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Information on EC 2.7.1.86 - NADH kinase
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2.7.1.86 NADH kinaseIUBMB Comments
CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). The enzyme is specific for NADH. Activated by acetate.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
nadh kinase, pos5p, atp-nadh kinase, atp:nadh 2'-phosphotransferase, nicotinamide adenine dinucleotide hydride kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP-NADH kinase
ATP:NADH 2'-phosphotransferase
ATP:NADH2 2'-phosphotransferase
-
-
-
-
DPNH kinase
-
-
-
-
EC 2.7.1.96
-
-
formerly
-
kinase, reduced nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
NADH kinase
NADH2 kinase
-
-
-
-
NADHK
NADK
nicotinamide adenine dinucleotide hydride kinase
Pos5
Pos5p
Posp5
Ppnk
reduced diphosphopyridine nucleotide kinase
-
-
-
-
reduced nicotinamide adenine dinucleotide kinase (phosphorylating)
-
-
-
-
Utr1
YEF1
ATP:NADH 2'-phosphotransferase
-
-
-
-
NADH kinase
-
-
-
-
Ppnk
-
exhibits polyphosphate- and ATP-dependent NADH kinase activities
Ppnk
-
exhibits polyphosphate- and ATP-dependent NADH kinase activities
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + NADH = ADP + NADPH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, ,
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SYSTEMATIC NAME
IUBMB Comments
ATP:NADH 2'-phosphotransferase
CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). The enzyme is specific for NADH. Activated by acetate.
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CAS REGISTRY NUMBER
COMMENTARY
62213-39-2
-
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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
ATP + NAD+
ADP + NADP+
-
phenotypic effects during overexpression analyzed by simulation of major metabolic fluxes
-
-
?
ATP + NAD+
ADP + NADP+
Aspergillus nidulans CBS 513.88 / FGSC A1513
-
phenotypic effects during overexpression analyzed by simulation of major metabolic fluxes
-
-
?
ATP + NAD+
ADP + NADP+
-
2fold preference for NADH over NAD+
-
?
ATP + NAD+
ADP + NADP+
-
activity with NAD+ is 50fold lower than with NADH
-
-
?
ATP + NAD+
ADP + NADP+
the enzyme has much higher NADH kinase than NAD kinase activity
-
-
?
ATP + NADH
ADP + NADPH
-
preferentially phosphorylates reduced NAD+ but can use oxidized NAD+. ATP is preferred phophoryl donor but UTP, GTP, and CTP may substitute with lower activity
-
-
?
ATP + NADH
ADP + NADPH
shows a 2fold preference for NADH over NAD+
-
-
?
ATP + NADH
ADP + NADPH
-
isoform NADK1 shows 169% activity compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
-
prefers NADH as a substrate, but can also use NAD+ with a much lower efficiency
-
-
?
ATP + NADH
ADP + NADPH
-
uses NADH as the preferred diphosphonicotinamide nucleotide donor
-
-
?
ATP + NADH
ADP + NADPH
-
uses NADH as the preferred diphosphonicotinamide nucleotide donor
-
-
?
ATP + NADH
ADP + NADPH
-
2fold preference for NADH over NAD+
-
?
ATP + NADH
ADP + NADPH
-
may be involved in maintaining the level of triphosphopyridine nucleotide in the mitochondria
-
?
ATP + NADH
ADP + NADPH
-
the enzyme has primarily NADH kinase activity in mitochondria, mitochondrial NADPH is largely provided by the POS5 NADH kinase
-
?
ATP + NADH
ADP + NADPH
phosphorylates NADH with 2% of the specific activity of its NAD kinase activity
-
-
?
ATP + NADH
ADP + NADPH
possesses 33% activity with NADH and ATP compared to the activity obtained with NAD and ATP
-
-
?
ATP + NADH
ADP + NADPH
Pos5 is responsible for all mitochondrial NAD/NADH kinase. Transitory exposure of Pos5 to the cytoplasm is required for the viability of utr1 mutants
-
-
?
ATP + NADH
ADP + NADPH
isoform Pos5p shows 167% activity compared to NAD+
-
-
?
