Information on EC 2.7.1.86 - NADH kinase:

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The expected taxonomic range for this enzyme is: Eukaryota

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EC NUMBERCOMMENTARY
2.7.1.86-

RECOMMENDED NAMEGeneOntology No.
NADH kinaseGO:0042736

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + NADH = ADP + NADPH
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
NAD/NADH phosphorylation and dephosphorylation-PWY-5083

SYSTEMATIC NAMEIUBMB Comments
ATP:NADH 2'-phosphotransferaseCTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing order of activity). The enzyme is specific for NADH. Activated by acetate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
ATP-NADH kinaseSaccharomyces cerevisiae-phosphorylates both NAD+ and NADH661696
ATP-NADH kinaseMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820, Mycobacterium tuberculosis--662376
ATP-NADH kinaseFusarium oxysporum--706568
ATP:NADH 2'-phosphotransferase----
ATP:NADH 2'-phosphotransferaseSaccharomyces cerevisiaeP32622-695829
ATP:NADH 2'-phosphotransferaseFusarium oxysporum--706568
ATP:NADH2 2'-phosphotransferase----
diphosphopyridine nucleotide (reduced) kinaseArabidopsis thaliana--657853
DPNH kinase----
kinase, reduced nicotinamide adenine dinucleotide (phosphorylating)----
MfnkMicrococcus flavus AKU 0502, Micrococcus flavus, Micrococcus flavus ICR 1820-exhibits polyphosphate- and ATP-dependent NADH kinase activities662376
NAD(H) kinaseArabidopsis thaliana--657853
NAD(H)KArabidopsis thalianaQ56YN3-676008
NADH kinase----
NADH kinaseEmericella nidulans--693998
NADH kinase POS5, mitochondrialSaccharomyces cerevisiae--674616
NADH2 kinase----
NADHKArabidopsis thaliana--657853
NADK-1Arabidopsis thalianaQ56YN3-676008
NADK1Arabidopsis thaliana-isoform691390
NADK3Arabidopsis thaliana--657853, 676516, 706395
nicotinamide adenine dinucleotide (reduced) kinaseArabidopsis thaliana--657853
Pos5Saccharomyces cerevisiae-; 674616
Pos5Saccharomyces cerevisiaeP32622-695829
Pos5pSaccharomyces cerevisiaeC7GJD6-691390
PpnkMycobacterium tuberculosis-exhibits polyphosphate- and ATP-dependent NADH kinase activities662376
reduced diphosphopyridine nucleotide kinase----
reduced nicotinamide adenine dinucleotide kinase (phosphorylating)----
Utr1Saccharomyces cerevisiaeQ06892-674616, 695829
YEF1Saccharomyces cerevisiae--661696, 674616, 695829
Yef1pSaccharomyces cerevisiae--661696
YEL041WSaccharomyces cerevisiae--674616

CAS REGISTRY NUMBERCOMMENTARY
62213-39-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thaliana-691390, 706395--Manually annotated by BRENDA team
Arabidopsis thaliana; first discovery in plants657853--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Col676516--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Ws-4676008Q56YN3SwissProtManually annotated by BRENDA team
Emericella nidulansstrain CBS 513.88 /FGSC A1513693998--Manually annotated by BRENDA team
Emericella nidulans CBS 513.88 /FGSC A1513strain CBS 513.88 /FGSC A1513693998--Manually annotated by BRENDA team
Fusarium oxysporumstrain F3706568--Manually annotated by BRENDA team
Fusarium oxysporum F3strain F3706568--Manually annotated by BRENDA team
Micrococcus flavus-662376--Manually annotated by BRENDA team
Mycobacterium tuberculosisstrain H37Rv662376--Manually annotated by BRENDA team
Pichia membranifaciens-642063--Manually annotated by BRENDA team
Saccharomyces cerevisiae-642062, 649040, 649041, 661696, 674616, 695829--Manually annotated by BRENDA team
Saccharomyces cerevisiae-674616, 695829Q06892SwissProtManually annotated by BRENDA team
Saccharomyces cerevisiae-691390C7GJD6UniProtManually annotated by BRENDA team
Saccharomyces cerevisiae-695829P32622SwissProtManually annotated by BRENDA team
Saccharomyces cerevisiaestrain X2181-1A642064, 642065, 642066--Manually annotated by BRENDA team
Saccharomyces cerevisiaestrain YPH925705593--Manually annotated by BRENDA team
Saccharomyces cerevisiae X2181-1Astrain X2181-1A642064, 642065, 642066--Manually annotated by BRENDA team
Saccharomyces cerevisiae YPH925strain YPH925705593--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
malfunctionSaccharomyces cerevisiae-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 mutations705593

