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Information on EC 3.6.1.22 - NAD+ diphosphatase
for references in articles please use BRENDA:EC3.6.1.22
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.22 NAD+ diphosphatase
IUBMB Comments
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+.
The enzyme appears in viruses and cellular organisms
- 3.6.1.22
- 5'-nucleotidase
-
ectoenzyme
-
phosphatidylinositol-specific
- n-acetyl-beta-glucosaminidase
-
plasma-membrane
-
3.1.4.1
-
3.6.1.9
- synthesis
- medicine
showSynonyms
alkaline phosphodiesterase i, nadh pyrophosphatase, nad pyrophosphatase, atnudx19, nudx19, nad+ pyrophosphatase, nudix hydrolase 19, nadph pyrophosphohydrolase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
msm1946
MSMEG_1946
NAD diphosphatase
-
-
-
-
NAD pyrophosphatase
-
-
-
-
NAD+ diphosphatase
-
-
-
-
NAD+ pyrophosphatase
-
-
-
-
NADH pyrophosphatase
NADP pyrophosphatase
-
-
-
-
NudC
NUDX7
UshA
NADH pyrophosphatase
-
-
-
-
NADH pyrophosphatase
-
growth factor gene 1 (GFG1, At4g12720) encodes a nudix hydrolase, that is an NADH pyrophosphatase and ADP-ribose pyrophosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD(H) + H2O = AMP + NMN(H)
-
-
-
-
NADH + H2O = AMP + NMNH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
NAD salvage (plants), NAD salvage pathway I (PNC VI cycle), NAD salvage pathway II (PNC IV cycle), NAD salvage pathway III (to nicotinamide riboside)
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SYSTEMATIC NAME
IUBMB Comments
NAD+ phosphohydrolase
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+.
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CAS REGISTRY NUMBER
COMMENTARY
37289-33-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ethionamide-NAD+ + H2O
ethionamide-NMNH + AMP
Substrates: -
Products: -
Products: -
?
isoniazid-NAD+ + H2O
isoniazid-NMNH + AMP
Substrates: -
Products: -
Products: -
?
thymidine 5'-p-nitrophenylphosphate + H2O
thymidine + 4-nitrophenyl phosphate
-
Substrates: -
Products: -
Products: -
?
NAD+ + H2O
AMP + NMN
-
Substrates: GFG1 transcript levels are rapidly and transiently induced during both biotic stresses imposed by avirulent pathogens and abiotic stresses like ozone and osmoticum.T-DNA knock out plants of GFG1 gene, gfg1-1, exhibit pleiotropic phenotypes such as reduced size, increased levels of reactive oxygen species and NADH, microscopic cell death, constitutive expression of pathogenesis-related genes and enhanced resistance to bacterial pathogens
Products: -
Products: -
?
NAD+ + H2O
AMP + NMN
-
Substrates: the enzyme is involved in NAD+ homeostasis
Products: -
Products: -
?
NAD+ + H2O
NMN + AMP
Substrates: weak substrate
Products: -
Products: -
?
NAD+ + H2O
NMN + AMP
Substrates: weak substrate
Products: -
Products: -
?
NAD+ + H2O
NMN + AMP
Substrates: weak substrate
Products: -
Products: -
?
NAD+ + H2O
NMN + AMP
-
Substrates: enzyme of the pyridine-nucleotide cycle, involved in nicotine production
Products: -
Products: -
ir
NAD+ + H2O
NMN + AMP
-
Substrates: -
Products: -
Products: -
ir
NAD+ + H2O
NMN + AMP
-
Substrates: possible function in NAD transport
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
Substrates: highest activity with NADH
Products: -
Products: -
?
NADH + H2O
NMNH + AMP
Substrates: highest activity with NADH
Products: -
Products: -
?
NADH + H2O
NMNH + AMP
Substrates: highest activity with NADH
Products: -
Products: -
?
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
Substrates: -
Products: -
Products: -
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
-
Substrates: possible function in regulation of NADP-level
Products: -
Products: -
?
NMN + H2O
nicotinamide riboside + phosphate
Substrates: -
Products: -
Products: -
?