ATP + NADH
ADP + NADPH
the enzyme has much higher NADH kinase than NAD kinase activity
-
-
?
ATP + NADH
ADP + NADPH
-
NAD+ completely ineffective
-
?
ATP + NADH
ADP + NADPH
the cytoplasmic NADH kinase is a primary source of the cytosolic NADPH
-
-
?
ATP + NADH
ADP + NADPH
the cytoplasmic NADH kinase is a primary source of the cytosolic NADPH
-
-
?
tetrapolyphosphate + NADH
tripolyphosphate + NADPH
-
-
-
-
?
additional information
?
-
-
diphosphate or polyphosphate is not used as a phosphoryl donor
-
-
?
additional information
?
-
-
no substrate: diphosphate, polyphosphate
-
-
?
additional information
?
-
-
the purified enzyme presents almost no activity against NAD+
-
-
?
additional information
?
-
-
the purified enzyme presents almost no activity against NAD+
-
-
?
additional information
?
-
-
POS5 NADH kinase is required for mitochondrial stability with a critical role in detoxification of reactive oxygen species
-
-
?
additional information
?
-
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
additional information
?
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
additional information
?
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
additional information
?
-
does not accept poly(P) as phosphoryl donor
-
-
?
additional information
?
-
enzyme additionally show NAD+ kinase activity, Km value for NAD+ is 0.5 mM
-
-
?
additional information
?
-
-
enzyme additionally show NAD+ kinase activity, Km value for NAD+ is 0.5 mM
-
-
?
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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 + NADH
ADP + NADPH
-
may be involved in maintaining the level of triphosphopyridine nucleotide in the mitochondria
-
?
ATP + NADH
ADP + NADPH
-
the enzyme has primarily NADH kinase activity in mitochondria, mitochondrial NADPH is largely provided by the POS5 NADH kinase
-
?
ATP + NADH
ADP + NADPH
Pos5 is responsible for all mitochondrial NAD/NADH kinase. Transitory exposure of Pos5 to the cytoplasm is required for the viability of utr1 mutants
-
-
?
ATP + NADH
ADP + NADPH
the cytoplasmic NADH kinase is a primary source of the cytosolic NADPH
-
-
?
ATP + NADH
ADP + NADPH
the cytoplasmic NADH kinase is a primary source of the cytosolic NADPH
-
-
?
additional information
?
-
-
POS5 NADH kinase is required for mitochondrial stability with a critical role in detoxification of reactive oxygen species
-
-
?
additional information
?
-
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
additional information
?
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
additional information
?
-
NADH kinase does not increase the rate of xylose consumption
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
-
K+ is the only monovalent metal ion resulting higher NADH kinase activity by almost 1.5fold
Mg2+
Mn2+
Zn2+
additional information
no significant increase in NAD(H) kinase activity is detected in the presence of Ca2+ /calmodulin
Mg2+
-
Mn2+ can substitute for Mg2+ to stabilize the phosphoanhydride bonds of ATP but with only 28% of the activity. Km-value Mg2+, 1.16 mM
Mg2+
-
either Mn2+ or Mg2+ activate at low concentrations. Km: Km: 1.0 mM
Mn2+
-
Mn2+ can substitute for Mg2+ to stabilize the phosphoanhydride bonds of ATP but with only 28% of the activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphoenolpyruvate
-
20 mM, 63% inhibition, reconstituted enzyme. Solubilized enzyme is inhibited 55% by 30 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetate
-
high concentrations of carboxylic acid, e.g. acetate required for maximal activity
acetate
-
maximal enhancement of activity, about 7fold is observed with 100 mM acetate, enzyme reconstituted in liposomes, maximal enhancement of solubilized enzyme with 400 mM acetate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypersensitivity
Deletion of the mitochondrial NADH kinase increases mitochondrial DNA stability and life span in the filamentous fungus Podospora anserina.