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM 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
Saccharomyces cerevisiae--661696--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Saccharomyces cerevisiaeQ06892-674616--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Emericella nidulans--693998--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Arabidopsis thalianaQ56YN3-676008--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Saccharomyces cerevisiaeC7GJD6-691390--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Saccharomyces cerevisiae-2fold preference for NADH over NAD+649040-649040?
ATP + NAD+ADP + NADP+
show the reaction diagram
Saccharomyces cerevisiae-activity with NAD+ is 50fold lower than with NADH649041--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Arabidopsis thaliana-NADH is preferred 100fold over NAD+657853--?
ATP + NAD+ADP + NADP+
show the reaction diagram
Emericella nidulans-phenotypic effects during overexpression analyzed by simulation of major metabolic fluxes693998--?
ATP + NAD+ADP + NADH
show the reaction diagram
Saccharomyces cerevisiaeP32622-695829--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae--642064-642064?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae--642065-642065?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae--649041, 661696--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeQ06892-674616--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae--705593--?
ATP + NADHADP + NADPH
show the reaction diagram
Arabidopsis thaliana--676516--?
ATP + NADHADP + NADPH
show the reaction diagram
Mycobacterium tuberculosis, Micrococcus flavus--662376--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeP32622-695829--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-specific for NADH642062-642062?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-specific for NADH642066-642066?
ATP + NADHADP + NADPH
show the reaction diagram
Pichia membranifaciens-specific for NADH642063-642063?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-NAD+ completely ineffective642066-642066?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-2fold preference for NADH over NAD+649040-649040?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-may be involved in maintaining the level of triphosphopyridine nucleotide in the mitochondria642062-642062?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-the enzyme has primarily NADH kinase activity in mitochondria, mitochondrial NADPH is largely provided by the POS5 NADH kinase649041-649041?
ATP + NADHADP + NADPH
show the reaction diagram
Arabidopsis thaliana-preferentially phosphorylates reduced NAD+ but can use oxidized NAD+. ATP is preferred phophoryl donor but UTP, GTP, and CTP may substitute with lower activity, NADH is preferred 100fold over NAD+657853--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeQ06892phosphorylates NADH with 2% of the specific activity of its NAD kinase activity, possesses 33% activity with NADH and ATP compared to the activity obtained with NAD and ATP674616--?
ATP + NADHADP + NADPH
show the reaction diagram
Arabidopsis thalianaQ56YN3shows a 2fold preference for NADH over NAD+676008--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeQ06892Pos5 is responsible for all mitochondrial NAD/NADH kinase. Transitory exposure of Pos5 to the cytoplasm is required for the viability of utr1 mutants674616--?
ATP + NADHADP + NADPH
show the reaction diagram
Arabidopsis thaliana-isoform NADK1 shows 169% activity compared to NAD+691390--?
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeC7GJD6isoform Pos5p shows 167% activity compared to NAD+691390--?
ATP + NADHADP + NADPH
show the reaction diagram
Arabidopsis thaliana-prefers NADH as a substrate, but can also use NAD+ with a much lower efficiency706395--?
ATP + NADHADP + NADPH
show the reaction diagram
Fusarium oxysporum-uses NADH as the preferred diphosphonicotinamide nucleotide donor706568--?
ATP + NADHADP + NADPH
show the reaction diagram
Pichia membranifaciens H 112-specific for NADH642063-642063?
CTP + NADHCDP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-67% of activity with ATP642062--?
CTP + NADHCDP + NADPH
show the reaction diagram
Arabidopsis thaliana-ATP is preferred substrate657853--?