NMN + H2O
nicotinamide riboside + phosphate
Substrates: -
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: AtNUDX19 catalyzes the hydrolysis of NADPH, but not NADH, in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in NAD uptake and processing to nicotinamide riboside
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + H2O
AMP + NMN
-
Substrates: GFG1 transcript levels are rapidly and transiently induced during both biotic stresses imposed by avirulent pathogens and abiotic stresses like ozone and osmoticum.T-DNA knock out plants of GFG1 gene, gfg1-1, exhibit pleiotropic phenotypes such as reduced size, increased levels of reactive oxygen species and NADH, microscopic cell death, constitutive expression of pathogenesis-related genes and enhanced resistance to bacterial pathogens
Products: -
Products: -
?
NAD+ + H2O
AMP + NMN
-
Substrates: the enzyme is involved in NAD+ homeostasis
Products: -
Products: -
?
NAD+ + H2O
NMN + AMP
-
Substrates: enzyme of the pyridine-nucleotide cycle, involved in nicotine production
Products: -
Products: -
ir
NAD+ + H2O
NMN + AMP
-
Substrates: possible function in NAD transport
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADH + H2O
NMNH + AMP
-
Substrates: possible function in regulation of NAD+/NADH-ratio
Products: -
Products: -
ir
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
Substrates: -
Products: -
Products: -
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
-
Substrates: possible function in regulation of NADP-level
Products: -
Products: -
?
additional information
?
-
Substrates: AtNUDX19 catalyzes the hydrolysis of NADPH, but not NADH, in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in NAD uptake and processing to nicotinamide riboside
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mg2+
Mn2+
Fe2+
the enzyme shows some activity on NADH in the presence of Fe2+
Mn2+
-
slight activation at concentration of 1.0 mM, reactivation of EDTA-treated enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
40% inhibition of the purified enzyme at concentration of 0.33 mM, activity in crude extract not affected
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Glucocorticoid hormones increase the activity of plasma membrane alkaline phosphodiesterase I in rat hepatoma cells.
Carcinoma, Hepatocellular
Stimulation of alkaline phosphodiesterase I activity by glucocorticoids in rat hepatoma cells [proceedings]
Cholestasis, Extrahepatic
Plasma alkaline phosphodiesterase I in intrahepatic cholestasis induced by alpha-naphthylisothiocyanate in rats.
Cholestasis, Intrahepatic
Plasma alkaline phosphodiesterase I in intrahepatic cholestasis induced by alpha-naphthylisothiocyanate in rats.
Herpes Simplex
Alkaline phosphodiesterase I and alkaline phosphatase I in plasma membranes of herpes simplex virus type 1 transformed hamster cells.
Infections
Is a NAD pyrophosphatase activity necessary for Haemophilus influenzae type b multiplication in the blood stream?
Infections
Macrophage activation measured by changes in 5'-nucleotidase and alkaline phosphodiesterase I activities after infection of newborn and juvenile guinea pigs with mycobacterium microti.
Neoplasms
Alkaline phosphodiesterase I release from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. III. The release from tumor cells.
Neoplasms
Characterization and control of expression of cell surface alkaline phosphodiesterase I activity in rat mesangial glomerular cells.
Neoplasms
Stimulatory effects of purified macrophage colony-stimulating factor on murine resident peritoneal macrophages.
Neoplasms
Tumor-associated macrophages of mouse mammary tumors. II. Differential distribution of macrophages from metastatic and nonmetastatic tumors.
Neurofibromatoses
Characterization of over-expressed alkaline phosphodiesterase I in tumour-derived fibroblasts from patients with neurofibromatosis.
Neurofibromatoses
Increase in alkaline phosphodiesterase I activity of tumor-derived cultured fibroblasts from neurofibromatosis patients.
Neurofibromatoses
Nicotinamide-induced activity of alkaline phosphodiesterase I toward tumor-derived cultured cells from neurofibromatosis patients.
Plasmacytoma
Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1.