Mitochondrial Diseases
POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA.
nadh kinase deficiency
Transcriptional response to mitochondrial NADH kinase deficiency in Saccharomyces cerevisiae.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
ATP
pH and temperature not specified in the publication
1.3
NAD+
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
2.39
NAD+
-
pH 7.9, 25°C, the specificity constant (vmax/Km) for NADH is 100fold greater than for NAD+
4.5
NAD+
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
0.032
NADH
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
0.042
NADH
-
pH 7.9, 25°C, the specificity constant (vmax/Km) for NADH is 100fold greater than for NAD+
0.19
NADH
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
0.35
NADH
-
with tetrapolyphosphate as the phosphate donor, wild type enzyme
0.72
NADH
-
with tetrapolyphosphate as the phosphate donor, mutant enzyme G183R
2
NADH
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.2
NAD+
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
7.4
NAD+
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
7.7
NADH
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
16.1
NADH
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
NAD+
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
4.8
NAD+
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
85
NADH
wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C
241
NADH
mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40.1
additional information
additional information
-
gene encoding NADH kinase identified, overexpression using constitutive promoter, physiologcal effects in combination with different aeration rates in glucose batch fermentation, metabolite profiling, relative amounts of intracellular amino and non-amino organic acids compared, enzyme activity significantly correlated with growth activity
additional information
-
the crude extract shows a specific activity of 0.017 units/mg, the 65.62fold purified enzyme shows a specific activity of 1.11 units/mg
additional information
-
amplification of NADH without the influence of coexisting NAD+, by phosphorylating NADH into NADPH and putting this NAPH through an NADP+-NADPH cycling system
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 9.9
-
pH 6.2: about 35% of maximal activity, pH 9.9: about 50% of maximal activity
6.5 - 8.5
-
less than 30% of the peak activity is displayed in pH 6.5 and 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
NADK3 localizes to the peroxisomal matrix via a novel type 1 peroxisomal targeting signal
brenda
-
the enzyme is localized and functions at the intermembrane space side of the inner membrane
brenda
-
enzyme functions exclusively in mitochondria
brenda
-
the enzyme is localized and functions at the intermembrane space side of the inner membrane
-
brenda
-
localized exclusively in mitochondria
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
yeast cells lacking the mitochondrial NADH kinase encoded by POS5 display increased sensitivity to hydrogen peroxide, a slow-growth phenotype, reduced mitochondrial function and increased levels of mitochondrial protein oxidation and mitochondrial DNA mutations
malfunction
-
deletion of the POS5 gene results in respiratory deficiency, anti-oxidative dysfunction and arginine auxotrophy of cells, and the respiratory deficiency is fatal for mitochondrial function
malfunction
-
DELTApos5 mitochondria cannot efficiently synthesize Fe-S clusters on endogenous aconitase or imported ferredoxin
malfunction
-
deletion of the POS5 gene results in respiratory deficiency, anti-oxidative dysfunction and arginine auxotrophy of cells, and the respiratory deficiency is fatal for mitochondrial function
-
malfunction
-
DELTApos5 mitochondria cannot efficiently synthesize Fe-S clusters on endogenous aconitase or imported ferredoxin
-
malfunction
-
yeast cells lacking the mitochondrial NADH kinase encoded by POS5 display increased sensitivity to hydrogen peroxide, a slow-growth phenotype, reduced mitochondrial function and increased levels of mitochondrial protein oxidation and mitochondrial DNA mutations
-
physiological function
-
the enzyme contributes to the maintenance of respiratory chain complex activities
physiological function
-
the enzyme is required for efficient iron-sulfur cluster biogenesis in wild type mitochondria
physiological function
