Information on EC 2.7.1.23 - NAD+ kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria

EC NUMBER
COMMENTARY
2.7.1.23
-
RECOMMENDED NAME
GeneOntology No.
NAD+ kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + NAD+ = ADP + NADP+
show the reaction diagram
sequential mechanism
-
ATP + NAD+ = ADP + NADP+
show the reaction diagram
isoenzyme 1: ping-pong mechanism. Isoenzyme 2: sequential mechanism
-
ATP + NAD+ = ADP + NADP+
show the reaction diagram
sequential addition of substrates
-
ATP + NAD+ = ADP + NADP+
show the reaction diagram
NAD+-binding mode and intersubunit contact
-
ATP + NAD+ = ADP + NADP+
show the reaction diagram
AMP portion of ATP uses the same binding site as the nicotinamide ribose portion of NAD/NADP, proposal for phosphate transfer mechanism
-, O30297
ATP + NAD+ = ADP + NADP+
show the reaction diagram
isoenzyme 1: ping-pong mechanism. Isoenzyme 2: sequential mechanism
Euglena gracilis Z
-
-
ATP + NAD+ = ADP + NADP+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
NAD phosphorylation and dephosphorylation I
-
NAD phosphorylation and dephosphorylation II
-
NAD/NADH phosphorylation and dephosphorylation
-
NAD/NADP-NADH/NADPH cytosolic interconversion (yeast)
-
NAD/NADP-NADH/NADPH mitochondrial interconversion (yeast)
-
Nicotinate and nicotinamide metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP: NAD(H) 2'-phosphotransferase
-
-
ATP: NAD(H) 2'-phosphotransferase
F7EXV6
-
ATP:NAD 2'-phosphotransferase
-
-
-
-
ATP:NAD+ 2'-phosphotransferase
-
-
C5orf33 protein
-
-
diphosphopyridine nucleotide kinase
-
-
diphosphppyridine kinase
-
-
DPN kinase
-
-
-
-
EC 2.7.1.23
-
related
kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
-
kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
NAD kinase
-
-
-
-
NAD kinase
Corynebacterium glutamicum ATCC13869
-
-
-
NAD kinase
Corynebacterium glutamicum subsp. lactofermentum
-
-
NAD kinase
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
NAD kinase
-
-
NAD kinase
Escherichia coli MG1655
-
-
-
NAD kinase
-
-
NAD kinase
Q8Y8D7
-
NAD kinase
-
-
NAD kinase
F7EXV6
-
NAD kinase
P32622
-
NAD kinase
-
-
NAD kinase 1
-
-
NAD kinase2
-
-
NAD(H) kinase
C4LSN1
-
NAD(H) kinase
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
-
-
NadF
O31612
-
NADHK
C4LSN1
-
NADHK
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
-
-
NADK
-
-
-
-
NADK
-
-
NADK
F7EXV6
-
NADK
Q6L7J5
-
NADK1
-
calcium-calmodulin nonbinding isoform of plant NAD+ kinase
NADK1
-
isoform
NADK1
Q56YN3
-
NADK2
-
calcium- and calmodulin-binding isoform of plant NAD+ kinase
NADK2
Q9C5W3
-
NADK3
Q500Y9
-
NADP phosphatase/NAD kinase
-
-
native plant calcium- and calmodulin-dependent NAD+-kinase
-
-
nicotinamide adenine dinucleotide kinase
-
-
-
-
Poly(P)/ATP NAD kinase
-
-
-
-
poly(P)/ATP-NAD kinase
P0A5S6
-
poly(P)/ATPdependent NAD kinase
-
-
poly(P)/ATPdependent NAD kinase
Corynebacterium glutamicum ATCC13869
-
-
-
poly(P)/ATPdependent NAD kinase
Corynebacterium glutamicum subsp. lactofermentum
-
-
poly(P)/ATPdependent NAD kinase
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
polyP/ATP-dependent NAD kinase
-
-
polyP/ATP-dependent NAD kinase
-
-
-
polyphosphate/ATP-NAD kinase
-
-
-
-
Ppnk
Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum ATCC13869
-
-
-
Ppnk
Corynebacterium glutamicum subsp. lactofermentum
-
-
Ppnk
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
PPNK_THEMA
Q9X255
-
sll1415
-
gene name
slr0040
-
gene name
YEF1
P32622
low specific activity cytosolic NAD kinase
Yef1p
C7GKE4, P32622
-
YfjB
-
gene name
YfjB
P0A7B3
-
YfjB
Escherichia coli MG1655
-
gene name
-
YjbN
O31612
-
YtdI
O34934
-
CAS REGISTRY NUMBER
COMMENTARY
9032-66-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achromobacter aceris
-
-
-
Manually annotated by BRENDA team
; isoforms NADK1, NADK2 plus a calmodulin-dependent isoform isolated from seedling; known to be present in other plants
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
isoform NADK2
-
-
Manually annotated by BRENDA team
subsp. lactofermentum
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum ATCC13869
subsp. lactofermentum
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum subsp. lactofermentum
-
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
Manually annotated by BRENDA team
Entamoeba histolytica HM1: IMSS cl 6
-
UniProt
Manually annotated by BRENDA team
Escherichia coli MG1655
-
-
-
Manually annotated by BRENDA team
Escherichia coli MG1655
MG1655
-
-
Manually annotated by BRENDA team
isoenzyme 1 and 2; strain Z
-
-
Manually annotated by BRENDA team
Euglena gracilis Z
strain Z
-
-
Manually annotated by BRENDA team
Merr. Cv. Maple Arrow
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
recombinant enzyme
Swissprot
Manually annotated by BRENDA team
L. cv. Akabana-tsurunashi-endo
-
-
Manually annotated by BRENDA team
enzyme also shows NAD+ kinase activity
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
Swissprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the reduction of the NADP(H) level in the sll1415 mutant leads to a significant accumulation of glucose-6-phosphate and a loss of photoheterotrophic growth
metabolism
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
NAD kinase is the key enzyme for the de novo biosynthesis of NADP+ and NADPH
metabolism
Corynebacterium glutamicum ATCC13869, Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
NAD kinase is the key enzyme for the de novo biosynthesis of NADP+ and NADPH
-
physiological function
Q500Y9, Q56YN3, Q9C5W3
chloroplast NAD kinase 2 has an important role in chlorophyll biosynthesis and protects chloroplasts from oxidative stress
physiological function
-
the enzyme regulates the size of the NADPH pool and insulin secretion in pancreatic beta-cells. Enzyme overexpression also protects beta-cells against oxidative damage by the redox cycling agent menadione and reverses menadione-mediated inhibition of glucose-stimulated insulin secretion
physiological function
F7EXV6
the enzyme regulates the size of the NADPH pool and insulin secretion in pancreatic beta-cells. Enzyme overexpression also protects beta-cells against oxidative damage by the redox cycling agent menadione and reverses menadione-mediated inhibition of glucose-stimulated insulin secretion
physiological function
C4LSN1, -
enzyme overexpression represses the production of intracellular reactive oxygen specie upon H2O2 exposure by 40%
physiological function
-
the NAD kinase gene sll1415 inhibits the transcription of genes involved in redox homeostasis and exerts stronger effects on methyl viologen tolerance than NAD kinase gene slr0040
physiological function
Entamoeba histolytica HM1: IMSS cl 6
-
enzyme overexpression represses the production of intracellular reactive oxygen specie upon H2O2 exposure by 40%
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + NADH
AMP + NADPH
show the reaction diagram
C4LSN1, -
13% activity compared to ATP
-
-
?
