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Information on EC 1.13.12.16 - nitronate monooxygenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I4V0
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1.13.12.16 nitronate monooxygenaseIUBMB Comments
Previously classified as 2-nitropropane dioxygenase (EC 1.13.11.32), but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Neither hydrogen peroxide nor superoxide were detected during enzyme turnover. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.
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Word Map
- 1.13.12.16
- nitroalkanes
- flavin
- nitroethane
- neurospora
- crassa
- fmn
- hansenula
- mrakii
-
flavosemiquinone
- 1-nitropropane
-
denitrification
-
3-nitropropionic
- ansochromogenes
-
fmn-dependent
- saturnus
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-nitropropane dioxygenase, nitronate monooxygenase, rv1894c, sa-nao, protein pa4202, nitropropane dioxygenase, p3n monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NAO
-
-
-
-
nitroalkane oxidase
-
-
-
-
oxidase, nitroalkane
-
-
-
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oxygenase, 2-nitropropane di-
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ethylnitronate + O2 = acetaldehyde + nitrite + other products
catalytic and kinetic reaction mechanism, comparison to the nitroalkane oxygenase, EC 1.7.3.1, and other flavin-dependent enzymes, ionization of nitroethane and ethylnitronate in aqueous solution, overview
ethylnitronate + O2 = acetaldehyde + nitrite + other products
catalyze the oxidation of propionate-3-nitronate or other nitronate analogues through a radical mechanism involving a catalytic flavosemiquinone without formation of a canonical C4a-(hydro)peroxyflavin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
nitronate:oxygen 2-oxidoreductase (nitrite-forming)
Previously classified as 2-nitropropane dioxygenase (EC 1.13.11.32), but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Neither hydrogen peroxide nor superoxide were detected during enzyme turnover. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity.
CAS REGISTRY NUMBER
COMMENTARY
61584-55-2
-
65802-82-6
-
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
ethylnitronate + O2 + FMNH2
acetaldehyde + nitrite + FMN + H2O
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-
-
?
ethylnitronate + O2
acetaldehyde + nitrite + other products
-
-
-
?
additional information
?
-
the enzyme is active on propionate-3-nitronate and other alkyl nitronates, but cannot oxidize nitroalkanes, e.g. 3-nitropropionate, nitroethane, 1-nitropropane, 1-nitrobutane, 1-nitropentane, or 2-nitropropane. Anaerobic reduction of the enzyme with propionate-3-nitronate yields a flavosemiquinone
-
-
?
3 propionate-3-nitronate + O2
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
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-
-
?
3 propionate-3-nitronate + O2
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
best substrate
-
-
?
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
ethylnitronate + O2 + FMNH2
acetaldehyde + nitrite + FMN + H2O
-
-
-
?
3 propionate-3-nitronate + O2
3 malonic semialdehyde + nitrite + 2 nitrate + H2O2
-
-
-
?
