substrate ATP, 78% activity
ZnCl2
231% of activity with MgCl2
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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(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'-AMP
-
2 mM, 25% inhibition
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-phenethylacetamide
2-(adenosine-8-thio)-N-[(3-indoyl)ethyl]acetamide
2-(adenosine-8-thio)-N-[(4-trifluoromethyl)phenethyl]acetamide
-
2-(adenosine-8-thio)-N-[(5-chloro-3-indoyl)ethyl]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
-
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
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
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-[(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-[3-(1-methylindolyl)ethyl]acetamide
3',5'-cAMP
-
3.5 mM, 20% inhibition
3'-AMP
-
2 mM, 20% inhibition
3-(bromoacetyl)pyridine
-
-
3-acetyl-pyridine adenine dinucleotide
1 mM, 30% inhibition
3-acetylpyridine-adenine-dinucleotide (oxidized form)
-
0.5 mM, 10% inhibition
3-aldehyde-pyridine adenine dinucleotide
1 mM, 32% inhibition
5'-AMP
-
2 mM, 15% inhibition
5'-thioacetyladenosine
-
-
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
adenosine diphosphoribose
-
3.5 mM, 31% inhibition
AMP
-
3.5 mM, 29% inhibition
CH3HgBr
-
0.1 mM, 63% inhibition
chlorpromazin
-
5 mM, 11% inhibition of the 410000 Da isoform, 80% inhibition of the 63000 Da isoform
citrate
-
3.5 mM, 55% inhibition
citrinin
-
phytotoxin from Guanomyces polythrix, 50% inhibition above 0.120 mM
deaminopyridinealdehyde adenine dinucleotide
-
0.5 mM, 10% inhibition
di-(5'-thioadenosine)
-
-
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
DTNB
-
0.1 mM, 74% inhibition
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
Hg(CH3COO)2
-
0.1 mM, complete inhibition
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%
NAD+
-
inhibits exchange reaction between ADP and ATP
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+
nicotinamide guanine dinucleotide
1 mM, 23% inhibition
nicotinamide hypoxanthine dinucleotide
1 mM, 24% inhibition
nicotinamide mononucleotide
-
2 mM, 15% inhibition
nicotinic acid adenine dinucleotide phosphate
1 mM, 37% inhibition
phosphoenolpyruvate
-
3.5 mM, 20% inhibition
pyruvate
-
3.5 mM, 10% inhibition
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-(3,4-dichlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(3-bromophenethyl)acetamide
-
-
2-(adenosine-8-thio)-N-(3-bromophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(3-chlorophenethyl)acetamide
-
-
2-(adenosine-8-thio)-N-(3-chlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(4-bromophenethyl)acetamide
-
-
2-(adenosine-8-thio)-N-(4-bromophenethyl)acetamide
-
2-(adenosine-8-thio)-N-(4-chlorophenethyl)acetamide
-
20% inhibition at 0.5 mM
2-(adenosine-8-thio)-N-(4-chlorophenethyl)acetamide
-
2-(adenosine-8-thio)-N-phenethylacetamide
-
10% inhibition at 0.4 mM
2-(adenosine-8-thio)-N-phenethylacetamide
-
2-(adenosine-8-thio)-N-[(3-indoyl)ethyl]acetamide
-
20% inhibition at 0.5 mM
2-(adenosine-8-thio)-N-[(3-indoyl)ethyl]acetamide
-
2-(adenosine-8-thio)-N-[(5-chloro-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-(3,4-dichlorophenethyl)acetamide
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
-
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
-
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
-
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-benzimidazolylethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-chloro-5-pyridyl)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-(2-naphthylethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)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-bromobenzyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)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-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-bromophenethyl)acetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-chlorophenethyl)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-phenethylacetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylpropanamide
-
-
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-propargylacetamide
-
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(3-indoyl)ethyl]acetamide
-
-
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
ADP
-
2 mM, 15% inhibition
ADP
-
inhibits NADP+ formation by NAD+ kinase
ADP
-
3 mM, 29% inhibition
ADP
-
3.5 mM, 63% inhibition
Ca2+
-
12% inhibition at 0.2 mM, 50% inhibition at 2 mM
Ca2+
-
ATP-dependent activity is reduced to 72% in the presence of 20 mM Ca2+