Sarcoma
A pyrophosphatase which degrades NAD+ is located on the external surface of cultured fibroblasts: evidence that NAD+ is not extruded during treatment with N-methyl-N'-nitro-N-nitrosoguanidine.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
NAD+
-
100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.29
-
activity of inner membrane fraction
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
enzyme activity rapidly decreases below pH 7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
40% of maximum activity at pH 7.5, 60% of maximum activity at pH 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
enzyme activity rapidly decreases below 35°C or above 45°C
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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
-
more than 95% of membrane bound activity located at inner membrane
-
brenda
additional information
AtNUDX19 is targeted to both chloroplasts and peroxisomes
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
structure and phylogenetic tree of AtNUDX19-type (SQPWP) enzymes, structure of subgroup I (including AtNUDX19) and II
malfunction
physiological function
additional information
malfunction
deletion of the NADH pyrophosphatase gene nudC results in increased susceptibility to isoniazid and ethionamide
malfunction
the msm1946-NADH pyrophosphatase mutant shows increased killing rate during exposure to isozianide and ethionamide (INH and ETH) as compared to wild-type. The msm1946::Tn transposon mutant grows indistinguishably from wild-type bacteria in standard 7H9 liquid medium. The ability of the mutant cells to form colonies on standard LB solid medium is also indistinguishable from wild-type cells. The impact of msm1946 disruption on drug-mediated killing is found to be specific to INH and ETH. Elevated levels of NADH in the msm1946::Tn mutant can contribute to enhanced formation of the INH-NAD adduct
malfunction
nudx19 mutants accumulate salicylic acid and show high sensitivity to the hormone. Physiological role of AtNUDX19 using its loss-of-function mutants. NADPH levels are increased in nudx19 mutants under both normal and high light conditions, while NADP+ and NAD+ levels are decreased. Despite the high redox states of NADP(H), nudx19 mutants exhibit high tolerance to moderate light- or methylviologen-induced photooxidative stresses. The tolerance of nudx19 mutants to photooxidative stress is due to an enhancement in photosynthesis, increase in antioxidant capacity, and/or modulation of the expression of defense genes through changes in the levels and redox states of NAD(P), phenotypes, overview. AtNUDX19 acts as a negative regulator of SA synthesis. In contrast, KO- and KD-nudx19 plants are slightly insensitive to jasmonic acid methyl (MeJA) and abscisic acid (ABA). This might be explained by the fact that SA acts as an antagonist of these hormones. The expression of AtNUDX19 is also responsive to treatments with these hormones
malfunction
-
the msm1946-NADH pyrophosphatase mutant shows increased killing rate during exposure to isozianide and ethionamide (INH and ETH) as compared to wild-type. The msm1946::Tn transposon mutant grows indistinguishably from wild-type bacteria in standard 7H9 liquid medium. The ability of the mutant cells to form colonies on standard LB solid medium is also indistinguishable from wild-type cells. The impact of msm1946 disruption on drug-mediated killing is found to be specific to INH and ETH. Elevated levels of NADH in the msm1946::Tn mutant can contribute to enhanced formation of the INH-NAD adduct
-
malfunction
-
the msm1946-NADH pyrophosphatase mutant shows increased killing rate during exposure to isozianide and ethionamide (INH and ETH) as compared to wild-type. The msm1946::Tn transposon mutant grows indistinguishably from wild-type bacteria in standard 7H9 liquid medium. The ability of the mutant cells to form colonies on standard LB solid medium is also indistinguishable from wild-type cells. The impact of msm1946 disruption on drug-mediated killing is found to be specific to INH and ETH. Elevated levels of NADH in the msm1946::Tn mutant can contribute to enhanced formation of the INH-NAD adduct
-
physiological function
NADH pyrophosphatase NudC plays an important role in the inactivation of isoniazid and ethionamide
physiological function
deletion of the UshA gene leads to faster cell growth and improves extracellular NAD stability by 3fold under conditions similar to whole-cell biocatalysis
physiological function
mycobacterial NADH diphosphatase isoforms play an important role for the mechanism of isoniazid (INH) and ethionamide activation. INH has been one of the most effective and widely used antitubercular drugs, it is a pro-drug that is oxidatively activated in vivo by the katG-encoded mycobacterial catalase-peroxidase to generate covalently modified INH-NAD adduct. INH-NAD adduct inhibits InhA, an enoyl reductase that is a member of the type II dissociated fatty acid biosynthesis pathway. INH interferes with the biosynthesis of mycolic acids, the very long chain fatty acid components of the mycobacterial cell wall
