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Literature summary for 1.13.12.16 extracted from

  • Gadda, G.; Francis, K.
    Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis (2009), Arch. Biochem. Biophys., 493, 53-61.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic mechanism with ethylnitronate, overview Neurospora crassa

Metals/Ions

Metals/Ions Comment Organism Structure
additional information NMO contains no iron atom at the active site Neurospora crassa
additional information NMO contains no iron atom at the active site Cyberlindnera saturnus
additional information NMO contains no iron atom at the active site Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethylnitronate + O2 + FMNH2 Neurospora crassa
-
acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2 Cyberlindnera saturnus
-
acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2 Pseudomonas aeruginosa
-
acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2 Cyberlindnera saturnus mrakii
-
acetaldehyde + nitrite + FMN + H2O
-
?
additional information Neurospora crassa both the neutral and anionic forms of nitroalkanes act as substrates for the oxidative denitrification reaction catalyzed by Neurospora crassa NMO. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-1- and propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms ?
-
?
additional information Cyberlindnera saturnus only alkyl nitronates are used as substrates in the oxidative denitrification reaction catalyzed by Williopsis saturnus var. mrakii NMO, nitroalkanes are no substrates. The different substrate specificity compared to other NMOs might result from the presence of a His residue in the active site and conformational differences. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms ?
-
?
additional information Cyberlindnera saturnus mrakii only alkyl nitronates are used as substrates in the oxidative denitrification reaction catalyzed by Williopsis saturnus var. mrakii NMO, nitroalkanes are no substrates. The different substrate specificity compared to other NMOs might result from the presence of a His residue in the active site and conformational differences. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms ?
-
?
nitroethane + O2 Neurospora crassa
-
acetaldehyde + nitrite
-
?
nitroethane + O2 Pseudomonas aeruginosa
-
acetaldehyde + nitrite
-
?
propyl-1-nitronate + O2 + FMNH2 Neurospora crassa
-
? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2 Neurospora crassa
-
? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2 Cyberlindnera saturnus
-
? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2 Cyberlindnera saturnus mrakii
-
? + nitrite + FMN + H2O
-
?

Organism

Organism UniProt Comment Textmining
Cyberlindnera saturnus
-
-
-
Cyberlindnera saturnus mrakii
-
-
-
Neurospora crassa
-
-
-
Pseudomonas aeruginosa Q9I4V0
-
-

Reaction

Reaction Comment Organism Reaction ID
ethylnitronate + O2 = acetaldehyde + nitrite + other products catalytic and kinetic reaction mechanism, comparison to the nitroalkane oxigenase, EC 1.7.3.1, and other flavin-dependent enzymes, ionization of nitroethane and ethylnitronate in aqueous solution, overview. Enzymatic turnover begins with the rapid equilibrium association of ethylnitronate and the enzyme. In the oxidative pathway, the transfer of a single electron oxidizes the organic substrate and reduces the enzyme-bound flavin to an anionic semiquinone species, the electron transfer occurs while the substrate radical is still bound in the active site of the enzyme. After formation of the flavosemiquinone species in the active site of NMO, the subsequent oxidation of the one electron reduced flavin occurs when molecular oxygen reacts with the anionic flavosemiquinone to yield an enzyme-associated superoxide species, with second-order rate constants Neurospora crassa
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 Cyberlindnera saturnus
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 Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-nitropropane + O2
-
Pseudomonas aeruginosa ?
-
?
ethylnitronate + O2 + FMNH2
-
Neurospora crassa acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2
-
Cyberlindnera saturnus acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2
-
Pseudomonas aeruginosa acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2 reaction via ethylnitronate radical. Catalytic turnover of NMO with ethylnitronate as substrate occurs through both an oxidative denitrification pathway and a non-oxidative pathway in which the anionic substrate is protonated in the active site of the enzyme to form nitroethane as a reaction product Neurospora crassa acetaldehyde + nitrite + FMN + H2O
-
?
ethylnitronate + O2 + FMNH2
-
Cyberlindnera saturnus mrakii acetaldehyde + nitrite + FMN + H2O
-
?
additional information both the neutral and anionic forms of nitroalkanes act as substrates for the oxidative denitrification reaction catalyzed by Neurospora crassa NMO. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-1- and propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms Neurospora crassa ?
-
?
additional information only alkyl nitronates are used as substrates in the oxidative denitrification reaction catalyzed by Williopsis saturnus var. mrakii NMO, nitroalkanes are no substrates. The different substrate specificity compared to other NMOs might result from the presence of a His residue in the active site and conformational differences. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms Cyberlindnera saturnus ?
-
?
additional information only alkyl nitronates are used as substrates in the oxidative denitrification reaction catalyzed by Williopsis saturnus var. mrakii NMO, nitroalkanes are no substrates. The different substrate specificity compared to other NMOs might result from the presence of a His residue in the active site and conformational differences. NMO does not produce and release hydrogen peroxide during turnover with linear alkyl nitronates of various lengths between 2 and 6 carbon atoms or with propyl-2-nitronate. With the exception of propyl-2-nitronate, there is no release of superoxide during turnover of NMO at pH 8.0 and 30°C with linear alkyl nitronates with chain lengths between 2 and 6 carbon atoms Cyberlindnera saturnus mrakii ?
-
?
nitroethane + O2
-
Neurospora crassa acetaldehyde + nitrite
-
?
nitroethane + O2
-
Pseudomonas aeruginosa acetaldehyde + nitrite
-
?
nitroethane + O2 catalytic turnover of NMO with nitroethane as substrate occurs with oxidative and non-oxidative pathways with ethylnitronate formation and release in assays of the enzyme with the neutral substrate. The nonoxidative pathway of the enzyme with nitroethane as substrate also involves the H196-catalyzed deprotonation of the nitroalkane and the release of ethylnitronate as a reaction product Neurospora crassa acetaldehyde + nitrite
-
?
propyl-1-nitronate + O2 + FMNH2
-
Neurospora crassa ? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2
-
Neurospora crassa ? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2
-
Cyberlindnera saturnus ? + nitrite + FMN + H2O
-
?
propyl-2-nitronate + O2 + FMNH2
-
Cyberlindnera saturnus mrakii ? + nitrite + FMN + H2O
-
?

Subunits

Subunits Comment Organism
More enzyme surface structure analysis using the structure PDB Code 2GJN Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
NMO
-
Neurospora crassa
NMO
-
Cyberlindnera saturnus
NMO
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Neurospora crassa
30
-
assay at Cyberlindnera saturnus
30
-
assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Pseudomonas aeruginosa
7.4 8 assay at Neurospora crassa
7.4 8 assay at Cyberlindnera saturnus

Cofactor

Cofactor Comment Organism Structure
FMN contains a tightly, but not covalently, bound flavin that is required for enzymatic activity Neurospora crassa
FMN contains a tightly, but not covalently, bound flavin that is required for enzymatic activity Cyberlindnera saturnus
FMN contains a tightly, but not covalently, bound flavin that is required for enzymatic activity Pseudomonas aeruginosa