GTP + NADHGDP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-45% of activity with ATP642062--?
GTP + NADHGDP + NADPH
show the reaction diagram
Arabidopsis thaliana-ATP is preferred substrate657853--?
tetrapolyphosphate + NADHtripolyphosphate + NADPH
show the reaction diagram
Mycobacterium tuberculosis, Micrococcus flavus--662376--?
UTP + NADHUDP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-50% of activity with ATP642062--?
UTP + NADHUDP + NADPH
show the reaction diagram
Arabidopsis thaliana-ATP is preferred substrate657853--?
ITP + NADHIDP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-61% of activity with ATP642062--?
additional information?-Saccharomyces cerevisiae-POS5 NADH kinase is required for mitochondrial stability with a critical role in detoxification of reactive oxygen species649040---
additional information?-Arabidopsis thaliana-diphosphate or polyphosphate is not used as a phosphoryl donor, no substrate: diphosphate, polyphosphate657853---
additional information?-Saccharomyces cerevisiaeP32622NADH kinase does not increase the rate of xylose consumption695829---
additional information?-Saccharomyces cerevisiaeC7GJD6does not accept poly(P) as phosphoryl donor691390---
additional information?-Fusarium oxysporum-the purified enzyme presents almost no activity against NAD+706568---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
ATP + NAD+ADP + NADP+
show the reaction diagram
Emericella nidulans--693998--
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-may be involved in maintaining the level of triphosphopyridine nucleotide in the mitochondria642062-642062
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiae-the enzyme has primarily NADH kinase activity in mitochondria, mitochondrial NADPH is largely provided by the POS5 NADH kinase649041-649041
ATP + NADHADP + NADPH
show the reaction diagram
Saccharomyces cerevisiaeQ06892Pos5 is responsible for all mitochondrial NAD/NADH kinase. Transitory exposure of Pos5 to the cytoplasm is required for the viability of utr1 mutants674616--
additional information?-Saccharomyces cerevisiae-POS5 NADH kinase is required for mitochondrial stability with a critical role in detoxification of reactive oxygen species649040--
additional information?-Saccharomyces cerevisiaeP32622NADH kinase does not increase the rate of xylose consumption695829--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820, Mycobacterium tuberculosis--662376 2D-image
ATPSaccharomyces cerevisiae--661696, 674616, 695829, 705593 2D-image
ATPArabidopsis thaliana--676008, 676516, 706395 2D-image
ATPFusarium oxysporum--706568 2D-image
NAD+Saccharomyces cerevisiaeP32622; 695829 2D-image
NADHArabidopsis thaliana--691390 2D-image
NADHSaccharomyces cerevisiaeC7GJD6-691390 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Arabidopsis thaliana-8% of the activity with Mg2+; far less active than Mg2+ and Mn2+657853
Ca2+Saccharomyces cerevisiae-26% activity in the presence of 1mM Ca2+661696
Co2+Saccharomyces cerevisiae-32% activity in the presence of 1mM Co2+661696
K+Fusarium oxysporum-K+ is the only monovalent metal ion resulting higher NADH kinase activity by almost 1.5fold706568
Mg2+Saccharomyces cerevisiae-either Mn2+ or Mg2+ activate at low concentrations. Km: Km: 1.0 mM642062
Mg2+Arabidopsis thaliana-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; required, Km-value 1.16 mM657853
Mg2+Saccharomyces cerevisiae-100% activity in the presence of 1mM Mg2+661696
Mg2+Arabidopsis thalianaQ56YN3required for activity676008
Mn2+Saccharomyces cerevisiae-either Mn2+ or Mg2+ activate at low concentrations642062
Mn2+Arabidopsis thaliana-28% of the activity with Mg2+; Mn2+ can substitute for Mg2+ to stabilize the phosphoanhydride bonds of ATP but with only 28% of the activity657853
Zn2+Arabidopsis thaliana-4% of the activity with Mg2+; far less active than Mg2+ and Mn2+657853
Mn2+Saccharomyces cerevisiae-77% activity in the presence of 1mM Mn2+661696
additional informationSaccharomyces cerevisiae-no activity is detected in the presence of 1 mm Zn2+, Fe2+, Cu2+, Na+, and Li+661696
additional informationArabidopsis thalianaQ56YN3no significant increase in NAD(H) kinase activity is detected in the presence of Ca2+ /calmodulin676008