physiological function
Arabidopsis Nudix hydrolase, AtNUDX19, has NADPH hydrolytic activity in vitro and is a regulator of the NADPH status. Role of ANUDX19 in regulation of the salicylic acid response in a negative manner. ANUDX19 acts as an NADPH diphosphohydrolase to modulate cellular levels and redox states of pyridine nucleotides and fine-tunes photooxidative stress response through the regulation of photosynthesis, antioxidant system, /and possibly hormonal signaling. The redox states of NADP(H) are crucial for regulating both ROS production and scavenging in chloroplasts. AtNUDX19 regulates NADPH levels and activity of enzymes involved in the NADPH production in Arabidopsis thaliana leaves and roots. AtNUDX19 catalyzes the hydrolysis of NADPH, but not NADH, in vivo and has significant impacts on the cellular levels and redox states of pyridine nucleotides
physiological function
overexpression of NUDX7 in Arabidopsis thaliana accelerates flowering and reduces inflorescence height. In Arabidopsis thaliana and maize lines with high, medium and low overexpression levels of the NUDX7 gene, the constitutive overexpression of NUDX7 gene does not improve tolerance to mild drought stress, while knocking down NUDX7 expression does, however at the expense of general growth under normal conditions
physiological function
-
overexpression of NUDX7 in Arabidopsis thaliana accelerates flowering and reduces inflorescence height. In Arabidopsis thaliana and maize lines with high, medium and low overexpression levels of the NUDX7 gene, the constitutive overexpression of NUDX7 gene does not improve tolerance to mild drought stress, while knocking down NUDX7 expression does, however at the expense of general growth under normal conditions
-
physiological function
-
mycobacterial NADH diphosphatase isoforms play an important role for the mechanism of isoniazid (INH) and ethionamide activation. INH has been one of the most effective and widely used antitubercular drugs, it is a pro-drug that is oxidatively activated in vivo by the katG-encoded mycobacterial catalase-peroxidase to generate covalently modified INH-NAD adduct. INH-NAD adduct inhibits InhA, an enoyl reductase that is a member of the type II dissociated fatty acid biosynthesis pathway. INH interferes with the biosynthesis of mycolic acids, the very long chain fatty acid components of the mycobacterial cell wall
-
physiological function
-
mycobacterial NADH diphosphatase isoforms play an important role for the mechanism of isoniazid (INH) and ethionamide activation. INH has been one of the most effective and widely used antitubercular drugs, it is a pro-drug that is oxidatively activated in vivo by the katG-encoded mycobacterial catalase-peroxidase to generate covalently modified INH-NAD adduct. INH-NAD adduct inhibits InhA, an enoyl reductase that is a member of the type II dissociated fatty acid biosynthesis pathway. INH interferes with the biosynthesis of mycolic acids, the very long chain fatty acid components of the mycobacterial cell wall
-
physiological function
-
deletion of the UshA gene leads to faster cell growth and improves extracellular NAD stability by 3fold under conditions similar to whole-cell biocatalysis
-
additional information
insights on isoniazid killing mechanism by microfluidics and automated time-lapse microscopy single-cell analysis, overview
additional information
-
insights on isoniazid killing mechanism by microfluidics and automated time-lapse microscopy single-cell analysis, overview
additional information
-
insights on isoniazid killing mechanism by microfluidics and automated time-lapse microscopy single-cell analysis, overview
-
additional information
-
insights on isoniazid killing mechanism by microfluidics and automated time-lapse microscopy single-cell analysis, overview
-
Show AA Sequence and Transmembrane Helices (12904 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
-
gel filtration, Sephadex G-150
51000
1 * 51000, purified recombinant NudC (fused with Trx tag), calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
AtNUDX19 has the NUDIX, NUDIX-like, and zf-NADH-PPase domains, and the Nudix and SQPWPFPxS motifs, structure of AtNUDX19-type (SQPWP) enzymes, structure of subgroup I (including AtNUDX19) and II
monomer
1 * 51000, purified recombinant NudC (fused with Trx tag), calculated from amino acid sequence
monomer
-
1 * 51000, purified recombinant NudC (fused with Trx tag), calculated from amino acid sequence
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
protein has a potential peroxisomal targeting signal