ATP + 3-acetyl pyridineadenine dinucleotide
?
show the reaction diagram
-
-
-
-
-
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
-, ?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
-
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-, O95544
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q6L7J5
-
-
-
-
ATP + NAD+
ADP + NADP+
show the reaction diagram
-, Q500Y9, Q56YN3, Q9C5W3
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q9X255, -
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
C7GKE4, Q06892
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q58327
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
O31612, O34934
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
P0A7B3
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q6L7J5
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q8VUL9
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
F7EXV6
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-, Q8Y8D7
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
100% activity
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-, Q500Y9, Q56YN3, Q9C5W3
100% activity
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
isoenzyme 1: most effective phosphate donor. Isoenzyme 2: 35% of the activity with GTP
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
most effective phosphate donor, NAD kinase is responsible for the light-induced conversion of NAD to NADP in the chloroplast
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-, O95544
synthesis of NADP+
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
key enzyme for NADP+ metabolism and quinolinic acid metabolism
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
UTP also may be used as phosphoryl donor
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
O58801, -
75% of the activity with polyP27
-
-
-
ATP + NAD+
ADP + NADP+
show the reaction diagram
P21373, P32622
Utr1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
P21373, P32622
Yef1 contributes very slightly to total NAD and NADH kinase activities in vivo
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 43fold higher than with NADH and ATP
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
P21373, P32622
specific activity is about 3fold higher than with NADH
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
Asp-45 is a key residue for the catalytic activity of NADK1
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
preferentially accepts NAD+ as substrate. At 100 micromol, NAD+ is 10fold faster phosphorylated than NADH
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
C4LSN1, -
50% activity compared to NADH
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
Corynebacterium glutamicum subsp. lactofermentum JHI3-156, Corynebacterium glutamicum ATCC13869
-
ATP is the preferred phosphoryl donor and NAD+ is the preferred acceptor
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
50% activity compared to NADH
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Euglena gracilis Z
-
-, 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+
show the reaction diagram
Euglena gracilis Z
-
isoenzyme 1: most effective phosphate donor. Isoenzyme 2: 35% of the activity with GTP
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Euglena gracilis Z
-
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
Escherichia coli MG1655
-
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
O58801, -
-
-
-
-
ATP + NADH
ADP + NADPH
show the reaction diagram
-
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
Q500Y9, Q56YN3, Q9C5W3
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
Q58327
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
-
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
Q8VUL9
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
-
low activity
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
C4LSN1, -
100% activity
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
-
14% of the activity NAD+
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
P21373, P32622
specific activity is 43fold lower than with NAD+ and ATP
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
P21373, P32622
specific activity is about 3fold lower than with NAD+ and ATP
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
-
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
show the reaction diagram
C7GKE4, Q06892
higher activity with NADH than with NAD+
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
C7GKE4, Q06892
low activity with NADH
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
C7GKE4, Q06892
isoform Utr1p displays 15% activity with NADH compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
C7GKE4, Q06892
while isoform Yef1p displays 15% activity with NADH compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
100% activity
-
-
?
ATP + NADH
ADP + NADH2
show the reaction diagram
-
10% activity compared to NAD+
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
-
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
Q6L7J5
37% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
60% of activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
11% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
O58801, -
76% of the activity with polyP27
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
102% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 16.5fold lower than with NAD+ and ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 7fold lower than with NAD+ and ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
56% activity compared to ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
Euglena gracilis Z
-
isoenzyme 1: 55% of the activity with ATP. Isoenzyme 2: 77% of the activity with ATP
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
Escherichia coli MG1655
-
60% of activity with ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
P21373, P32622
specific activity is 13.2fold lower than with NADH and ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
P21373, P32622
specific activity is 2.4fold lower than with NADH and ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
C4LSN1, -
74% activity compared to ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
74% activity compared to ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
73% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
42% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
77% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
Q6L7J5
58% of the activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 2.6fold lower than with ATP and NAD+
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
P21373, P32622
specific activity is similar to reaction with ATP and NAD+
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
99% activity compared to ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
Escherichia coli MG1655
-
42% of the activity with ATP
-
-
?
dATP + NADH
dADP + NADPH
show the reaction diagram
C4LSN1, -
103% activity compared to ATP
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
-
30% of the activity with ATP
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 11fold lower than with ATP and NAD+
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 3.3fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
-
77% of the activity with ATP
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 11fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
P21373, P32622
specific activity is 13.2fold lower than with ATP and NAD+
-
-
?
di-adenosine diphosphate
?
show the reaction diagram
-
-
-
-
?
diphosphate + NAD+
phosphate + NADP+
show the reaction diagram
-
10% of the activity with ATP
-
-
?
dITP + NAD+
dIDP + NADP+
show the reaction diagram
-
141% activity compared to ATP
-
-
?
dTTP + NAD+
dTDP + NADP+
show the reaction diagram
-
35% of the activity with ATP
-
-
?
fructose-1,6-bisphosphate + ?
?
show the reaction diagram
Q58327
-
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
-
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
Q6L7J5
100% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
14% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-, O95544
7% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
-
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
69% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
56% of activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
O58801, -
111% of the activity with polyP27
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
66% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
162% activity compared to ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
Euglena gracilis Z
-
isoenzyme 1: 96% of the activity with ATP. Isoenzyme 2: most effective phosphoryl donor
-
-
-
GTP + NAD+
GDP + NADP+
show the reaction diagram
Escherichia coli MG1655
-
56% of activity with ATP
-
-
?
GTP + NADH
GDP + NADPH
show the reaction diagram
C4LSN1, -
102% activity compared to ATP
-
-
?
hexametaphosphate + NAD+
NADP+ + ?
show the reaction diagram
-
47% of the activity with ATP
-
-
?
hexametaphosphate + NAD+
? + NADP+
show the reaction diagram
-
194% activity compared to ATP
-
-
?
hexaphosphate + NAD+
pentaphosphate + NADP+
show the reaction diagram
Corynebacterium glutamicum subsp. lactofermentum, Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
-
-
-
?
hexapolyphosphate + NAD+
pentapolyphosphate + NADP+
show the reaction diagram
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC13869
-
-
-
-
?
ITP + NAD+
IDP + NADP+
show the reaction diagram
-
-
-
-
?
ITP + NAD+
IDP + NADP+
show the reaction diagram
-
-
-
?
ITP + NAD+
IDP + NADP+
show the reaction diagram
-
7% of the activity with ATP
-
-
?
ITP + NAD+
IDP + NADP+
show the reaction diagram
O58801, -
89% of the activity with polyP27
-
-
-
ITP + NAD+
IDP + NADP+
show the reaction diagram
-
104% activity compared to ATP
-
-
?
NAD+ + ATP
NADP+ + ADP
show the reaction diagram
-
-
-
-
?
NAD+ + ATP
NADP+ + ADP
show the reaction diagram
-
-
-
-
?
NAD+ + poly(P)4
NADP+ + poly(P)3
show the reaction diagram
-
-
-
-
?