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3-acetyl-NAD+Saccharomyces cerevisiae-1 mM, 15% inhibition642066 2D-image
Ag2+Fusarium oxysporum-1 mM Ag+ lowers the activity to 3%706568 2D-image
ATPSaccharomyces cerevisiae-above 5 mM642062 2D-image
ATPSaccharomyces cerevisiae-above 6 mM642066 2D-image
beta-mercaptoethanolFusarium oxysporum-slightly inhibits NADH kinase706568 2D-image
Ca2+Fusarium oxysporum-no activity in the presence of 10 mM706568 2D-image
Cu2+Fusarium oxysporum-1 mM Cu2+ lowers the activity to 33%706568 2D-image
diphosphateArabidopsis thaliana-mixed inhibitor both to NADH and ATP657853 2D-image
eosin-5-maleimideSaccharomyces cerevisiae--642064 2D-image
Fe2+Fusarium oxysporum-no activity in the presence of 10 mM706568 2D-image
HgCl2Saccharomyces cerevisiae-13% residual activity at 0.1 mM, 6% residual activity at 0.25 mM661696 2D-image
iodoacetic acidSaccharomyces cerevisiae-5 mM, 87% inhibition, NADH protects642066 2D-image
Mg2+Saccharomyces cerevisiae-at 10 mM or above642062 2D-image
NADHSaccharomyces cerevisiae-slight inhibition661696 2D-image
NADP+Fusarium oxysporum-slightly inhibits NADH kinase706568 2D-image
NADPHSaccharomyces cerevisiae-slight inhibition661696 2D-image
NEMSaccharomyces cerevisiae-5 mM, 77% inhibition, NADH protects, ATP not642066 2D-image
p-chloromercuribenzoateArabidopsis thaliana-0.01 mM, 42% residual activity657853 2D-image
PCMBSaccharomyces cerevisiae--642064 2D-image
PCMBSaccharomyces cerevisiae-5 mM, 49% inhibition642066 2D-image
phosphoenolpyruvateSaccharomyces cerevisiae-20 mM, 63% inhibition, reconstituted enzyme. Solubilized enzyme is inhibited 55% by 30 mM642065 2D-image
phosphoenolpyruvateSaccharomyces cerevisiae-30 mM, 57% inhibition642066 2D-image
Zn2+Fusarium oxysporum-1 mM Zn2+ lowers the activity to 35%706568 2D-image
Mn2+Saccharomyces cerevisiae-at 1 mM or above642062 2D-image
additional informationFusarium oxysporum-NAD+ causes no inhibition of the enzyme706568-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
acetateSaccharomyces cerevisiae-high concentrations of carboxylic acid, e.g. acetate required for maximal activity642062 2D-image
acetateSaccharomyces cerevisiae-maximal enhancement of activity, about 7fold is observed with 100 mM acetate, enzyme reconstituted in liposomes, maximal enhancement of solubilized enzyme with 400 mM acetate642065 2D-image
acetateSaccharomyces cerevisiae-activates642066 2D-image
EGTAArabidopsis thalianaQ56YN30.5 mM676008 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.062-ATPArabidopsis thaliana-pH 7.9, 25°C; pH 7.9, 25°C, cosubstrate NADH657853 2D-image
0.133-ATPSaccharomyces cerevisiae-NADH kinase reconstituted in liposomes642065 2D-image
0.32-ATPMicrococcus flavus-wild type enzyme662376 2D-image
0.47-ATPMicrococcus flavus-mutant enzyme G183R662376 2D-image
1-ATPSaccharomyces cerevisiae-pH 7.8, 30°C, in presence of 0.2 M sodium acetate642062 2D-image
2.1-ATPSaccharomyces cerevisiae-solubilized enzyme form642065 2D-image
2.1-ATPSaccharomyces cerevisiae-pH 7.4, 30°C642066 2D-image
2.59-ATPFusarium oxysporum--706568 2D-image
0.759-CTPArabidopsis thaliana-pH 7.9, 25°C, cosubstrate NADH657853 2D-image