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H149E
mutation leads to electrostatic repulsion with the O?of the phosphate bond on NADH, enhancing the activity
H149E
-
mutation leads to electrostatic repulsion with the O?of the phosphate bond on NADH, enhancing the activity
-
P237Q
additional information
P237Q
the mutation prevents dimer formation, and results in a loss of enzymatic activity
P237Q
-
the mutation prevents dimer formation, and results in a loss of enzymatic activity
-
P237Q
the mutation prevents dimer formation, and results in a loss of enzymatic activity
additional information
construction of AtNUDX19 mutants, Arabidopsis lines SALK_115339 and SALK_135053 containing a T-DNA insert in the AtNUDX19 gene, physiological function analysis. Neither transcript nor protein of AtNUDX19 is detected in the homozygous SALK_135053 line, and very low levels of the AtNUDX19 transcript and protein are observed in the homozygous SALK_115339 line. Thus, the SALK_135053 and SALK_115339 lines are knockout (KO-nudx19) and knockdown (KD-nudx19) mutants of this gene, respectively. The growth of the mutants is similar to that of wild-type plants under normal growth conditions. The ratio of NADPH to total NADP(H) in KD- and KO-nudx19 plants is approximately 2fold higher than that in wild type under both conditions. The lack of AtNUDX19 had no impact on NADH levels. Under normal light intensity, there is also no difference in NAD+ levels between wild-type and mutant plants. Although NAD+ levels are increased in response to high light in wild type, this increase is almost completely inhibits in the nudx19 mutants, which increases the ratio of NADH to total NAD(H). Tolerance of nudx19 mutants to photooxidative stress, phenotypes. The tolerance of nudx19 mutants to photooxidative stress is due to an enhancement in photosynthesis, increase in antioxidant capacity, and/or modulation of the expression of defense genes through changes in the levels and redox states of NAD(P). Effects of AtNUDX19-disruption on nuclear gene expression, overview
additional information
construction of the Mycobacterium smegmatis msm1946::Tn transposon mutant, single-cell analysis for isoniazid-treated mutant msm1946-NADH pyrophosphatase using microfluidics and automated time-lapse microscopy
additional information
-
construction of the Mycobacterium smegmatis msm1946::Tn transposon mutant, single-cell analysis for isoniazid-treated mutant msm1946-NADH pyrophosphatase using microfluidics and automated time-lapse microscopy
additional information
-
construction of the Mycobacterium smegmatis msm1946::Tn transposon mutant, single-cell analysis for isoniazid-treated mutant msm1946-NADH pyrophosphatase using microfluidics and automated time-lapse microscopy
-
additional information
-
construction of the Mycobacterium smegmatis msm1946::Tn transposon mutant, single-cell analysis for isoniazid-treated mutant msm1946-NADH pyrophosphatase using microfluidics and automated time-lapse microscopy
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
half-life of WT, R148A, H149E and mutant R148A/H149E are 8 h, 10.9 h, 54 h, and 53.2 h, respectively
50
half-life of WT, R148A, H149E and mutant R148A/H149E are 4.8 min, 6.8 min, 14.1 min, and 17.5 min, respectively
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA, 5h, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography and Superdex 200 gel filtration
purification of gene product from Escherichia coli
nickel affinity column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells and in Mycobacterium smegmatis strain mc2155
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
medicine
-
enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
synthesis
agriculture
overexpression of NUDX7 in Arabidopsis thaliana accelerates flowering and reduces inflorescence height. In Arabidopsis thaliana and maize lines with high, medium and low overexpression levels of the NUDX7 gene, the constitutive overexpression of NUDX7 gene does not improve tolerance to mild drought stress, while knocking down NUDX7 expression does, however at the expense of general growth under normal conditions
agriculture
-
overexpression of NUDX7 in Arabidopsis thaliana accelerates flowering and reduces inflorescence height. In Arabidopsis thaliana and maize lines with high, medium and low overexpression levels of the NUDX7 gene, the constitutive overexpression of NUDX7 gene does not improve tolerance to mild drought stress, while knocking down NUDX7 expression does, however at the expense of general growth under normal conditions
-
synthesis
production of NMNH by mutant R148A/H149E reaches 33.0 U/ml in a 7 l fermenter, i.e. 16.65 g/l
synthesis
-
production of NMNH by mutant R148A/H149E reaches 33.0 U/ml in a 7 l fermenter, i.e. 16.65 g/l
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wagner, R.; Feth, F.; Wagner, K.G.