NADH + ATP
NADPH + ADP
show the reaction diagram
-
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
-
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
Q58327
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
-
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
O31612, O34934
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
Q8VUL9
-
-
-
?
polyphosphate + NAD+
?
show the reaction diagram
-
-
-
-
?
polyphosphate + NAD+
?
show the reaction diagram
-
-
-
-
?
polyphosphate + NAD+
?
show the reaction diagram
-
50% of the activity with ATP
-
-
?
polyphosphate + NAD+
(phosphate)n-1 + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate + NAD+
(phosphate)n-1 + NADP+
show the reaction diagram
O58801, -
activity with polyphosphates in decreasing order: polyP27, polyP32, polyP18, polyP46, polyP62, polyP5, no activity with orthophosphate or diphosphate
-
-
?
polyphosphate(20) + NAD+
polyphosphate(19) + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate(25) + NAD+
polyphosphate(24) + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate(45) + NAD+
polyphosphate(44) + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate(65) + NAD+
polyphosphate(64) + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate(75) + NAD+
polyphosphate(74) + NADP+
show the reaction diagram
-
-
-
-
?
tetraphosphate + NAD+
triphosphate + NADP+
show the reaction diagram
-
-
-
-
?
tetrapolyphosphate + NAD+
tripolyphosphate + NADP+
show the reaction diagram
-
84% activity compared to ATP
-
-
?
triphosphate + NAD+
diphosphate + NADP+
show the reaction diagram
-
-
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
Q6L7J5
19% of the activity with ATP
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
-
40% of maximal activity
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
O58801, -
13% of the activity with polyP27
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
-
71% of the activity with ATP
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
-
87% activity compared to ATP
-
-
?
TTP + NADH
TDP + NADPH
show the reaction diagram
C4LSN1, -
50% activity compared to ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
-
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
5% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
109% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
isoenzyme 1: 12% of the activity with ATP. Isoenzyme 2: 19% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
Q6L7J5
48% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
O58801, -
94% of the activity with polyP27
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
114% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
41% activity compared to ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
Euglena gracilis Z
-
isoenzyme 1: 12% of the activity with ATP. Isoenzyme 2: 19% of the activity with ATP
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
Escherichia coli MG1655
-
109% of the activity with ATP
-
-
?
UTP + NADH
UDP + NADPH
show the reaction diagram
C4LSN1, -
69% activity compared to ATP
-
-
?
UTP + NADH
UDP + NADPH
show the reaction diagram
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
69% activity compared to ATP
-
-
?
metaphosphate + NAD+
? + NADP+
show the reaction diagram
-
280% activity compared to ATP
-
-
?
additional information
?
-
-
the enzyme also catalyzes an exchange reaction between ADP and ATP
-
-
-
additional information
?
-
-
NADP is not phosphorylated, tetrapolyphosphate or diphosphate are not used as phosphoryl donors
-
-
-
additional information
?
-
-
the enzyme also shows phosphatase activity
-
-
-
additional information
?
-
-
absence of any NADH-phosphorylating (NADH kinase) activity of NAD kinase
-
-
-
additional information
?
-
C7GKE4, Q06892
no activity with poly(P)
-
-
-
additional information
?
-
-, Q500Y9, Q56YN3, Q9C5W3
does not accept poly(P) as phosphoryl donor
-
-
-
additional information
?
-
C7GKE4, Q06892
does not accept poly(P) as phosphoryl donor
-
-
-
additional information
?
-
-
no activity with NAAD, ADP-ribose, adenosine, 5'-AMP, ADP, sphingosine, diacylglycerol, fructose 6-phosphate, trimetaphosphate, tripolyphosphate, phosphoenolpyruvate, and phosphocreatine
-
-
-
additional information
?
-
C4LSN1, -
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
?
-
-, Q8Y8D7
the NAD kinase from Listeria monocytogenes can promote amide formation between 5'-amino-5'-deoxyadenosine and carboxylic acid groups
-
-
-
additional information
?
-
Entamoeba histolytica HM1: IMSS cl 6
C4LSN1
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
show the reaction diagram
Q9X255, -
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
NAD kinase is responsible for the light-induced conversion of NAD to NADP in the chloroplast
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-, O95544
synthesis of NADP+
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
-
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+
show the reaction diagram
-
key enzyme for NADP+ metabolism and quinolinic acid metabolism
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
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+
show the reaction diagram
P21373, P32622
Utr1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
P21373, P32622
Yef1 contributes very slightly to total NAD and NADH kinase activities in vivo
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Euglena gracilis Z
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
5 mM, 33% of the activation obtained with Mn2+
Ca2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+; 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+
-
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+
-
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+
-
Ca2+-calmodulin-dependent enzyme. Half-saturating concentration of Ca2+ is 0.07 mM
Ca2+
-
half-maximal activity at free calcium of approximately 0.0004 mM
Ca2+
-
a 410000 Da Ca2+-calmodulin-independent isoform and a 63000 Da Ca2+-calmodulin-dependent isoform
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+
-
Ca2+/calmodulin-binding domain
Ca2+
-
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
Ca2+
-
Ca2+/calmodulin-binding domain
Ca2+
C4LSN1, -
43% activity at 5 mM compared to Mg2+
CaCl2
-
5 mM, substrate polyP27, 57% activity, substrate ATP, 65% activity
CaCl2
Q6L7J5
46% of activity with MgCl2
Co2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Co2+
C4LSN1, -
36% activity at 5 mM compared to Mg2+
CoCl2
Q6L7J5
31% of activity with MgCl2
Cu2+
C7GKE4, Q06892
POS5 is upregulated 3.4fold after treatment for 10 to 12 min with 2.5 mM
Cu2+
C4LSN1, -
2% activity at 5 mM compared to Mg2+
CuCl2
-
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
Fe2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Fe2+
C4LSN1, -
83% activity at 5 mM compared to Mg2+
Mg2+
-
optimal concentration: 5 mM
Mg2+
-
divalent cation required; Mg2+ at 1 mM gives 60% of the maximum activity obtained with Mn2+
Mg2+
-
divalent cation required; maximal activation at a Mg2+:ATP ratio of 1:1
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+
-
optimal concentration is 10 mM. At 1 mM, 29% of the activation with 1 mM Zn2+
Mg2+
-
activity is strictly dependent on Mg2+. Maximal activity above 5 mM
Mg2+
-
; required to stabilize phosphoanhydride bonds to ATP
Mg2+