0.461-GTPArabidopsis thaliana-pH 7.9, 25°C, cosubstrate NADH657853 2D-image
2.39-NAD+Arabidopsis thaliana-pH 7.9, 25°C; pH 7.9, 25°C, the specificity constant (vmax/Km) for NADH is 100fold greater than for NAD+657853 2D-image
0.027-NADHSaccharomyces cerevisiae-NADH kinase reconstituted in liposomes642065 2D-image
0.042-NADHSaccharomyces cerevisiae-pH 7.8, 30°C, in presence of 0.2 M sodium acetate642062 2D-image
0.042-NADHArabidopsis thaliana-pH 7.9, 25°C; pH 7.9, 25°C, the specificity constant (vmax/Km) for NADH is 100fold greater than for NAD+657853 2D-image
0.105-NADHSaccharomyces cerevisiae-solubilized enzyme form642065 2D-image
0.105-NADHSaccharomyces cerevisiae-pH 7.4, 30°C642066 2D-image
0.13-NADHFusarium oxysporum--706568 2D-image
0.35-NADHMicrococcus flavus-with tetrapolyphosphate as the phosphate donor, wild type enzyme662376 2D-image
0.45-NADHMicrococcus flavus-with ATP as the phosphate donor, wild type enzyme662376 2D-image
0.72-NADHMicrococcus flavus-with tetrapolyphosphate as the phosphate donor, mutant enzyme G183R662376 2D-image
1.66-NADHMicrococcus flavus-with ATP as the phosphate donor, mutant enzyme G183R662376 2D-image
2-NADHSaccharomyces cerevisiae-in 100 mM Tris-HCl (pH 8.0) at 30°C661696 2D-image
0.58-TetrapolyphosphateMicrococcus flavus-wild type enzyme662376 2D-image
0.68-TetrapolyphosphateMicrococcus flavus-mutant enzyme G183R662376 2D-image
0.156-UTPArabidopsis thaliana-pH 7.9, 25°C, cosubstrate NADH657853 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.84-ATPFusarium oxysporum--706568 2D-image
0.95-NADHFusarium oxysporum--706568 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.078-Saccharomyces cerevisiae-cell extract, at 30°C661696
0.1-Saccharomyces cerevisiae-with GTP as phosphate donor674616
0.22-Mycobacterium tuberculosis-in the presence of 5 mM tetrapolyphosphate662376
0.279-Saccharomyces cerevisiae--642062
0.5-Saccharomyces cerevisiae-with CTP as phosphate donor674616
0.65-Mycobacterium tuberculosis-in the presence of 5 mM ATP662376
1.2-Saccharomyces cerevisiae-with ATP as phosphate donor674616
3.04-Micrococcus flavus-in the presence of 5 mM tetrapolyphosphate662376
3.4-Arabidopsis thalianaQ56YN3in the presence of 0.5 mM EGTA, using NAD+ as a substrate676008
5.75-Arabidopsis thalianaQ56YN3in the presence of 0.5 mM EGTA, using NADH as a substrate676008
8.66-Micrococcus flavus-in the presence of 5 mM ATP662376
9.475-Saccharomyces cerevisiae-after 122fold purification, at 30°C661696
15.1-Arabidopsis thaliana-NAD+ as substrate, pH 7.9, 25°C657853
15.6-Arabidopsis thaliana-pH 7.9, 25°C, substrate NAD+657853
40.1-Arabidopsis thaliana-NADH as susbtrate, pH 7.9, 25°C; pH 7.9, 25°C, substrate NADH657853
729-Saccharomyces cerevisiae--642066
additional information-Pichia membranifaciens, Pichia membranifaciens H 112-amplification of NADH without the influence of coexisting NAD+, by phosphorylating NADH into NADPH and putting this NAPH through an NADP+-NADPH cycling system642063
additional information-Emericella nidulans-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 activity693998
additional information-Fusarium oxysporum-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/mg706568