The pyridine-nucleotide cycle in tobacco. Enzyme activities for the recycling of NAD
Planta
167
226-232
1986
Nicotiana tabacum
brenda
Wagner, R.; Feth, F.; Wagner, K.G.
Regulation in tobacco callus of enzyme activities of the nicotine pathway II. The pyridine-nucleotide cycle
Planta
168
408-413
1986
Nicotiana tabacum
brenda
Foster, J.W.
Pyridine nucleotide cycle of Salmonella typhimurium: in vitro demonstration of nicotinamide adenine dinucleotide glycohydrolase, nicotinamide mononucleotide glycohydrolase, and nicotinamide adenine dinucleotide pyrophosphatase activities
J. Bacteriol.
145
1002-1009
1981
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Anderson, B.M.; Lang, C.A.
Nicotinamide-adenin dinucleotide pyrophosphatase in the growing and aging mosquito
Biochem. J.
101
392-396
1966
Aedes aegypti
brenda
Nakajima, Y.; Fukunaga, N.; Sasaki, S.; Usami, S.
Purification and properties of NADP pyrophosphatase from Proteus vulgaris
Biochim. Biophys. Acta
293
242-255
1973
Proteus vulgaris
brenda
Jeck, R.; Heik, P.; Woenckhaus, C.
Simple methods of preparing nicotinamide mononucleotide
FEBS Lett.
42
161-164
1974
Solanum tuberosum
brenda
Davies, R.; King, H.K.
An enzyme degrading reduced nicotinamide-adenine dinucleotide in Proteus vulgaris
Biochem. J.
175
669-674
1978
Proteus vulgaris
brenda
Berghaeuser, J.; Jeck, R.; Pfeiffer, M.
A simple preparation of an enzyme reactor producing nicotinamidemononucleotide
Biotechnol. Lett.
3
339-344
1981
Solanum tuberosum
-
brenda
Falconer, D.F.; Spector, M.P.; Foster, J.W.
Membrane association of NAD pyrophosphatase in Salmonella typhimurium
Curr. Microbiol.
10
237-242
1984
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Frick, D.N.; Bessman, M.J.
Cloning, purification, and properties of a novel NADH pyrophosphatase
J. Biol. Chem.
270
1529-1534
1995
Escherichia coli
brenda
Hagen, T.; Ziegler, M.
Detection and identification of NAD-catabolizing activities in rat tissue homogenates
Biochim. Biophys. Acta
1340
7-12
1997
Rattus norvegicus
brenda
Xu, W.; Dunn, C.A.; Bessman, M.J.
Cloning and characterization of the NADH pyrophospatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a nudix hydrolase subfamily
Biochem. Biophys. Res. Commun.
273
753-758
2000
Caenorhabditis elegans, Escherichia coli, Saccharomyces cerevisiae
brenda
AbdelRaheim, S.R.; Cartwright, J.L.; Gasmi, L.; McLennan, A.G.
The NADH diphosphatase encoded by the Saccharomyces cerevisiae NPY1 nudix hydrolase gene is located in peroxisomes
Arch. Biochem. Biophys.
388
18-24
2001
Saccharomyces cerevisiae (P53164)
brenda
Schmidt-Brauns, J.; Herbert, M.; Kemmer, G.; Kraiss, A.; Schlor, S.; Reidl, J.