a triple mutant lacking the activities of ATP-NAD/NADH kinase Utr1, ATP-NADH kinase Pos5 and ATP-NADH kinase Yel041wp, i.e. Yef1, is viable and does not show growth defects. Presence of Utr1 protein is critical for growth in low iron medium
physiological function
the enzyme might have a role in waterlogging tolerance in legumes
physiological function
the enzyme might have a role in waterlogging tolerance in legumes
physiological function
-
the enzyme contributes to the maintenance of respiratory chain complex activities
-
physiological function
-
the enzyme is required for efficient iron-sulfur cluster biogenesis in wild type mitochondria
-
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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). POS5_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
386
0
43500
Swiss-Prot
Mitochondrion (Reliability: 2)
POS5_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
414
0
46247
Swiss-Prot
Mitochondrion (Reliability: 3)
NADHK_ARATH
317
0
34831
Swiss-Prot
other Location (Reliability: 4)
NADHK_ORYSJ
325
0
35517
Swiss-Prot
Mitochondrion (Reliability: 3)
NADK1_ARATH
524
0
58245
Swiss-Prot
other Location (Reliability: 2)
YEF1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
495
0
55874
Swiss-Prot
other Location (Reliability: 1)
A2R9N0_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
426
0
46336
TrEMBL
Mitochondrion (Reliability: 4)
B9T1K4_RICCO
313
0
34249
TrEMBL
other Location (Reliability: 3)
I7AYG7_9FABA
250
0
27511
TrEMBL
other Location (Reliability: 4)
B7P2M0_IXOSC
414
0
46465
TrEMBL
other Location (Reliability: 3)
A0A364N4X5_9PLEO
326
0
35642
TrEMBL
Mitochondrion (Reliability: 2)
A0A3G2S3B2_9BASI
388
0
43573
TrEMBL
other Location (Reliability: 4)
A0A0B2QLL1_GLYSO
508
0
56809
TrEMBL
other Location (Reliability: 4)
A0A0F4YJF9_TALEM
411
0
44579
TrEMBL
Mitochondrion (Reliability: 2)
B9RIE7_RICCO
532
0
59318
TrEMBL
other Location (Reliability: 5)
K0KC12_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
437
0
49132
TrEMBL
Mitochondrion (Reliability: 2)
B9WES7_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
530
0
57759
TrEMBL
Mitochondrion (Reliability: 4)
A0A0F8CYT2_CERFI
408
0
45361
TrEMBL
other Location (Reliability: 1)
C7GJD6_YEAS2
Saccharomyces cerevisiae (strain JAY291)
414
0
46273
TrEMBL
-
J9Z3N7_9FABA
522
0
58331
TrEMBL
Secretory Pathway (Reliability: 2)
UTR1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
530
0
59469
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homooctamer
additional information
additional information
-
presence of 2 or more subunits of different size
additional information
-
presence of 2 or more subunits of different size
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Pos5 complexed with NADH, sitting drop vapor diffusion method, using 15% (v/v) 2-methyl 2,4-pentanediol, 5% (w/v) polyethylene glycol 4000 and 100 mM imidazole-HCl, pH 8.0, at 20°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H231D
the mutant exhibits no activity towards NAD+ and low activity for NADH
R293H
the mutation reduces the ratio of NADH kinase activity to NAD kinase activity from 8.6 to 2.1
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, 20 mM Tris-HCl buffer, pH 7.8, 0.2 M ammonium sulfate, 20 mM MgCl2, 2 mM EDTA, stable for 1 month or more
-
0-5°C, 20 mM Tris-HCl buffer, pH 7.8, 0.2 M ammonium sulfate, 20 mM MgCl2, 2 mM EDTA, stable for 7 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Butyl-Toyopearl 650M column chromatography
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
Q-Sepharose column chromatography, Sephacryl S300 gel filtration, SP-Sepharose column chromatography, and t-butyl hydrophobic interaction column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a NADK3-GFP reporter fusion construct is expressed in Arabidopsis suspension-cultured cells
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)pLysS cells
expression in Escherichia coli as N-terminally His-tagged fusion
overexpressed in Aspergillus AR1 derived from the natural isolate A4, pTr04 expression vector
-
overpressed in Pichia pastoris, either directed to the cytosol or to the mitochondria. POS5 overexpression increases the NADPH/NADPx02 ratio in all the strains and under all conditions tested
-
pos5 is co-expressed with poly-3-hydroxybutyrate (PHB) synthetic operon phbCAB in Escherichia coli. The recombinant strain carrying pos5 and phbCAB co-expression plasmid reaches 5.96 g/l cell dry weight with 64.1% PHB accumulation in 72 h shake flask cultivation, while the control strain without pos5 yields 3.93 g/l cell dry weight with 58.5% PHB content