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.5-Fusarium oxysporum--706568
7.98.6Saccharomyces cerevisiae--642062
7.9-Arabidopsis thaliana--657853
8-Saccharomyces cerevisiae-NADH kinase reconstituted in liposomes642065
8.5-Saccharomyces cerevisiae--642066, 661696

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
6.29.9Saccharomyces cerevisiae-pH 6.2: about 35% of maximal activity, pH 9.9: about 50% of maximal activity642062
6.58.5Fusarium oxysporum-less than 30% of the peak activity is displayed in pH 6.5 and 8.5706568

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
45-Saccharomyces cerevisiae--661696
45-Fusarium oxysporum--706568

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.46-Saccharomyces cerevisiae-calculated from amino acid sequence661696
5.6-Fusarium oxysporum-isoelectric focusing706568

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
cell cultureArabidopsis thaliana--657853Manually annotated by BRENDA team
cell suspension cultureArabidopsis thaliana--657853Manually annotated by BRENDA team
flowerArabidopsis thaliana--676516Manually annotated by BRENDA team
leafArabidopsis thaliana--657853, 676008, 676516Manually annotated by BRENDA team
leafArabidopsis thaliana-restricted primarily to leaf vasculature706395Manually annotated by BRENDA team
rootArabidopsis thaliana--676516Manually annotated by BRENDA team
root primordiumArabidopsis thaliana-restricted to lateral root primordium706395Manually annotated by BRENDA team
siliqueArabidopsis thaliana--676516Manually annotated by BRENDA team
stemArabidopsis thaliana--676516Manually annotated by BRENDA team
vascular bundleArabidopsis thaliana-restricted primarily to leaf vasculature706395Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytoplasmSaccharomyces cerevisiae--5737674616Manually annotated by BRENDA team
cytoplasmArabidopsis thaliana--5737676516Manually annotated by BRENDA team
cytosolSaccharomyces cerevisiae--5829642062Manually annotated by BRENDA team
cytosolArabidopsis thaliana-putative5829657853Manually annotated by BRENDA team
cytosolSaccharomyces cerevisiaeP32622; 5829695829Manually annotated by BRENDA team
mitochondrionPichia membranifaciens, Pichia membranifaciens H 112--5739642063Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae-the enzyme is localized and functions at the intermembrane space side of the inner membrane5739642064Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae-localized exclusively in mitochondria5739642066Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae-enzyme functions exclusively in mitochondria5739649040Manually annotated by BRENDA team
peroxisomeArabidopsis thaliana-NADK3 localizes to the peroxisomal matrix via a novel type 1 peroxisomal targeting signal5777706395Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae--5739642062, 649041, 674616, 691390, 695829, 705593Manually annotated by BRENDA team
additional informationArabidopsis thaliana-not: mitochondrial-657853Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3afo, downloadSCOP (3afo)CATH (3afo)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
46000-Saccharomyces cerevisiaeC7GJD6-691390
49000-Emericella nidulans-predicted693998
55900-Saccharomyces cerevisiae-calculated from amino acid sequence661696
58000-Arabidopsis thalianaQ56YN3SDS-PAGE676008
58000-Arabidopsis thaliana-isoform NADK1691390
58250-Arabidopsis thalianaQ56YN3calculated from amino acid sequence676008
78000-Arabidopsis thaliana-gel filtration657853
156000-Fusarium oxysporum-gel filtration706568
160000-Saccharomyces cerevisiae-gel filtration642066
480000-Saccharomyces cerevisiae-gel filtration661696