-, O30297
-
Mg2+
-
activity is dependent on Mg2+, maximal activity at 50 mM
Mg2+
-
-
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+
C4LSN1, -
preferred cation, 100% activity at 5 mM
MgCl2
-
5 mM, substrate polyP27, 100% activity, substrate ATP, 100% activity
MgCl2
Q6L7J5
-
Mn2+
-
divalent cation required; maximal activity at 0.5 mM
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; divalent cation required
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+
-
1 mM, 83% of the activation with 1 mM Zn2+
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+
C4LSN1, -
15% activity at 5 mM compared to Mg2+
MnCl2
-
5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity
Ni2+
C4LSN1, -
6% activity at 5 mM compared to Mg2+
NiCl2
-
5 mM, substrate polyP27, 80% activity, substrate ATP, 36% activity
Zn2+
-
several divalent cations satisfy the metal ion requirement: Mg2+, Mn2+, Ca2+, Fe2+, Zn2+ and Co2+
Zn2+
-
1 mM, highest activation of divalent metal ions tested
Zn2+
C4LSN1, -
10% activity at 5 mM compared to Mg2+
ZnCl2
-
5 mM, substrate polyP27, 56% activity, substrate ATP, 78% activity
ZnCl2
Q6L7J5
231% of activity with MgCl2
MnCl2
Q6L7J5
329% of activity with MgCl2
additional information
Q500Y9, Q56YN3, Q9C5W3
NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin; NADK2 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin; NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
additional information
-
addition of NaCl or KCl does not alter ATP-dependent activity; enzyme activity is independent of bivalent cations when using ATP
additional information
C4LSN1, -
no activity is detected in presence of Li+, Na+, and K+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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'-AMP
-
2 mM, 25% inhibition
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
-, Q8Y8D7
-
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
ADP
-
2 mM, 15% inhibition
ADP
-
3.5 mM, 63% inhibition
ADP
-
inhibits NADP+ formation by NAD+ kinase
ADP
-
5 mM, 4% inhibition of the 410000 Da isoform, 25% inhibition of the 63000 Da isoform
ADP
-
3 mM, 29% inhibition
AMP
-
3.5 mM, 29% 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+
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
HgCl2
-
1 mM, 75% inhibition
HgCl2
-
0.25 mM, 65% inhibition
HgCl2
Q6L7J5
1 mM, 6% residual activity
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
NADH
-
0.1 mM, 20% inhibition
NADH
-
0.01 mM, 61% inhibition
NADH
-
0.4 mM, 43% residual activity
NADH
-
allosterically inhibited
NADH
-
may become inhibitory at very high concentrations (mM)
NADH
Corynebacterium glutamicum subsp. lactofermentum
-
-
NADH
-
40% residual activity at 0.5 mM
NADH
-
34% residual activity at 0.5 mM NADH
NADP+
-
0.1-0.2 mM, marked inhibition
NADP+
-
0.05 mM, 75% inhibition
NADP+
-
0.1 mM, 21% inhibition
NADP+
-
0.4 mM, 22% residual activity
NADP+
Q6L7J5
0.1 mM, 38% residual activity
NADP+
-
0.3 mM, complete inhibition
NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
-
NADP+
-
58% residual activity at 0.5 mM NADP+
NADPH
-
0.01 mM, 76% inhibition
NADPH
-
0.4 mM, 50% residual activity
NADPH
Q6L7J5
0.1 mM, 67% residual activity
NADPH
-
0.3 mM, 18% inhibition
NADPH
-
allosterically inhibited
NADPH
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
-
NADPH
-
66% residual activity at 0.5 mM
NADPH
-
17% residual activity at 0.5 mM NADPH
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
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
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
-
Trifluoperazine
-
-
Trifluoperazine
-
inhibits stimulation by calmodulin
Trifluoperazine
-
2 mM, 8% inhibition of the 410000 da isoform, 83% inhibition of the 63000 Da isoform
Trifluoperazine
-
; calmodulin-dependent isoform, 50% inhibition at 0.057 mM, isoforms NADK1, NADK2, no effect
additional information
-
no inhibition by 2-mercaptoethanol, isoenzyme 1 and 2
-
additional information
Q6L7J5
not inhibitory: NADH
-
additional information
C7GKE4, Q06892
utr1 shows slow growth in a low-iron medium
-
additional information
-
not inhibited by NADP+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5'-AMP
-
1.56fold activation at 3.0 mM
adenine
-
5 mM, activity of both isoenzymes is modestly enhanced
AMP
-
5 mM, activity of both isoenzymes is modestly enhanced
Caffeine
-
5 mM, activity of both isoenzymes is modestly enhanced
Calmodulin
-
CaM-2 isoform is a significantly more efficient activator of NAD kinase compared with the CaM-4 and CaM-6 isoforma
Calmodulin
-
independent on calmodulin
Calmodulin
-
the enzyme can be activated by soybean CaM-1, but not by the divergent soybean CaM isoform CaM-4
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; 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
-
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
-
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
Calmodulin
-
Ca2+-calmodulin-dependent enzyme. Half-saturating concentration of calmodulin is 19 ng
Calmodulin
-
calmodulin-dependent enzyme is stimulated 3.5fold by addition of calmodulin in presence of Ca2+
Calmodulin
-
a 410000 Da Ca2+-calmodulin-independent isoform and a 63000 Da Ca2+-calmodulin-dependent isoform
Calmodulin
-
; calmodulin-dependent isoform, full activation in presence of Ca2+
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
-
activates
Calmodulin
-
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
D-ribose 5-phosphate
-
5 mM, activity of both isoenzymes is modestly enhanced
H2O2
Q500Y9, Q56YN3, Q9C5W3
upregulates NADK1 by 3fold after treatment of plant cells with 5 mM
nicotinic acid
-
5 mM, activity of both isoenzymes is modestly enhanced
Pyridine
-
5 mM, activity of both isoenzymes is modestly enhanced
Quinolinic acid
-
allosteric activator
imidazole
-
5 mM, activity of both isoenzymes is modestly enhanced
additional information
Q500Y9, Q56YN3, Q9C5W3
irradiation upregulates NADK1 by 8fold. NADK1 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin; 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; NADK3 is Ca2+/calmodulin-independent, and not activated by Ca2+/calmodulin
-
additional information
Q8VUL9
is not regulated by NADH
-
additional information
-
overexpression of NADK results in an almost 200fold increase of both the mRNA level, the protein amount and the catalytic activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.3
-
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.032
-
ATP
-
isoenzyme 1
0.16
-
ATP
-
pH 7.0, 37C, mutant G183R
0.17
-
ATP
-
calmodulin-dependent isoform, pH 7.9, 25C
0.17
-
ATP
-
30C, pH 8.0
0.2
-
ATP
-
pH 7.0, 37C, mutant R175G
0.23
-
ATP
-
pH 7.0, 37C, wild-type
0.23
-
ATP
-
pH 7.0, 37C, wild-type
0.24
-
ATP
-
pH 8
0.35
-
ATP
-
85C, pH 8.5, 20 mM Mg2+
0.4
-
ATP
C4LSN1, -
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
0.49
-
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.73
-
ATP
-
isoform NADK1, pH 7.9, 25C
0.74
-
ATP
-
isoform NADK2, pH 7.9, 25C
0.9
-
ATP
-
-
1.07
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
1.7
-
ATP
-
in 100 mM Tris-HCl (pH 8.0), at 37C
1.74
-
ATP
C4LSN1, -
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
1.92
-
ATP
Q6L7J5
30C, pH 8.0
1.95
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
2.1
-
ATP
-
mutant D45N
2.15
-
ATP
-
