1.13.12.16: nitronate monooxygenase

This is an abbreviated version!
For detailed information about nitronate monooxygenase, go to the full flat file.

Reaction

Synonyms

2-nitropropane dioxygenase, EC 1.13.11.32, NAO, ncd2, nitroalkane oxidase, nitroalkane-oxidizing enzyme, nitronate monooxygenase, nitropropane dioxygenase, NMO, NMO-Nc, NMO-Ws, nmoA, Npd1, Npd2, Npd3, Npd4, Npd5, Npd6, oxidase, nitroalkane, oxygenase, 2-nitropropane di-, P3N monooxygenase, Pa-NMO, PA4202, protein PA4202, Rv1894c, Sa-NAO

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

                1.13.12.16 nitronate monooxygenase

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Results	in table
3	Activating Compound
3508	AA Sequence
2	CAS Registry Number
13	Cloned(Commentary)
32	Cofactor
5	Crystallization (Commentary)
3	Expression
8	General Information
3	General Stability
84	Inhibitors
57	kcat/KM [mM/s]
20	Ki Value [mM]
122	KM Value [mM]
9	Metals/Ions
16	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
57	Organism
3	Pathway
16	PDB ID
26	pH Optimum
5	pH Range
1	pH Stability
11	Protein Variants
21	Purification (Commentary)
11	Reaction
3	Reaction Type
40	Reference
4	Source Tissue
9	Specific Activity [micromol/min/mg]
2	Storage Stability
234	Substrates and Products (Substrate)
14	Subunits
76	Synonyms
1	Systematic Name
21	Temperature Optimum [°C]
3	Temperature Range [°C]
6	Temperature Stability [°C]
67	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.13.12.16 - nitronate monooxygenase

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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.