ethylnitronate + O2
acetaldehyde + nitrite + other products
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
contains a tightly, but not covalently, bound flavin that is required for enzymatic activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
NMO contains no iron atom at the active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by valeric acid and EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic mechanism
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11818.2
propionate-3-nitronate
pH 7.5, 30°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
NMO is a member of the group H flavin-dependent monooxygenases
malfunction
deletion of the nmoA gene results in an increased sensitivity of the cells to 3-nitropropionic acid (3-NPA), phenotype, overview
physiological function
additional information
four conserved motifs are identified in PA4202. Oxidation of propionate-3-nitronate by NMO yields malonic semialdehyde, which is an important metabolite that can be converted to acetyl-CoA, acetate, or 3-hydroxypropionate and enter various catabolic or anabolic pathways. Active site structure analysis, overview
physiological function
nitronate monooxygenase oxidizes the mitochondrial toxin propionate 3-nitronate to malonate semialdehyde, and detoxifies the deadly toxin
physiological function
role of the nitronate monooxygenase protein in the detoxification of nitronate. At physiological pH, 3-nitropropionate, a nitro toxin produced by plants and fungi, exists in equilibrium with its conjugate base, propionate-3-nitronate, the tauromer of 3-nitropropionic acid
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
enzyme surface structure analysis using the structure PDB Code 2GJN
additional information
the dimer interface includes eight contacts mainly in the FMN-binding domain and it does not seem to be directly relevant for catalysis as it is far from the active site pocket, structure analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 10% (w/v) polyethylene glycol monomethyl ether 5000
purified recombinant His-tagged enzyme, vapor diffusion hanging drop method at room temperature, 0.002 ml of 14 mg/ml protein in 50 mM Tris-Cl, pH 8.0, 100 mM NaCl, 20 mM 2-nitropropane, with 0.002 ml of reservoir solution containing 14% w/v PEG 5000 monomethylether and 0.1 M Na-HEPES, pH 7.0, and equilibration against 1 ml of reservoir solution, 7-10 days, X-ray diffraction structure determination and analysis at 1.44 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H152A
S288A
additional information
H152A
His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon
H152A
site-directed mutagenesis. His152 likely functions as the catalytic base that initiates oxidation of neutral substrates by abstracting a proton from the alpha-carbon
S288A
mutant enzyme forms inclusion bodies when overexpressed in Escherichia coli
S288A
site-directed mutagenesis. Mutant enzyme forms inclusion bodies when overexpressed in Escherichia coli
additional information
construction of an enzyme deletion mutant by the in vivo recombination system of the yeast Saccharomyces cerevisiae strain InvSc1, overview. Quantitative RT-PCR enzyme expression analysis. The expression of ddlA is not changed in the DELTAnmoA mutant compared to the wild-type
additional information
-
construction of an enzyme deletion mutant by the in vivo recombination system of the yeast Saccharomyces cerevisiae strain InvSc1, overview. Quantitative RT-PCR enzyme expression analysis. The expression of ddlA is not changed in the DELTAnmoA mutant compared to the wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiLoad XK 16 Superdex 200 prep-grade column gel filtration and Mono Q HR5/5 column chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3)pLysS by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PA4202 or nmoA, monocistronic, low expression level gene, has an intergenic region of 97 nucleotides with neighbouring gene PA4201 (ddlA) encoding D-alanine alanine ligase, and an intergenic region of 107 nucleotides with gene PA4203 encoding a LysR regulator, PA4203 (nmoR) represses its own transcription and the expression of PA4202 (nmoA), presence of a single NmoR binding site between nmoA and nmoR, and interaction of NmoR with the intergenic nmoA-nmoR control region. In silico analysis of the ddlA-nmoA-nmoR-ppgL locus in Pseudomonas aeruginosa genomes, transcriptome analysis
gene pa4202, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ha, J.Y.; Min, J.Y.; Lee, S.K.; Kim, H.S.; Kim, d.o.J.; Kim, K.H.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base
J. Biol. Chem.
281
18660-18667
2006
Pseudomonas aeruginosa (Q9I4V0), Pseudomonas aeruginosa
Gadda, G.; Francis, K.
Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis
Arch. Biochem. Biophys.
493
53-61
2009
Cyberlindnera saturnus, Cyberlindnera saturnus mrakii, Neurospora crassa, Pseudomonas aeruginosa (Q9I4V0)
Vercammen, K.; Wei, Q.; Charlier, D.; Doetsch, A.; Hauessler, S.; Schulz, S.; Salvi, F.; Gadda, G.; Spain, J.; Rybtke, M.L.; Tolker-Nielsen, T.; Dingemans, J.; Ye, L.; Cornelis, P.
Pseudomonas aeruginosa LysR PA4203 regulator NmoR acts as a repressor of the PA4202 nmoA gene, encoding a nitronate monooxygenase
J. Bacteriol.
197
1026-1039
2015
Pseudomonas aeruginosa (Q9HWH9), Pseudomonas aeruginosa
Salvi, F.; Agniswamy, J.; Yuan, H.; Vercammen, K.; Pelicaen, R.; Cornelis, P.; Spain, J.C.; Weber, I.T.; Gadda, G.
The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II
J. Biol. Chem.
289
23764-23775
2014
Pseudomonas aeruginosa (Q9HWH9)
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