wild type enzyme, at pH 7.5 and 30C
2.2
-
ATP
-
mutant S199A, 37C, pH 8.0; mutant T195A, 37C, pH 8.0
2.3
-
ATP
-
pH 9.0, 30C
2.5
-
ATP
-
native enzyme
2.5
-
ATP
-
pH 7.0, 37C
2.5
-
ATP
-
wild-type, 37C, pH 8.0
2.7
-
ATP
-
mutant G208A, 37C, pH 8.0
2.8
-
ATP
-
wild-type
3.3
-
ATP
-
30C
3.73
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
4.5
-
ATP
-
enzyme immobilized on CNBr-activated Sepharose 4B
0.59
-
CTP
-
pH 8
0.43
-
fructose-1,6-bisphosphate
Q58327
-
2.86
-
GTP
-
pH 8
1.54
-
ITP
-
pH 8
0.08
-
MgATP2-
-
pH 7.5, 30C
0.17
-
MgATP2-
-
pH 7.9, 25C
0.18
-
MgATP2-
-
pH 8
0.73
-
MgATP2-
-
pH 7.9, 25C
0.74
-
MgATP2-
-
pH 7.9, 25C
0.11
-
NAD+
-
pH 8
0.2
-
NAD+
-
pH 7.5, 30C
0.2
-
NAD+
-
calmodulin-dependent isoform, pH 7.9, 25C; pH 7.9, 25C
0.22
-
NAD+
-
in 100 mM Tris-HCl (pH 8.0), at 37C
0.26
-
NAD+
-
isoenzyme 1
0.26
-
NAD+
-
pH 7.0, 37C, cosubstrate poly(P)4, wild-type
0.3
-
NAD+
-
cosubstrate polyP27, pH 6.8, 70C
0.4
-
NAD+
-
cosubstrate ATP, pH 6.8, 70C
0.43
-
NAD+
-
isoform NADK2, pH 7.9, 25C; pH 7.9, 25C
0.43
-
NAD+
Q6L7J5
30C, pH 8.0
0.52
-
NAD+
-
isoform NADK1, pH 7.9, 25C; pH 7.9, 25C
0.53
-
NAD+
-
pH 7.0, 37C, cosubstrate ATP, wild-type
0.54
-
NAD+
-
30C
0.6
-
NAD+
-
-
0.67
-
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.68
-
NAD+
-
pH 9.0, 30C
1
-
NAD+
-
wild-type
1.03
-
NAD+
-
isoenzyme 2
1.07
-
NAD+
-
at pH 8.0 and 50C
1.1
-
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
1.2
-
NAD+
-
native enzyme
1.2
-
NAD+
-
cosubstrate polyphosphate, wild-type, 37C, pH 8.0
1.4
-
NAD+
-
cosubstrate polyphosphate, mutant T195A, 37C, pH 8.0
1.4
-
NAD+
-
wild type enzyme, at pH 7.5 and 30C
1.41
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
1.43
-
NAD+
-
pH 7.0, 37C, cosubstrate ATP, mutant G183R
1.5
-
NAD+
-
enzyme immobilized on CNBr-activated Sepharose 4B
1.59
-
NAD+
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
1.85
-
NAD+
-
pH 7.0, 37C, wild-type
1.86
-
NAD+
-
pH 7.0, 37C, cosubstrate poly(P)4, mutant G183R
2
-
NAD+
-
pH 7.0, 37C
2
-
NAD+
-
pH 7.0, 37C, mutant R175G
2.1
-
NAD+
-
cosubstrate polyphosphate, mutant S199A, 37C, pH 8.0
2.11
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
2.7
-
NAD+
-
pH 6.8
2.7
-
NAD+
-
cosubstrate ATP, mutant T195A, 37C, pH 8.0
3
-
NAD+
-
85C, pH 8.5, 20 mM Mg2+
3.3
-
NAD+
-
cosubstrate ATP, mutant S199A, 37C, pH 8.0; cosubstrate ATP, wild-type, 37C, pH 8.0
3.8
-
NAD+
-
cosubstrate polyphosphate, mutant G208A, 37C, pH 8.0
4.02
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
6.5
-
NAD+
-
cosubstrate ATP, mutant G208A, 37C, pH 8.0
0.05
-
NADH
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
2
-
NADH
-
30C, pH 8.0
0.21
-
poly(P)4
-
pH 7.0, 37C, mutant G183R
0.33
-
poly(P)4
-
pH 7.0, 37C, wild-type
2.2
-
Polyphosphate
-
mutant S199A, 37C, pH 8.0; mutant T195A, 37C, pH 8.0
2.5
-
Polyphosphate
-
wild-type, 37C, pH 8.0
2.7
-
Polyphosphate
-
mutant G208A, 37C, pH 8.0
5.9
-
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
17.2
-
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
14.1
-
polyphosphate(45)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
18.4
-
polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
3.1
-
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
2.1
-
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
12
-
Tetrapolyphosphate
-
in 100 mM Tris-HCl (pH 8.0), at 37C
2.4
-
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.42
-
UTP
-
pH 8
0.2
-
MgGTP2-
-
isoenzyme 2
additional information
-
additional information
-
allosteric enzyme, Hill coefficient for ATP 1.5, for polyphosphate 1.4
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.3
-
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.52
-
ATP
-
wild type enzyme, at pH 7.5 and 30C
0.6
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
2.02
-
ATP
C4LSN1, -
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
2.03
-
ATP
-
mutant D45N
2.54
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
2.68
-
ATP
C4LSN1, -
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
13.78
-
ATP
-
wild-type
20.51
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
29.2
-
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
30.33
-
ATP
Q6L7J5
30C, pH 8.0
55
-
ATP
-
pH 7.0, 37C
399
-
ATP
-
85C, pH 8.5, 20 mM Mg2+
0.41
-
NAD+
-
mutant D45N, in the presence of 0.5 mM ATP
0.5
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
0.54
-
NAD+
-
wild type enzyme, at pH 7.5 and 30C
1.34
-
NAD+
-
mutant D45N, in the presence of 4 mM ATP
1.9
-
NAD+
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
2.95
-
NAD+
Q6L7J5
30C, pH 8.0
3.62
-
NAD+
-
wild-type, in the presence of 0.5 mM ATP
3.8
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
7.8
-
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
13.12
-
NAD+
-
wild-type, in the presence of 4 mM ATP
15.42
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
27.1
-
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
125
-
NAD+
-
pH 7.0, 37C
424
-
NAD+
-
85C, pH 8.5, 20 mM Mg2+
1.9
-
NADH
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
7.8
-
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
7.3
-
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
3.4
-
polyphosphate(45), polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
1.8
-
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
-
8.7
-
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
3
-
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
212
-
fructose-1,6-bisphosphate
Q58327
-
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, 30C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.5
-
ADP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
6504
0.24
-
ATP
-
wild type enzyme, at pH 7.5 and 30C
22040
0.56
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
22040
1.16
-
ATP
C4LSN1, -
with NAD+ as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
22040
1.3
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
22040
5.5
-
ATP
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
22040
6.72
-
ATP
C4LSN1, -
with NADH as cosubstrate, in 100 mM Tris-HCl (pH 7.5), at 37C
22040
59.6
-
ATP
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
22040
0.36
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 6.0 and 30C
14330
0.39
-
NAD+
-
wild type enzyme, at pH 7.5 and 30C
14330
0.94
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
wild type enzyme, at pH 7.5 and 30C
14330
1.2
-
NAD+
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
14330
7.05
-
NAD+
-
in the presence of polyphosphate(20), in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
14330
7.32
-
NAD+
Corynebacterium glutamicum subsp. lactofermentum
-
mutant enzyme P57S/P117S, at pH 7.5 and 30C
14330
40.5
-
NAD+
-
in the presence of ATP, in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
14330
56.48
-
NADH
C4LSN1, -
in 100 mM Tris-HCl (pH 7.5), at 37C
14331
1.3
-
polyphosphate(20)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0
0.42
-
polyphosphate(25)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
329208
0.24
-
polyphosphate(45)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0
0.19
-
polyphosphate(65)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0
0.58
-
polyphosphate(75)
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0
4.1
-
Tetraphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
17083
1.2
-