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
NADK3 activity is first observed in stage 1.0-1.02, most notably in the procambium and vasculature of cotyledons
-
transcript level is upregulated in response to waterlogging
transcription of isoform NADK1 is upregulated by 3 and 8fold after treatment of plant cells with 5 mM H2O2 and irradiation, respectively
-
transcription of POS5 is upregulated 3.4fold after treatment for 10-12 min with 2.5 mM Cu2+
transcript level is upregulated in response to waterlogging
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is useful for amplification of NADH in presence of excess NAD+ and is applicable to sensitive measurement of NAD+ dependent dehydrogenase or ist substrate
biotechnology
synthesis
biotechnology
NADH kinase can be employed as an effective metabolic manipulation target to improve poly-3-hydroxybutyrate synthesis
biotechnology
-
recombinant protein overproduction often results in oxidative stress, causing deviations from the optimal redox cofactor regeneration balance. This becomes one of the limiting factors in obtaining high levels of heterologous protein production. Overexpression of NADH kinase enzyme from Saccharomyces cerevisiae (Pos5) in the cytosol of Pichia pastoris results in a significant improvement in the production of the model protein
biotechnology
-
NADH kinase can be employed as an effective metabolic manipulation target to improve poly-3-hydroxybutyrate synthesis
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synthesis
NADH kinase can be employed as an effective metabolic manipulation target to improve poly-3-hydroxybutyrate synthesis
synthesis
-
NADH kinase can be employed as an effective metabolic manipulation target to improve poly-3-hydroxybutyrate synthesis
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Griffiths, M.M.; Bernofsky, C.
Purification and properties of reduced diphosphopyridine nucleotide kinase from yeast mitochondria
J. Biol. Chem.
247
1473-1478
1972
Saccharomyces cerevisiae
brenda
Ohno, T.; Suzuki, T.; Horiuchi, T.
Specific amplification of NADH using NADH kinase in a reaction mixture containing excess NAD+
Biosci. Biotechnol. Biochem.
58
976-977
1994
Pichia membranifaciens
-
brenda
Iwahashi, Y.; Nakamura, T.
Localization of the NADH kinase in the inner membrane of yeast mitochondria
J. Biochem.
105
916-921
1989
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
brenda
Iwahashi, Y.; Nakamura, T.
Orientation and reactivity of NADH kinase in proteoliposomes
J. Biochem.
105
922-926
1989
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
brenda
Iwahashi, Y.; Hitoshio, A.; Tajima, N.; Nakamura, T.
Characterization of NADH kinase from Saccharomyces cerevisiae
J. Biochem.
105
588-593
1989
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A
brenda
Strand, M.K.; Stuart, G.R.; Longley, M.J.; Graziewicz, M.A.; Dominick, O.C.; Copeland, W.C.
POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA
Eukaryot. Cell
2
809-820
2003
Saccharomyces cerevisiae
brenda
Outten, C.E.; Culotta, V.C.
A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
EMBO J.
22
2015-2024
2003
Saccharomyces cerevisiae
brenda
Turner, W.L.; Waller, J.C.; Snedden, W.A.
Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana (thale cress)
Biochem. J.
385
217-223
2005
Arabidopsis thaliana
brenda
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 (P21373), Saccharomyces cerevisiae
brenda
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
Micrococcus flavus, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
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, Saccharomyces cerevisiae (Q06892)
brenda
Berrin, J.; Brutesco, C.; Montillet, J.; Kazmaier, M.; Pierrugues, O.; Alonso, B.; Roby, D.
Stress induces the expression of AtNADK-1, a gene encoding a NAD(H) kinase in Arabidopsis thaliana
Mol. Genet. Genomics
273
10-19
2005
Arabidopsis thaliana (Q56YN3)
brenda
Chai, M.F.; Wei, P.C.; Chen, Q.J.; An, R.; Chen, J.; Yang, S.; Wang, X.C.
NADK3, a novel cytoplasmic source of NADPH, is required under conditions of oxidative stress and modulates abscisic acid responses in Arabidopsis
Plant J.
47
665-674
2006
Arabidopsis thaliana
brenda
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, Saccharomyces cerevisiae (C7GJD6)
brenda
Panagiotou, G.; Grotkjaer, T.; Hofmann, G.; Bapat, P.M.; Olsson, L.
