Any feedback?
Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Homo sapiens and UniProt Accession O95544
for references in articles please use BRENDA:EC2.7.1.23Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.23 NAD+ kinaseSpecify your search results
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, nad(h) kinase, utr1p, osnadk1, slr0400, c5orf33, sll1415, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:NAD 2'-phosphotransferase
-
-
-
-
DPN kinase
-
-
-
-
kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
-
kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
NAD kinase
NADK
nicotinamide adenine dinucleotide kinase
-
-
-
-
Poly(P)/ATP NAD kinase
-
-
-
-
polyphosphate/ATP-NAD kinase
-
-
-
-
NAD kinase
-
-
-
-
NADK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9032-66-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetrapolyphosphate + NAD+
tripolyphosphate + NADP+
-
84% activity compared to ATP
-
-
?
additional information
?
-
-
no activity with NAAD, ADP-ribose, adenosine, 5'-AMP, ADP, sphingosine, diacylglycerol, fructose 6-phosphate, trimetaphosphate, tripolyphosphate, phosphoenolpyruvate, and phosphocreatine
-
-
?
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+
-
preferentially accepts NAD+ as substrate. At 100 micromol, NAD+ is 10fold faster phosphorylated than NADH
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
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+
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
Mg2+
optimal concentration is 10 mM. At 1 mM, 29% of the activation with 1 mM Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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-trifluoromethylphenethyl)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
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
overexpression of NADK results in an almost 200fold increase of both the mRNA level, the protein amount and the catalytic activity
-
Calmodulin
calmodulin-dependent enzyme is stimulated 3.5fold by addition of calmodulin in presence of Ca2+
Calmodulin
Ca2+/calmodulin regulates NAD kinase activity. Ca2+/calmodulin has no detectable effect on recombinant human NAD kinase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
pH 7.4, 30°C
0.08
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)propanamide
-
pH 7.4, 30°C
0.13
2-[(5'-amino-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.525
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-benzimidazolylethyl)acetamide
-
pH 7.4, 30°C
0.22
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-chloro-5-pyridyl)acetamide
-
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(2-naphthylethyl)acetamide
-
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3,4-dichlorophenethyl)acetamide
-
pH 7.4, 30°C
0.055
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromobenzyl)acetamide
-
pH 7.4, 30°C
0.33
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.02
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-chlorophenethyl)acetamide
-
pH 7.4, 30°C
0.3
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(3-trifluoromethylphenethyl)acetamide
-
pH 7.4, 30°C
0.08
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-bromophenethyl)acetamide
-
pH 7.4, 30°C
0.21
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-(4-chlorophenethyl)acetamide
-
pH 7.4, 30°C
0.35
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylacetamide
-
pH 7.4, 30°C
0.15
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-phenethylpropanamide
-
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-propargylacetamide
-
pH 7.4, 30°C
0.14
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.23
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(4-trifluoromethyl)phenethyl]acetamide
-
pH 7.4, 30°C
0.065
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-chloro-3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.16
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[(5-methoxy-3-indoyl)ethyl]acetamide
-
pH 7.4, 30°C
0.35
2-[(5'-azido-5'-deoxyadenosine)-8-thio]-N-[3-(1-methylindolyl)ethyl]acetamide
-
pH 7.4, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is required for the de novo synthesis of NADP+ from NAD+. In neutrophils, the enzyme plays an essential role by providing sufficient levels of NADPH to support a robust oxidative burst
drug target
-
nicotinamide adenine dinucleotide kinases are attractive for inhibitor development, since they catalyze the phosphorylation of NAD to NADP, which is an essential step of NADP metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NADK_HUMAN
446
0
49228
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
homodimer
homotetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
Akt-mediated phosphorylation of NAD+ kinase stimulates its activity to increase NADP+ production through relief of an autoinhibitory function inherent to its amino terminus. NAD+ kinase (isoform 3) lacking this regulatory region exhibits constitutively increased activity
phosphoprotein
phosphorylation of NAD+ kinase by a protein kinase C isoform, possibly PKCdelta, in stimulated neutrophils results in a rapid increase in its activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lerner, F.; Niere, M.; Ludwig, A.; Ziegler, M.
Structural and functional characterization of human NAD kinase
Biochem. Biophys. Res. Commun.
288
69-74
2001
Bos taurus, Homo sapiens (O95544), Homo sapiens
Williams, M.B.; Jones, H.P.
Calmodulin-dependent NAD kinase of human neutrophils
Arch. Biochem. Biophys.