Triphosphate
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
17460
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-, Q8Y8D7
in 50 mM Tris-HCl, pH 7.4, 10 mM MgCl2, at 30C
3.6
-
5'-thioacetyladenosine
-
-
0.02
-
di-(5'-thioadenosine)
-
-
0.03
-
NADH
-
pH 6.5, 30C
0.11
-
NADH
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.24
-
NADH
-
at pH 8.0 and 30C
0.62
-
NADH
Corynebacterium glutamicum subsp. lactofermentum
-
at pH 7.5 and 30C
1.02
-
NADH
-
pH 8
0.13
-
NADP+
-
pH 6.8
0.21
-
NADP+
-
at pH 8.0 and 30C
0.34
-
NADP+
-
in 100 mM HEPES, pH 7.3, containing 20 mM MgCl2, at 30C
0.43
-
NADP+
Corynebacterium glutamicum subsp. lactofermentum
-
at pH 7.5 and 30C
0.013
-
NADPH
-
pH 6.5, 30C
0.16
-
NADPH
-
pH 8
0.17
-
NADPH
-
at pH 8.0 and 30C
0.22
-
NADPH
Corynebacterium glutamicum subsp. lactofermentum
-
at pH 7.5 and 30C
2.8
-
Trifluoperazine
-
pH 8
0.01
-
W-7
-
pH 8
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0009966
-
-
-
0.281
-
Q6L7J5
30C, pH 8.0
0.5
-
-
substrates ATP, NAD+, mutant G208A, 37C, pH 8.0
0.7
-
-
substrates ATP, NAD+, mutant S199A, 37C, pH 8.0
0.8
-
-
-
1.1
-
-
substrates ATP, NAD+, mutant T195A, 37C, pH 8.0
1.2
-
-
substrates ATP, NAD+, wild-type, 37C, pH 8.0
1.4
-
-
pH 7.0, 37C, substrate NAD+, cosubstrate poly(P)4, mutant G183R
1.78
-
-
pH 7.0, 37C, substrate NAD+, cosubstrate ATP, mutant G183R
2.2
-
-
substrates polyphosphate, NAD+, mutant G208A, 37C, pH 8.0
2.33
-
-
pH 7.0, 37C, mutant R175G, substrate NAD+
2.5
-
-
substrates polyphosphate, NAD+, mutant S199A, 37C, pH 8.0
2.68
-
-
pH 7.0, 37C, mutant R175, substrate ATP
3.5
-
-
substrates polyphosphate, NAD+, mutant T195A, 37C, pH 8.0
3.8
-
-
substrates polyphosphate, NAD+, wild-type, 37C, pH 8.0
3.84
-
-
activated by Ca2+-calmodulin
6.7
-
-
-
8.63
-
-
pH 7.0, 37C, substrate NAD+, cosubstrate poly(P)4, wild-type
11.1
-
-
isoform NADK1, pH 7.9, 25C; pH 7.9, 25C
12.45
-
-
pH 7.0, 37C, wild-type, substrate ATP
12.86
-
-
pH 7.0, 37C, wild-type, substrate NAD+
14.3
-
-
isoform NADK2, pH 7.9, 25C; pH 7.9, 25C
18.67
-
-
pH 7.0, 37C, substrate NAD+, cosubstrate ATP, wild-type
23.2
-
-
ATP-dependent activity
24.3
-
-
polyphosphate-dependent activity
213
-
-
; calmodulin-depndent isoform, pH 7.9, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
enzyme immobilized on CNBr-activated Sepharose 4B, phosphate buffer
7
7.6
-
enzyme from liver
7
9.5
-
-
7
-
-
native enzyme, phosphate buffer, Tris-HCl buffer
7.1
-
-
for polyphosphate-dependent activity
7.2
8
-
enzyme from heart muscle
7.3
-
-
for ATP-dependent activity
7.5
8
-
410000 Da Ca2+-calmodulin-independent isoform and 63000 Da Ca2+-calmodulin-dependent isoform
7.5
-
-
enzyme immobilized on CNBr-activated Sepharose 4B, Tris-HCl buffer
7.5
-
-
Tris/HCl buffer
7.5
-
C4LSN1, -
-
7.5
-
Corynebacterium glutamicum subsp. lactofermentum
-
-
7.8
-
-
-
7.9
-
-
; isoforms NADK1, NADK2
8
-
-
50 mM Hepes-KOH buffer or tricine-KOH buffer
8
-
-
; calmodulin-dependent isoform
8
-
Q6L7J5
-
9
-
-
glycine-NaOH buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
about 50% of maximal activity at pH 5.5 and pH 7.5
6
10
-
pH 6.0: about 40% of maximal activity, pH 10.0: about 80% of maximal activity
6
7
-
activity decreases sharply below pH 6.0 and above pH 7.0
6.5
7.2
-
90% of maximal activity at pH 6.5 and pH 7.2
6.5
9.5
-
pH 6.5: about 35% of maximal activity, pH 9.5: about 90% of maximal activity
6.8
9.2
-
90% of maximal activity between pH 6.8 and pH 9.2, 410000 Da Ca2+-calmodulin-independent isoform
7
10
-
pH 7.0: about 35% of maximal activity, pH 10.0: about 50% of maximal activity
7.2
8.5
-
90% of maximal activity between pH 7.2 and pH 8.5, 63000 Da Ca2+-calmodulin-dependent isoform
additional information
-
-
broad
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
native enzyme
50
-
-
-
55
-
-
enzyme immobilized on CNBr-activated Sepharose 4B
55
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
25C: about 45% of maximal activity, 50C: about 70% of maximal activity
37
68
-
about 50% of maximal activity at 37C and at 68C
50
55
Q6L7J5
-
80
100
-
80C: about 45% of maximal activity, 100C: optimum
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
isoelectric focusing
6.5
-
C4LSN1, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
maximal activity is observed on day 5 in light-exposed calli or day 14 in day-exposed ones. After 5 d of salt exposure, NAD kinase activity is markedly lower than in control, but NAD kinase of dark-exposed and NaCl-exposed calli is 10times more active than that of both light-exposed and NaCl-exposed calli
Manually annotated by BRENDA team
-
grown heterotrophically in darkness at pH 3.5 in the presence of lactate as sole carbon source. Treatment with AlCl3 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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Euglena gracilis Z
-
grown heterotrophically in darkness at pH 3.5 in the presence of lactate as sole carbon source. Treatment with AlCl3 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
-
Manually annotated by BRENDA team
-
initiated from white and friable root calli
Manually annotated by BRENDA team
-
fibroblast
Manually annotated by BRENDA team
-
from embryo
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
isoform NADK2
Manually annotated by BRENDA team
-
isoform NADK1
Manually annotated by BRENDA team
-
culture of after-ripened and dormant seeds
Manually annotated by BRENDA team
-
calmodulin-dependent isoform
Manually annotated by BRENDA team
-
no expression of NAD kinase in skeletal muscle
Manually annotated by BRENDA team
-
lowest expression
Manually annotated by BRENDA team
-
little expression
Manually annotated by BRENDA team
additional information
-
both isoforms NADK1 and NADK2 are present in all tissues examined and throughout development
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q500Y9, Q56YN3, Q9C5W3
; isoform NADK2
Manually annotated by BRENDA team
-
the enzyme from skeletal muscle is susceptible to seasonal alterations: in autumn and winter, NADP+ synthesis proceeds maximally in the cytoplasm, in spring, higher activity is found in the mitochondrial fraction
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
the enzyme from skeletal muscle is susceptible to seasonal alterations: in autumn and winter, NADP+ synthesis proceeds maximally in the cytoplasm, in spring, higher activity is found in the mitochondrial fraction
Manually annotated by BRENDA team
-
isoenzyme 1 and 2
-
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Euglena gracilis Z
-
isoenzyme 1 and 2
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60000
-
-
gel filtration
63000
-
-
Ca2+-calmodulin-dependent isoenzyme
64000
-
Q6L7J5
gel filtration
68000
-
-
gel filtration
75000
-
-
gel filtration
82000
-
-
gel filtration
110000
-
Q500Y9, Q56YN3, Q9C5W3
isoform NADK2
124000
-
-
equilibrium sedimentation
140000
-
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
gel filtration
145000
-
-
gel filtration
167500
-
-
gel filtration
169000
-
-
gel filtration
172000
-
-
gel filtration
180000
-
-
gel filtration
200000
-
-
gel filtration
260000
-
-
non-denaturing PAGE
270000
-
-
gel filtration
410000
-
-
Ca2+-calmodulin-independent NAD+ kinase, gel filtration
480000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 39114, calculation from nucleotide sequence
?