Is a NAD pyrophosphatase activity necessary for Haemophilus influenzae type b multiplication in the blood stream?
Int. J. Med. Microbiol.
291
219-225
2001
Haemophilus influenzae
brenda
Bortell, R.; Moss, J.; McKenna, R.C.; Rigby, M.R.; Niedzwiecki, D.; Stevens, L.A.; Patton, W.A.; Mordes, J.P.; Greiner, D.L.; Rossini, A.A.
Nicotinamide adenine dinucleotide (NAD) and its metabolites inhibit T lymphocyte proliferation: role of cell surface NAD glycohydrolase and pyrophosphatase activities
J. Immunol.
167
2049-2059
2001
Rattus norvegicus
brenda
Magni, G.; Amici, A.; Emanuelli, M.; Orsomando, G.; Raffaelli, N.; Ruggieri, S.
Enzymology of NAD+ homeostasis in man
Cell. Mol. Life Sci.
61
19-34
2004
Homo sapiens
brenda
Jambunathan, N.; Mahalingam, R.
Analysis of Arabidopsis growth factor gene 1 (GFG1) encoding a nudix hydrolase during oxidative signaling
Planta
224
1-11
2006
Arabidopsis sp.
brenda
Wang, X.D.; Gu, J.; Wang, T.; Bi, L.J.; Zhang, Z.P.; Cui, Z.Q.; Wei, H.P.; Deng, J.Y.; Zhang, X.E.
Comparative analysis of mycobacterial NADH pyrophosphatase isoforms reveals a novel mechanism for isoniazid and ethionamide inactivation
Mol. Microbiol.
82
1375-1391
2011
Mycobacterium tuberculosis (P9WIX5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIX5), Mycobacterium tuberculosis variant bovis (C1AGW8)
brenda
Wang, L.; Zhou, Y.J.; Ji, D.; Lin, X.; Liu, Y.; Zhang, Y.; Liu, W.; Zhao, Z.K.
Identification of UshA as a major enzyme for NAD degradation in Escherichia coli
Enzyme Microb. Technol.
58-59
75-79
2014
Escherichia coli (B1XCS0), Escherichia coli DH10B (B1XCS0)
brenda
Njuguna, E.; Coussens, E.G.; Neyt, P.; Aesaert, S.; Storme, V.; Demuynck, K.; Vanhaeren, H.; Dhondt, S.; van Haver, Y.; Paul, L.; Inze, D.; Nelissen, H.; van Lijsebettens, M.
Functional analysis of Arabidopsis and maize transgenic lines overexpressing the ADP-ribose/NADH pyrophosphohydrolase, AtNUDX7
Int. J. Dev. Biol.
63
45-55
2019
Arabidopsis thaliana (Q9SU14)
brenda
Maruta, T.; Ogawa, T.; Tsujimura, M.; Ikemoto, K.; Yoshida, T.; Takahashi, H.; Yoshimura, K.; Shigeoka, S.
Loss-of-function of an Arabidopsis NADPH pyrophosphohydrolase, AtNUDX19, impacts on the pyridine nucleotides status and confers photooxidative stress tolerance
Sci. Rep.
6
37432
2016
Arabidopsis thaliana (Q94A82)
-
brenda
Elitas, M.
Isoniazid killing of Mycobacterium smegmatis NADH pyrophosphatase mutant at single-cell level using microfluidics and time-lapse microscopy
Sci. Rep.
7
10770
2017
Mycolicibacterium smegmatis (A0QTS4), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0QTS4), Mycolicibacterium smegmatis mc(2)155 (A0QTS4)
brenda
Liu, Y.; Gong, J.; Marshall, G.; Su, C.; Hall, M.; Li, H.; Xu, G.; Shi, J.; Xu, Z.
Protein engineering of NADH pyrophosphatase for efficient biocatalytic production of reduced nicotinamide mononucleotide
Front. Bioeng. Biotechnol.
11
1159965
2023
Escherichia coli (P32664), Escherichia coli JM109 (P32664)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.1.22)
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