HgCl2
-
1 mM, 75% inhibition
HgCl2
-
0.25 mM, 65% inhibition
HgCl2
1 mM, 6% residual activity
NADH
-
0.1 mM, 20% inhibition
NADH
Corynebacterium glutamicum subsp. lactofermentum
-
-
NADH
-
0.01 mM, 61% inhibition
NADH
-
may become inhibitory at very high concentrations (mM)
NADH
-
40% residual activity at 0.5 mM
NADH
-
34% residual activity at 0.5 mM NADH
NADH
-
0.4 mM, 43% residual activity
NADH
-
allosterically inhibited
NADP+
-
0.1-0.2 mM, marked inhibition
NADP+
-
0.05 mM, 75% inhibition
NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
-
NADP+
-
0.1 mM, 21% inhibition
NADP+
-
58% residual activity at 0.5 mM NADP+
NADP+
-
0.3 mM, complete inhibition
NADP+
-
0.4 mM, 22% residual activity
NADP+
0.1 mM, 38% residual activity
NADPH
-
-
NADPH
Corynebacterium glutamicum subsp. lactofermentum
-
-
NADPH
-
0.01 mM, 76% inhibition
NADPH
-
66% residual activity at 0.5 mM
NADPH
-
17% residual activity at 0.5 mM NADPH
NADPH
-
0.3 mM, 18% inhibition
NADPH
-
0.4 mM, 50% residual activity
NADPH
-
allosterically inhibited
NADPH
0.1 mM, 67% residual activity
PCMB
-
0.01 mM, 79% inhibition, NAD+ and ATP protect from inactivation
PCMB
-
0.02 mM, 35% inhibition
PCMB
-
0.25 mM, 67% inhibition
PCMB
-
0.5 mM, 74% inhibition of isoenzyme 1, 23% inhibition of isoenzyme 2
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
Trifluoperazine
inhibits stimulation by calmodulin
additional information
-
no inhibition by 2-mercaptoethanol, isoenzyme 1 and 2
-
additional information
-
not inhibited by NADP+
-
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
-
additional information
not inhibitory: NADH
-
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4.3
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
0.43
fructose-1,6-bisphosphate
-
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
12
Tetrapolyphosphate
-
in 100 mM Tris-HCl (pH 8.0), at 37°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
-
0.032
ATP
-
isoenzyme 1
0.062
ATP
pH and temperature not specified in the publication
0.08
ATP
-
ATP in form of MgATP2-
0.16
ATP
-
pH 7.0, 37°C, mutant G183R
0.17
ATP
-
calmodulin-dependent isoform, pH 7.9, 25°C
0.17
ATP
-
ATP in form of MgATP2-
0.18
ATP
-
ATP in form of MgATP2-
0.2
ATP
-
pH 7.0, 37°C, mutant R175G
0.23
ATP
-
pH 7.0, 37°C, wild-type
0.23
ATP
-
pH 7.0, 37°C, wild-type
0.263
ATP
pH and temperature not specified in the publication
0.35
ATP
-
85°C, pH 8.5, 20 mM Mg2+
0.397
ATP
pH and temperature not specified in the publication
0.4
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
0.43
ATP
pH and temperature not specified in the publication
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
-
isoform NADK1, pH 7.9, 25°C
0.73
ATP
pH and temperature not specified in the publication
0.73
ATP
-
ATP in form of MgATP2-
0.74
ATP
-
isoform NADK2, pH 7.9, 25°C
0.74
ATP
pH and temperature not specified in the publication
0.74
ATP
-
ATP in form of MgATP2-
1.07
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
1.7
ATP
pH and temperature not specified in the publication
1.7
ATP
-
in 100 mM Tris-HCl (pH 8.0), at 37°C
1.74
ATP
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37°C
1.92
ATP
pH and temperature not specified in the publication
1.95
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
2
ATP
pH and temperature not specified in the publication
2.15
ATP
-
wild type enzyme, at pH 7.5 and 30°C
2.2
ATP
-
mutant S199A, 37°C, pH 8.0
2.2
ATP
-
mutant T195A, 37°C, pH 8.0
2.5
ATP
-
wild-type, 37°C, pH 8.0
2.7
ATP
-
mutant G208A, 37°C, pH 8.0
3.3
ATP
pH and temperature not specified in the publication
3.73
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30°C
4.5
ATP
-
enzyme immobilized on CNBr-activated Sepharose 4B
0.2
GTP
-
isoenzyme 2
0.2
GTP
-
GTP in form of MgGTP2-
0.022
NAD+
pH and temperature not specified in the publication
0.2
NAD+
-
calmodulin-dependent isoform, pH 7.9, 25°C
0.212
NAD+
pH and temperature not specified in the publication
0.22
NAD+
-
in 100 mM Tris-HCl (pH 8.0), at 37°C
0.26
NAD+
-
pH 7.0, 37°C, cosubstrate poly(P)4, wild-type
0.3
NAD+
cosubstrate polyP27, pH 6.8, 70°C
0.4
NAD+
cosubstrate ATP, pH 6.8, 70°C
0.43
NAD+
-
pH 7.9, 25°C
0.43
NAD+
-
isoform NADK2, pH 7.9, 25°C
0.43
NAD+
pH and temperature not specified in the publication
0.52
NAD+
-
pH 7.9, 25°C
0.52
NAD+
-
isoform NADK1, pH 7.9, 25°C
0.52
NAD+
pH and temperature not specified in the publication
0.53
NAD+
-
pH 7.0, 37°C, cosubstrate ATP, wild-type
0.54
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
0.68
NAD+
-
pH 9.0, 30°C
1
NAD+
pH and temperature not specified in the publication