Q500Y9, Q56YN3, Q9C5W3
? x 110000; ? x 58000
?
C7GKE4, Q06892
x * 46000
?
C4LSN1, -
x * 29500, calculated from amino acid sequence; x * 32000, recombinant enzyme, SDS-PAGE
?
-
x * 31000, SDS-PAGE
?
Entamoeba histolytica HM1: IMSS cl 6
-
x * 29500, calculated from amino acid sequence; x * 32000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 30000, SDS-PAGE
dimer
-
or trimer, 2 * 33000, SDS-PAGE
dimer
-
or tetramer, crystallization data
dimer
Q6L7J5
2 * 32000, SDS-PAGE
dimer
-
without effectors, NadK exists as an equilibrium mixture of dimers and tetramers but is converted entirely to tetramers in the presence of the inhibitor NADPH. Comparison of NadK kinetic parameters with pool sizes of NADH and NADPH suggests that NadK is substantially inhibited during normal growth and, thus, can increase its activity greatly in response to temporary drops in the pools of inhibitory NADH and NADPH. The primary inhibitor is NADPH during aerobic growth and NADH during anaerobic growth
hexamer
-
6 * 30000, SDS-PAGE
hexamer
-
4 * 49228, calculation from nucleotide sequence
hexamer
Escherichia coli MG1655
-
6 * 30000, SDS-PAGE
-
homodimer
Q500Y9, Q56YN3, Q9C5W3
2 x 38000
homodimer
O31612, O34934
2 * 30000
homodimer
Q8VUL9
2 x 34000
homodimer
Q6L7J5
2 * 32000
homodimer
-
2 * 43000, SDS-PAGE; 2 * 43300, calculated from amino acid sequence
homohexamer
P0A7B3
6 x 30000
homohexamer
C7GKE4, Q06892
6 * 60000; 6 * 60000, Utr1p
homooctamer
C7GKE4, Q06892
6 * 60000, Yef1p; 8 * 60000
homotetramer
-
4 * 49000; 4 x 49000
homotetramer
Q58327
4 x 64000
homotetramer
-
4 x 35000
homotetramer
-
4 * 37000
homotetramer
-
crystallography
homotetramer
-
2 * 34300, SDS-PAGE
homotetramer
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
4 * 36000, SDS-PAGE
homotetramer
-
4 * 43000, SDS-PAGE
homotetramer
-
2 * 34300, SDS-PAGE
-
octamer
-
8 * 34000, SDS-PAGE
octamer
-
8 * 60000, SDS-PAGE
oligomer
-
x * 32000, SDS-PAGE
tetramer
-
4 * 31000 SDS-PAGE
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
or dimer, crystallization data
tetramer
-
without effectors, NadK exists as an equilibrium mixture of dimers and tetramers but is converted entirely to tetramers in the presence of the inhibitor NADPH. Comparison of NadK kinetic parameters with pool sizes of NADH and NADPH suggests that NadK is substantially inhibited during normal growth and, thus, can increase its activity greatly in response to temporary drops in the pools of inhibitory NADH and NADPH. The primary inhibitor is NADPH during aerobic growth and NADH during anaerobic growth
trimer
-
or dimer, 3 * 33000, SDS-PAGE
homotetramer
Corynebacterium glutamicum ATCC13869, Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
4 * 36000, SDS-PAGE
-
additional information
-
Ca2+-dependent calmodulin-binding domain near N-terminal extension of isoform NADK2
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with ATP, NAD, or NADP, AMP portion of ATP uses the same binding site as the nicotinamide ribose portion of NAD/NADP
-, O30297
by hanging-drop-based sparse-matrix screening strategy. NAD kinase crystallized in complex with its substrate NAD, its product NADP, or two synthesized NAD mimics, at near 2 A resolution. D45N mutant using the I222 5'-thioacetyladenosine-bound crystal form, to 2.2 A resolution, and mutant H223E
-
enzyme bound to compounds 5'-O-propargyl-5'-deoxyadenosine, 5'-azido-5'-deoxyadenosine, 8-bromo-5'-amino-5'-deoxyadenosine, or 8-thioglycolic-5'-azido-5'-deoxyadenosine, using 30 mM sodium bromide, 220 mM potassium citrate, pH 4.8-5.1, 6% glycerol, 15%-16% (w/v) polyethylene glycol 400
-, Q8Y8D7
apo form of Ppnk at 2.8 A resolution. Crystals belong to space group C2 (a=140.2, b=69.4, c=106.4 A, and beta=130). Holo form of Ppnk complexed with NAD+ at 2.6 A resolution. Crystals belong space group to P62 (a=b=110.5 and c=108.9 A). Overall structures of apo-Ppnk and Ppnk-NAD consist of an N-domain (residues 1-138 and 279-283), a C-domain (residues 139-278), and a C-terminal tail (residues 284-307)
-
in complex with NAD+
-
recombinant enzyme, crystallization by hanging-drop vapour-diffusion method with polyethylene glycol 4000 as the precipitant
-
T-state of protein
-
crystals of SeMet-containing PPNK_THEMA are obtained at room temperature in hanging drops. Crystal structure of inorganic polyphosphate/ATP-NAD kinase is determined at 2.3 A resolution. The crystal structure is solved using single-wavelength anomalous diffraction data collected at the Se absorption-peak wavelength in a state in which no cofactors or substrates are bound. It revealed that the 258-amino-acid protein is folded into two distinct domains. The N-terminal alpha/beta-domain spans the first 100 amino acids and the last 30 amino acids of the polypeptide and has several topological matches in the PDB, whereas the other domain, which spans the middle 130 residues, adopts a unique beta-sandwich architecture and only appreciably matches the recently deposited PDB structures of NAD kinases
Q9X255, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
4C, 18 h, about 60% loss of activity, irreversible loss of activity
5.5
7
-
4C, stable for at least 48 h, irreversible loss of activity below pH 5.5
5.5
7
-
37C, 2 h, native and immobilized stable
5.5
-
-
rapid inactivation below
6
7
-
4C, 18 h, stable
7
8
-
the enzyme is precipitated and denatured at pH 7.0. Even at pH 8.0, the enzyme is depolymerized and denatured after long-time storing
7
-
Corynebacterium glutamicum subsp. lactofermentum
-
the enzyme remains stable at pH 7.0
8
-
-
4C, 18 h, about 50% loss of activity, loss of activity is reversible by dialysis to pH 6.2
8.5
-
-
4C, 18 h, about 70% loss of activity, loss of activity is reversible by dialysis to pH 6.2
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
20 min, 12% loss of activity
30
-
-
20 min, 37% loss of activity
38
-
-
20 min, 70% loss of activity. 5 min, about 50% loss of activity
40
-
-
native enzyme and immobilized enzyme, stable
40
-
-
15 min, 50% loss of activity
45
60
-
preheating the enzyme for 1 h at temperatures up to 45C does not alter the activity. When preheated at 50C for 1 h, enzyme activity measured at 30C decreases by 30% and preincubation at 56C and 60C leads to a fast and complete loss of activity after 10 and 5 min, respectively
50
-
-
10 min, stable
54
-
-
10 min, 50% loss of activity
55
-
-
immobilized enzyme is more stable than the native enzyme above 55C
60
68
-
stable for 5-30 min
60
-
-
10 min, about 10% loss of activity
60
-
-
5 min, less than 5% loss of activity
63
-
Q6L7J5
10 min, 50% residual activity
65
-
-
10 min, about 45% loss of activity
70
-
-
60 min, stable in pH-range 4.0-10.5
70
-
-
preincubating the enzyme for 2 h at 70C results in a loss of 50% of its activity
70
-
Corynebacterium glutamicum subsp. lactofermentum
-
preheating the enzyme for 2 h at temperatures up to 70C does not alter the ATP-NAD+ kinase activity significantly (less than 10% of the activity lost)
95
-
-
10 min, stable
100
-
-
10 min, 20% residual activity
additional information
-
-
ATP, NAD+ and 2-mercaptoethanol stabilize against thermal inactivation
additional information
-
-
the enzyme immobilized on CNBr-activated Sepharose is more stable against heat than the native enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable, loses activity at room temperature overnight
-
partial loss of activity after freezing and thawing
-