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerArabidopsis thaliana-2 * 35000, SDS-PAGE657853
homodimerMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820--662376
homodimerFusarium oxysporum-2 * 72000, gel filtration706568
homooctamerSaccharomyces cerevisiae-8 * 60000, gel filtration661696
additional informationSaccharomyces cerevisiae-presence of 2 or more subunits of different size642066

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
5.5-Fusarium oxysporum-the enzyme is very unstable at pH values higher than 5.5706568

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
30-Pichia membranifaciens, Pichia membranifaciens H 112-10 min, stable642063
35-Pichia membranifaciens, Pichia membranifaciens H 112-10 min, 17% loss of activity642063
35-Saccharomyces cerevisiae-5 min, 35% loss of activity642066
40-Pichia membranifaciens, Pichia membranifaciens H 112-10 min, 40% loss of activity642063
50-Fusarium oxysporum-the enzyme retains 8% of the activity after 1 h at 50°C706568
54-Saccharomyces cerevisiae-half of its activity is lost on treatment at 54°C for 10 min661696
55-Saccharomyces cerevisiae-5 min, 95% loss of activity642066

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
ammonium sulfate, 0.2 M protects against denaturationSaccharomyces cerevisiae-642062

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. 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 moreSaccharomyces cerevisiae-642066
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 daysSaccharomyces cerevisiae-642066
4°C or -20°C, 95% loss of activity after overnight storageSaccharomyces cerevisiae-642062

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis thaliana-657853
HiTrap Chelating HP column chromatographyArabidopsis thalianaQ56YN3676008
Q-Sepharose column chromatography, Sephacryl S300 gel filtration, SP-Sepharose column chromatography, and t-butyl hydrophobic interaction column chromatographyFusarium oxysporum-706568
Butyl-Toyopearl 650M column chromatographyMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820, Mycobacterium tuberculosis-662376
-Saccharomyces cerevisiae-642062, 642066, 649040
; cobalt chelate affinity column chromatographySaccharomyces cerevisiae-674616
DEAE-Toyopearl column chromatography, Butyl-Toyopearl column chromatography, Ni-chelate AF Toyopearl column chromatographySaccharomyces cerevisiae-661696

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
a NADK3-GFP reporter fusion construct is expressed in Arabidopsis suspension-cultured cellsArabidopsis thaliana-706395
expressed in Escherichia coliArabidopsis thalianaQ56YN3676008
expression in Escherichia coliArabidopsis thaliana-657853
overexpressed in Aspergillus AR1 derived from the natural isolate A4, pTr04 expression vectorEmericella nidulans-693998
expressed in Escherichia coli BL21(DE3)pLysS cellsMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820, Mycobacterium tuberculosis-662376
expressed in Escherichia coli strain MK746 as a fusion recombinant protein with a V5 epitope and His6 tag at the C terminusSaccharomyces cerevisiae-661696
expressed in Escherichia coli; expression in Escherichia coli as N-terminally His-tagged fusionSaccharomyces cerevisiae-674616
overexpression in Escherichia coliSaccharomyces cerevisiae-649041
overproduction of the POS5 gene product in Escherichia coliSaccharomyces cerevisiae-649040

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
transcription of isoform NADK1 is upregulated by 3 and 8fold after treatment of plant cells with 5 mM H2O2 and irradiation, respectivelyArabidopsis thaliana-691390
NADK3 activity is first observed in stage 1.0-1.02, most notably in the procambium and vasculature of cotyledonsArabidopsis thaliana-706395
transcription of POS5 is upregulated 3.4fold after treatment for 10-12 min with 2.5 mM Cu2+Saccharomyces cerevisiaeC7GJD6691390