Overexpression of a novel endogenous NADH kinase in Aspergillus nidulans enhances growth
Metab. Eng.
11
31-39
2008
Aspergillus nidulans, Aspergillus nidulans CBS 513.88 / FGSC A1513
brenda
Hou, J.; Vemuri, G.N.; Bao, X.; Olsson, L.
Impact of overexpressing NADH kinase on glucose and xylose metabolism in recombinant xylose-utilizing Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
82
909-919
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892)
brenda
Stuart, G.R.; Humble, M.M.; Strand, M.K.; Copeland, W.C.
Transcriptional response to mitochondrial NADH kinase deficiency in Saccharomyces cerevisiae
Mitochondrion
9
211-221
2009
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH925
brenda
Waller, J.C.; Dhanoa, P.K.; Schumann, U.; Mullen, R.T.; Snedden, W.A.
Subcellular and tissue localization of NAD kinases from Arabidopsis: compartmentalization of de novo NADP biosynthesis
Planta
231
305-317
2010
Arabidopsis thaliana
brenda
Panagiotou, G.; Papadakis, M.; Topakas, E.; Olsson, L.; Christakopoulos, P.
Identification of NADH kinase activity in filamentous fungi and structural modelling of the novel enzyme from Fusarium oxysporum
Process Biochem.
43
1114-1120
2008
Fusarium oxysporum, Fusarium oxysporum F3
-
brenda
Shi, F.; Li, Z.; Sun, M.; Li, Y.
Role of mitochondrial NADH kinase and NADPH supply in the respiratory chain activity of Saccharomyces cerevisiae
Acta Biochim. Biophys. Sin.
43
989-995
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda
Lee, W.H.; Kim, J.W.; Park, E.H.; Han, N.S.; Kim, M.D.; Seo, J.H.
Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli
Appl. Microbiol. Biotechnol.
97
1561-1569
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae CEN.PK2-1D
brenda
Lee, W.H.; Kim, M.D.; Jin, Y.S.; Seo, J.H.
Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation
Appl. Microbiol. Biotechnol.
97
2761-2772
2013
Saccharomyces cerevisiae
brenda
Pain, J.; Balamurali, M.M.; Dancis, A.; Pain, D.
Mitochondrial NADH kinase, Pos5p, is required for efficient iron-sulfur cluster biogenesis in Saccharomyces cerevisiae
J. Biol. Chem.
285
39409-39424
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Ando, T.; Ohashi, K.; Ochiai, A.; Mikami, B.; Kawai, S.; Murata, K.
Structural determinants of discrimination of NAD+ from NADH in yeast mitochondrial NADH kinase Pos5
J. Biol. Chem.
286
29984-29992
2011
Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae
brenda
Tomas-Gamisans, M.; Andrade, C.C.P.; Maresca, F.; Monforte, S.; Ferrer, P.; Albiol, J.
Redox engineering by ectopic overexpression of NADH kinase in recombinant Pichia pastoris (Komagataella phaffii) impact on cell physiology and recombinant production of secreted proteins
Appl. Environ. Microbiol.
86
e02038-19
2020
Saccharomyces cerevisiae
brenda
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
Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae ATCC 204508 (P32622), Saccharomyces cerevisiae ATCC 204508 (Q06892)
brenda
Hong, P.H.; Zhang, J.; Liu, X.J.; Tan, T.W.; Li, Z.J.
Effect of NADH kinase on poly-3-hydroxybutyrate production by recombinant Escherichia coli
J. Biosci. Bioeng.
122
685-688
2016
Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q06892)
brenda
Joshi, R.; Bhattacharya, P.; Sairam, R.; Sathee, L.; Chinnusamy, V.
Identification and characterization of NADH kinase-3 from a stress-tolerant wild mung bean species (Vigna luteola (Jacq.) Benth.) with a possible role in waterlogging tolerance
Plant Mol. Biol. Rep.
38
137-150
2020
Vigna radiata var. radiata (A0A1S3TKV1), Vigna luteola (J9Z3N7)
-
brenda
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Release 2023.1 (January 2023)
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