EC Number   |
General Information |
Reference |
|---|
   1.13.12.16 | evolution |
NMO is a member of the group H flavin-dependent monooxygenases |
745306 |
| 1.13.12.16 | malfunction |
a knockout mutant of Neurospora crassa lacking NMO is inhibited by concentrations of propionate-3-nitronate and 3-nitropropionate |
726808 |
| 1.13.12.16 | malfunction |
deletion of the nmoA gene results in an increased sensitivity of the cells to 3-nitropropionic acid (3-NPA), phenotype, overview |
745219 |
| 1.13.12.16 | malfunction |
the mixture propionate-3-nitronate/3-nitropropionate is toxic to recombinant Escherichia coli cells lacking expression of NMO, but the toxicity is overcome through either induction of the gene for NMO or through addition of exogenous enzyme to the cultures |
726808 |
| 1.13.12.16 | more |
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 |
745306 |
| 1.13.12.16 | physiological function |
nitronate monooxygenase oxidizes the mitochondrial toxin propionate 3-nitronate to malonate semialdehyde, and detoxifies the deadly toxin |
745306 |
| 1.13.12.16 | 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 |
745219 |