237
80-87
1985
Homo sapiens (O95544), Homo sapiens
McGuiness, E.T.; Butler, J.R.
NAD+ kinase-a review
Int. J. Biochem.
17
1-11
1985
Achromobacter aceris, Azotobacter vinelandii, Bos taurus, Columba sp., Corynebacterium ammoniagenes, Cyberlindnera jadinii, Gallus gallus, Homo sapiens (O95544), Nicotiana tabacum, Oryctolagus cuniculus, Pisum sativum, Rattus norvegicus, Saccharomyces cerevisiae, Spinacia oleracea, Triatoma infestans
Bonnac, L.; Chen, L.; Pathak, R.; Gao, G.; Ming, Q.; Bennett, E.; Felczak, K.; Kullberg, M.; Patterson, S.E.; Mazzola, F.; Magni, G.; Pankiewicz, K.W.
Probing binding requirements of NAD kinase with modified substrate (NAD) analogues
Bioorg. Med. Chem. Lett.
17
1512-1515
2007
Homo sapiens (O95544), Homo sapiens, Saccharomyces cerevisiae (P21373)
Kawai, S.; Murata, K.
Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
Biosci. Biotechnol. Biochem.
72
919-930
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Archaeoglobus fulgidus, Bacillus subtilis (O31612), Bacillus subtilis (O34934), Candida albicans, Columba livia, Cyberlindnera jadinii, Dictyostelium discoideum, Escherichia coli (P0A7B3), Glycine max, Homo sapiens, Homo sapiens (O95544), Lactuca sativa, Listeria monocytogenes, Methanocaldococcus jannaschii (Q58327), Micrococcus luteus (Q8VUL9), Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis H37Rv (P9WHV7), Oryza sativa, Pyrococcus horikoshii (O58801), Saccharomyces cerevisiae (C7GKE4), Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae, Salmonella enterica, Schizosaccharomyces pombe, Sorghum sp., Sphingomonas sp. A1 (Q6L7J5), Synechococcus elongatus PCC 6301, Thermotoga maritima, Triticum sp.
Pollak, N.; Niere, M.; Ziegler, M.
NAD kinase levels control the NADPH concentration in human cells
J. Biol. Chem.
282
33562-33571
2007
Homo sapiens
Ohashi, K.; Kawai, S.; Koshimizu, M.; Murata, K.
NADPH regulates human NAD kinase, a NADP+-biosynthetic enzyme
Mol. Cell. Biochem.
355
57-64
2011
Homo sapiens
Ohashi, K.; Kawai, S.; Murata, K.
Identification and characterization of a human mitochondrial NAD kinase
Nat. Commun.
3
1248
2012
Homo sapiens
Paoletti, J.; Assairi, L.; Gelin, M.; Huteau, V.; Nahori, M.A.; Dussurget, O.; Labesse, G.; Pochet, S.
8-Thioalkyl-adenosine derivatives inhibit Listeria monocytogenes NAD kinase through a novel binding mode
Eur. J. Med. Chem.
124
1041-1056
2016
Homo sapiens, Listeria monocytogenes serotype 1/2a (Q8Y8D7), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y8D7)
Rabani, R.; Cossette, C.; Graham, F.; Powell, W.S.
Protein kinase C activates NAD kinase in human neutrophils
Free Radic. Biol. Med.
161
50-59
2020
Homo sapiens (O95544), Homo sapiens
Li, B.; Wang, X.; Tai, L.; Ma, T.; Shalmani, A.; Liu, W.; Li, W.; Chen, K.
NAD kinases Metabolic targets controlling redox co-enzymes and reducing power partitioning in plant stress and development
Front. Plant Sci.
9
379
2018
Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Archaeoglobus fulgidus (P0A7B3), Bacillus subtilis (M4KX93), Escherichia coli (P0A7B3), Escherichia coli K12 (P0A7B3), Glycine max (I1KAE3), Glycine max (I1LPA7), Glycine max (I1LVA5), Glycine max (K7LNT1), Glycine max (K7LY64), Homo sapiens (O95544), Homo sapiens (Q4G0N4), Pyrococcus horikoshii (O58801), Pyrococcus horikoshii ATCC 700860 (O58801), Solanum lycopersicum (A0A3Q7E928), Solanum lycopersicum (A0A3Q7JHB9), Sphingomonas sp. (O58801), Strongylocentrotus purpuratus (C3RSF7), Strongylocentrotus purpuratus (P21373)
EXTERNAL LINKS (specific for EC-Number 2.7.1.23)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