1.07
NAD+
-
at pH 8.0 and 50°C
1.1
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30°C
1.2
NAD+
-
cosubstrate polyphosphate, wild-type, 37°C, pH 8.0
1.4
NAD+
-
cosubstrate polyphosphate, mutant T195A, 37°C, pH 8.0
1.4
NAD+
-
wild type enzyme, at pH 7.5 and 30°C
1.41
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30°C
1.43
NAD+
-
pH 7.0, 37°C, cosubstrate ATP, mutant G183R
1.5
NAD+
-
enzyme immobilized on CNBr-activated Sepharose 4B
1.59
NAD+
in 100 mM Tris-HCl (pH 7.5), at 37°C
1.85
NAD+
-
pH 7.0, 37°C, wild-type
1.86
NAD+
-
pH 7.0, 37°C, cosubstrate poly(P)4, mutant G183R
2
NAD+
-
pH 7.0, 37°C, mutant R175G
2.1
NAD+
-
cosubstrate polyphosphate, mutant S199A, 37°C, pH 8.0
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
2.5
NAD+
pH and temperature not specified in the publication
2.7
NAD+
-
cosubstrate ATP, mutant T195A, 37°C, pH 8.0
3
NAD+
-
85°C, pH 8.5, 20 mM Mg2+
3.3
NAD+
-
cosubstrate ATP, mutant S199A, 37°C, pH 8.0
3.3
NAD+
-
cosubstrate ATP, wild-type, 37°C, pH 8.0
3.8
NAD+
-
cosubstrate polyphosphate, mutant G208A, 37°C, pH 8.0
4.02
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30°C
6.5
NAD+
-
cosubstrate ATP, mutant G208A, 37°C, pH 8.0
0.042
NADH
pH and temperature not specified in the publication
0.05
NADH
in 100 mM Tris-HCl (pH 7.5), at 37°C
0.18
NADP+
-
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
0.21
poly(P)4
-
pH 7.0, 37°C, mutant G183R
0.33
poly(P)4
-
pH 7.0, 37°C, wild-type
2.2
Polyphosphate
-
mutant S199A, 37°C, pH 8.0
2.2
Polyphosphate
-
mutant T195A, 37°C, pH 8.0
2.5
Polyphosphate
-
wild-type, 37°C, pH 8.0
2.7
Polyphosphate
-
mutant G208A, 37°C, pH 8.0
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P117S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S/P117S
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
S57P
-
the variation is associated with the decreased enzyme activity
P117S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S/P117S
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
-
S57P
-
the variation is associated with the decreased enzyme activity
-
P117S
Corynebacterium glutamicum subsp. lactofermentum
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S
Corynebacterium glutamicum subsp. lactofermentum
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S/P117S
Corynebacterium glutamicum subsp. lactofermentum
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
S57P
Corynebacterium glutamicum subsp. lactofermentum
-
the variation is associated with the decreased enzyme activity
P117S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S/P117S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
-
S57P
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the variation is associated with the decreased enzyme activity
-
R175E
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175G
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175H
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175I
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175K
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175Q
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175T
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
D45N
-
only minor changes, its active site is similar to that of the wild-type enzyme with the ligand present in the same conformation. The asparagine adopts the same buried conformation as the aspartate but does not form any hydrogen bond with NAD. Mutation results in a 10fold decrease in activity
H223E
-
is twice less active than the wild-type on the biologically relevant substrate NAD. In contrast, its activity toward di-(5'-thioadenosine) is increased 2fold
G183R
-
decrease both in NAD+ kinase and NADH kinase activity
G190A
-
no enzymic activity
G198A
-
no enzymic activity
G207A
-
no enzymic activity
G208A
-
decrease in Vmax-value
L192A
-
no enzymic activity
P196A
-
no enzymic activity
S199A
-
decrease in Vmax-value
T195A
-
kinetic parameters similar to wild-type
T197A
-
no enzymic activity
T200A
-
no enzymic activity
Y202A
-
no enzymic activity
additional information
-
enzyme knockout mutant, growth inhibition and smaller rosette leaves than wild-type, with pale yellow colour. Mutant plant show a reduced chlorophyll content, and hypersensitivity to environmental stress such as UV-B, drought, heat shock and salinity
additional information
-
NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
-