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
G183RMicrococcus flavus, Micrococcus flavus AKU 0502, Micrococcus flavus ICR 1820-mutant with partially retained NADH kinase activity662376

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisPichia membranifaciens, Pichia membranifaciens H 112-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 substrate642063

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
642062Griffiths, M.M.; Bernofsky, C.Purification and properties of reduced diphosphopyridine nucleotide kinase from yeast mitochondriaJ. Biol. Chem.2471473-14781972Saccharomyces cerevisiae PubMed
642063Ohno, T.; Suzuki, T.; Horiuchi, T.Specific amplification of NADH using NADH kinase in a reaction mixture containing excess NAD+Biosci. Biotechnol. Biochem.58976-9771994Pichia membranifaciens-
642064Iwahashi, Y.; Nakamura, T.Localization of the NADH kinase in the inner membrane of yeast mitochondriaJ. Biochem.105916-9211989Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A PubMed
642065Iwahashi, Y.; Nakamura, T.Orientation and reactivity of NADH kinase in proteoliposomesJ. Biochem.105922-9261989Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A PubMed
642066Iwahashi, Y.; Hitoshio, A.; Tajima, N.; Nakamura, T.Characterization of NADH kinase from Saccharomyces cerevisiaeJ. Biochem.105588-5931989Saccharomyces cerevisiae, Saccharomyces cerevisiae X2181-1A PubMed
649040Strand, 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 DNAEukaryot. Cell2809-8202003Saccharomyces cerevisiae PubMed
649041Outten, C.E.; Culotta, V.C.A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiaeEMBO J.222015-20242003Saccharomyces cerevisiae PubMed
657853Turner, 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.385217-2232005Arabidopsis thaliana PubMed
661696Shi, 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 cerevisiaeFEBS J.2723337-33492005Saccharomyces cerevisiae PubMed
662376Mori, S.; Kawai, S.; Shi, F.; Mikami, B.; Murata, K.Molecular conversion of NAD Kinase to NADH kinase through single amino acid residue substitutionJ. Biol. Chem.28024104-241122005Micrococcus flavus, Mycobacterium tuberculosis PubMed
674616Bieganowski, 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 functionsJ. Biol. Chem.28122439-224452006Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q06892) PubMed
676008Berrin, 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 thalianaMol. Genet. Genomics27310-192005Arabidopsis thaliana, Arabidopsis thaliana (Q56YN3) PubMed
676516Chai, 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 ArabidopsisPlant J.47665-6742006Arabidopsis thaliana PubMed
691390Kawai, 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.72919-9302008Arabidopsis thaliana, Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Saccharomyces cerevisiae (C7GKE4), Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae, Saccharomyces cerevisiae (C7GJD6) PubMed
693998Panagiotou, G.; Grotkjaer, T.; Hofmann, G.; Bapat, P.M.; Olsson, L.Overexpression of a novel endogenous NADH kinase in Aspergillus nidulans enhances growthMetab. Eng.1131-392008Emericella nidulans, Emericella nidulans CBS 513.88 /FGSC A1513 PubMed
695829Hou, J.; Vemuri, G.N.; Bao, X.; Olsson, L.Impact of overexpressing NADH kinase on glucose and xylose metabolism in recombinant xylose-utilizing Saccharomyces cerevisiaeAppl. Microbiol. Biotechnol.82909-9192009Saccharomyces cerevisiae, Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892) PubMed
705593Stuart, G.R.; Humble, M.M.; Strand, M.K.; Copeland, W.C.Transcriptional response to mitochondrial NADH kinase deficiency in Saccharomyces cerevisiaeMitochondrion9211-2212009Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH925 PubMed
706395Waller, 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 biosynthesisPlanta231305-3172010Arabidopsis thaliana PubMed
706568Panagiotou, 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 oxysporumProcess Biochem.431114-11202008Fusarium oxysporum, Fusarium oxysporum F3-

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.86)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)