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Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Escherichia coli and UniProt Accession P0A7B3

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Escherichia coli
UNIPROT: P0A7B3 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
NAD+
=
ADP
+
NADP+
+
=
+
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
-
-
-
-
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
-
-
-
-
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 + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
CTP + NAD+
CDP + NADP+
show the reaction diagram
-
60% of activity with ATP
-
-
?
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
42% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
56% of activity with ATP
-
-
?
NAD+ + ATP
NADP+ + ADP
show the reaction diagram
-
-
-
-
?
TTP + NAD+
TDP + NADP+
show the reaction diagram
-
40% of maximal activity
-
-
?
UTP + NAD+
UDP + NADP+
show the reaction diagram
-
109% of the activity with ATP
-
-
?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
-
0.25 mM, 65% inhibition
NADH
-
0.01 mM, 61% inhibition
NADP+
-
0.1 mM, 21% inhibition
NADPH
-
0.01 mM, 76% inhibition
PCMB
-
0.25 mM, 67% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
ATP
pH and temperature not specified in the publication
2.5
NAD+
pH and temperature not specified in the publication
0.2 - 2.5
ATP
1.85 - 2
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
55
ATP
-
pH 7.0, 37°C
125
NAD+
-
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.45
-
pH 7.0, 37°C, wild-type, substrate ATP
12.86
-
pH 7.0, 37°C, wild-type, substrate NAD+
2.33
-
pH 7.0, 37°C, mutant R175G, substrate NAD+
2.68
-
pH 7.0, 37°C, mutant R175, substrate ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
Tris/HCl buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6.0: about 40% of maximal activity, pH 10.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 68
-
about 50% of maximal activity at 37°C and at 68°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
-
gel filtration
30000
-
6 * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 30000
homohexamer
6 x 30000
hexamer
-
6 * 30000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R175E
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175G
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175H
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175I
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175K
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175Q
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175T
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, stable
60
-
10 min, about 10% loss of activity
65
-
10 min, about 45% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
-
preparation of a superparamagnetic NAD kinase catalyst to synthesize NADP in vitro
synthesis
additional information
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawai, S.; Mori, S.; Mukai, T.; Hashimoto, W.; Murata, K.
Molecular characterization of Escherichia coli NAD kinase
Eur. J. Biochem.
268
4359-4365
2001
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Mori, S.; Kawai, S.; Shi, F.; Mikami, B.; Murata, K.
Molecular conversion of NAD Kinase to NADH kinase through single amino acid residue substitution
J. Biol. Chem.
280
24104-24112
2005
Escherichia coli, Micrococcus flavus
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
Shi, A.; Zhu, X.; Lu, J.; Zhang, X.; Ma, Y.
Activating transhydrogenase and NAD kinase in combination for improving isobutanol production
Metab. Eng.
16C
1-10
2012
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Liu, C.; Yang, Y.; Gao, H.; Bai, X.; Li, Z.
Preparation and enzymatic activity of Fe3O4-IDA-Ni/NAD kinase magnetic catalyst
Korean J. Chem. Engin.
37
475-481
2020
Escherichia coli, Escherichia coli JM109
-
Manually annotated by BRENDA team