NADK2-deficient mutant grows slowly, is sensitive to environmental stress, which leads to oxidative stress, and shows reduced chlorophyll content. NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK2-deficient mutant grows slowly, is sensitive to environmental stress, which leads to oxidative stress, and shows reduced chlorophyll content. NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK2-deficient mutant grows slowly, is sensitive to environmental stress, which leads to oxidative stress, and shows reduced chlorophyll content. NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
NADK2-deficient mutant grows slowly, is sensitive to environmental stress, which leads to oxidative stress, and shows reduced chlorophyll content. NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress
additional information
mutant for NadF is lethal
additional information
mutant for NadF is lethal
additional information
-
sensitivity of NADK(-) cells to oxidative stress is the same as that of the control cells
additional information
sensitivity of NADK(-) cells to oxidative stress is the same as that of the control cells
additional information
mutants of the NAD kinase gene are lethal
additional information
-
mutants of the NAD kinase gene are lethal
-
additional information
triple mutant utr1yef1pos5 is lethal
additional information
triple mutant utr1yef1pos5 is lethal
additional information
triple mutant utr1yef1pos5 is lethal
additional information
triple mutant utr1yef1pos5 is lethal
additional information
-
triple mutant utr1yef1pos5 is lethal
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds
additional information
-
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds. Mutant for POS5 shows several phenotypes related to decreased NADPH concentration in the mitochondria, and consequently, decreased mitochondrial function
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds. Mutant for POS5 shows several phenotypes related to decreased NADPH concentration in the mitochondria, and consequently, decreased mitochondrial function
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds. Mutant for POS5 shows several phenotypes related to decreased NADPH concentration in the mitochondria, and consequently, decreased mitochondrial function
additional information
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds. Mutant for POS5 shows several phenotypes related to decreased NADPH concentration in the mitochondria, and consequently, decreased mitochondrial function
additional information
-
triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds. Mutant for POS5 shows several phenotypes related to decreased NADPH concentration in the mitochondria, and consequently, decreased mitochondrial function
additional information
-
mutants of the NAD kinase gene are lethal
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Butler, J.R.; McGuinness, E.T.
Candida utilis NAD+ kinase: purification, properties and affinity gel studies
Int. J. Biochem.
14
839-844
1982
Cyberlindnera jadinii
brenda
Chung, A.E.
Nicotinamide adenine dinucleotide kinase from Azotobacter vinelandii. I. Purification and properties of the enzyme
J. Biol. Chem.
242
1182-1186
1967
Azotobacter vinelandii
brenda
Bulygina, E.R.; Telepneva, V.I.
Properties of pigeon heart nicotinamide adenine dinucleotide kinase
Biochem. Int.
4
135-141
1982
Columba sp.
-
brenda
Blomquist, C.H.
NAD+ kinase from sea urchin eggs
Methods Enzymol.
66
101-104
1980
Strongylocentrotus purpuratus
brenda
Blomquist, C.H.
Partial purification and characterization of nicotinamide adenine dinucleotide kinase from sea urchin eggs
J. Biol. Chem.
248
7044-7048
1973
Strongylocentrotus purpuratus
brenda
Ji, X.; Li, H.; Yuan, Z.; Liu, S.
Immobilization of NAD kinase
Ann. N. Y. Acad. Sci.
434
264-266
1984
Gallus gallus
brenda
Apps, D.K.
Pigeon-liver NAD kinase. The structural and kinetic basis of regulation of NADPH
Eur. J. Biochem.
55
475-483
1975
Columba sp.
brenda
Zerez, C.R.; Moul, D.E.; Andreoli, A.J.
NAD kinase from Bacillus licheniformis: inhibition by NADP and other properties
Arch. Microbiol.
144
313-316
1986
Bacillus licheniformis
brenda
Orringer, B.P.; Chung, A.E.
Nicotinamide adenine dinucleotide kinase from Azotobacter vinelandii cells. A possible mechanism for the enzyme reaction
Biochim. Biophys. Acta
250
86-91
1971
Azotobacter vinelandii
brenda
Tseng, Y.M.; Harris, B.G.; Jacobson, M.K.
Isolation and characterization of yeast nicotinamide adenine dinucleotide kinase
Biochim. Biophys. Acta
568
205-214
1979
Saccharomyces cerevisiae
brenda
Garavaglia, S.; Galizzi, A.; Rizzi, M.
Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid
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