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Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P21373

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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P21373 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, nad(h) kinase, utr1p, osnadk1, slr0400, c5orf33, sll1415, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:NAD 2'-phosphotransferase
-
-
-
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DPN kinase
-
-
-
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kinase (phosphorylating), nicotinamide adenine dinucleotide
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-
-
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kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
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NAD kinase
NADK
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-
-
-
nicotinamide adenine dinucleotide kinase
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-
-
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Poly(P)/ATP NAD kinase
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-
-
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polyphosphate/ATP-NAD kinase
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-
-
-
YEF1
low specific activity cytosolic NAD kinase
Yef1p
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NAD+ = ADP + NADP+
show the reaction diagram
sequential mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-66-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
show the reaction diagram
ATP + NADH
ADP + NADPH
show the reaction diagram
CTP + NAD+
CDP + NADP+
show the reaction diagram
specific activity is 7fold lower than with NAD+ and ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
specific activity is 13.2fold lower than with NADH and ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
specific activity is 2.6fold lower than with ATP and NAD+
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
specific activity is 3.3fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
specific activity is 13.2fold lower than with ATP and NAD+
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
ATP + NADH
ADP + NADPH
show the reaction diagram
CTP + NAD+
CDP + NADP+
show the reaction diagram
specific activity is 16.5fold lower than with NAD+ and ATP
-
-
?
CTP + NADH
CDP + NADPH
show the reaction diagram
specific activity is 2.4fold lower than with NADH and ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
specific activity is similar to reaction with ATP and NAD+
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
specific activity is 11fold lower than with ATP and NAD+
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
specific activity is 11fold lower than with ATP and NAD+
-
-
?
NADH + ATP
NADPH + ADP
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
show the reaction diagram
Utr1 is responsible for essentially all of the NAD/NADH kinase activity resident in the cytoplasm
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
Yef1 contributes very slightly to total NAD and NADH kinase activities in vivo
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
POS5 is upregulated 3.4fold after treatment for 10 to 12 min with 2.5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 2.3
ATP
0.68
NAD+
-
pH 9.0, 30°C
2
NADH
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30°C, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
124000
-
equilibrium sedimentation
31000
-
4 * 31000 SDS-PAGE
480000
-
gel filtration
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
homooctamer
octamer
-
8 * 60000, SDS-PAGE
tetramer
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4 * 31000 SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54
-
10 min, 50% loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as N-terminally His-tagged fusion
overexpression of UTR1 via a high-copy plasmid
expression in Escherichia coli as N-terminally His-tagged fusion
overexpression of YEF1 via a high-copy plasmid
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tseng, Y.M.; Harris, B.G.; Jacobson, M.K.
Isolation and characterization of yeast nicotinamide adenine dinucleotide kinase
Biochim. Biophys. Acta
568
205-214
1979
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shi, F.; Kawai, S.; Mori, S.; Kono, E.; Murata, K.
Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae
FEBS J.
272
3337-3349
2005
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Bieganowski, P.; Seidle, H.F.; Wojcik, M.; Brenner, C.
Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions
J. Biol. Chem.
281
22439-22445
2006
Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team