liver enzyme can be dialyzed at 4C for at least 16 h with loss of activity and is also stable towards freezing and thawing
-
stability is enhanced by immobilization on CNBr-activated Sepharose 4B
-
liver preparation is unstable to dialysis and repeated freezing and thawing
-
dialysis at 4C for 18 h against buffer at pH 8.5 results in loss of 80% of the activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, 30% v/v glycerol, stable for more than 3 months
-
4C, 80% loss of activity after 7 days, no loss of activity after 5 days in presence of serum albumin
-
-30 or -80C, 10-15% (v/v) glycerol, at least 3 months, no loss of activity
C4LSN1, -
4C, 0.1 M phosphate buffer, pH 7.5, activity of the native enzyme is entirely lost after 55 days, enzyme immobilized and CNBr-activated Sepharose 4B retains activity without any detectable loss of after 70 days
-
-20C, stable for several weeks
-
precipitation during dialysis against phosphate buffer without NaCl and imidazole, storage in 0.5 M NaCl and 0.5 M imidazole at 4C for up to 2 months without loss of activity
-
4C, stored as a slurry in 60% saturated (NH4)2SO4 stable for at least 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial; recombinant isoforms NADK1, NADK2, partial purification of calmodulin-dependent isoform; single-step calmodulin-affinity chromatography
-
partially purified; partially purified; partially purified
Q500Y9, Q56YN3, Q9C5W3
partial
-
Ni-NTA column chromatography, gel filtration
Corynebacterium glutamicum, Corynebacterium glutamicum subsp. lactofermentum
-
Ni-NTA agarose column chromatography, gel filtration
C4LSN1, -
partial
-
recombinant enzyme
-
Talon column chromatography
-
TALON column chromatography and Mono Q column chromatography
-
affinity chromatography and gel filtration
-
cobalt-based IMAC resin column chromatography
-, Q8Y8D7
recombinant enzyme
-
recombinant enzyme
-
recombinant enzyme
-
partially purified; partially purified; partially purified
C7GKE4, Q06892
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
Corynebacterium glutamicum subsp. lactofermentum
-
expressed in Escherichia coli BL21(DE3) cells
C4LSN1, -
expressed in Escherichia coli
-
cDNA is amplified and functionally overexpressed in Escherichia coli
-
expressed in Escherichia coli Rosetta-gami(DE3)pLysS cells
-
overexpressed in HEK-293 cells
-
expressed in Escherichia coli
-, Q8Y8D7
into vector pET22b and expressed in Escherichia coli BL21(DE3)/pDIA17
-
expression in Escherichia coli
-
cloning of mknk and determination of primary structure
-
Ppnk overexpressed
-
expression in Escherichia coli as N-terminally His-tagged fusion; expression in Escherichia coli as N-terminally His-tagged fusion
-
overexpression of UTR1 via a high-copy plasmid; overexpression of YEF1 via a high-copy plasmid
C7GKE4, Q06892
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
Q9X255, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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 ATCC13869
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S
Corynebacterium glutamicum ATCC13869
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S/P117S
Corynebacterium glutamicum ATCC13869
-
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 ATCC13869
-
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
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
P196A
-
no enzymic activity
S199A
-
decrease in Vmax-value
T195A
-
kinetic parameters similar to wild-type
T197A
-
no enzymic activity
T200A
-
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
Q500Y9, Q56YN3, Q9C5W3
NADK1-deficient mutant exhibits sensitivity to gamma irradiation and paraquat-induced oxidative stress; 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
O31612, O34934
mutant for NadF is lethal
R175T
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
additional information
-
sensitivity of NADK(-) cells to oxidative stress is the same as that of the control cells
L192A
-
no enzymic activity
additional information
-
mutants of the NAD kinase gene are lethal
Y202A
-
no enzymic activity
additional information
C7GKE4, Q06892
triple mutant utr1yef1pos5 is lethal; triple mutant utr1yef1pos5 is lethal. Double mutant utr1pos5 is lethal against the SEY6210.5 and S288c backgrounds; 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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
Q9X255, -
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
overexpressing NAD kinase is a useful metabolic engineering strategy to improve NADPH supply and isoleucine biosynthesis
synthesis
Corynebacterium glutamicum ATCC13869
-
overexpressing NAD kinase is a useful metabolic engineering strategy to improve NADPH supply and isoleucine biosynthesis
-
synthesis
Corynebacterium glutamicum subsp. lactofermentum
-
overexpressing NAD kinase is a useful metabolic engineering strategy to improve NADPH supply and isoleucine biosynthesis
synthesis
-
combined activation of PntAB and YfjB leads to 28% and 22% increase of aerobic isobutanol titer and yield, resulting in production of 10.8 g/l isobutanol in 24 h with a yield of 0.62 mol/mol
analysis
-
enzyme-dependent assay for detection and quantification of calmodulin inhibitors
analysis
-
studies of enzyme activation by calmodulin, calmodulin-like proteins, calcium-binding proteins, and calmodulin mutants
additional information
Q500Y9, Q56YN3, Q9C5W3
one of the key enzymes regulating the balance of NAD(H) and NADP(H); one of the key enzymes regulating the balance of NAD(H) and NADP(H); one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
agriculture
-
an excess of the Ca2+-calmodulin-dependent isoforms could by a marker of stress or lethal conditions
additional information
O31612, O34934
one of the key enzymes regulating the balance of NAD(H) and NADP(H); one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
synthesis
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
overexpressing NAD kinase is a useful metabolic engineering strategy to improve NADPH supply and isoleucine biosynthesis
-
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
P0A7B3
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
synthesis
Escherichia coli MG1655
-
combined activation of PntAB and YfjB leads to 28% and 22% increase of aerobic isobutanol titer and yield, resulting in production of 10.8 g/l isobutanol in 24 h with a yield of 0.62 mol/mol
-
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
key role of NADK in animal cells for the maintenance of the cellular NADPH pool. NADK overexpression and the ensuing increase of the NADPH level only moderately enhances protection against oxidant treatment
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
conserved GGDGT motif of NADKs
additional information
Q58327
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
Q8VUL9
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
analysis
-
in-gel activity staining of oxidized nicotinamide adenine dinucleotide kinase by blue native polyacrylamide gel electrophoresis. This technique allows the monitoring of the activity and expression of this kinase in various biological systems
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
C7GKE4, Q06892
one of the key enzymes regulating the balance of NAD(H) and NADP(H); one of the key enzymes regulating the balance of NAD(H) and NADP(H); one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
Q6L7J5
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)