Sandbox GGC1
From Proteopedia
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== Function == | == Function == | ||
| - | NMOs are FMN-dependent enzymes that can quickly and efficiently catalyze the oxidation of P3N. They can also oxidize alkyl nitronates but with lower catalytic efficiency in comparison to P3N.<ref> Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.</ref><ref>Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.</ref> Recent structural studies suggest there are two classes of NMOs, Class I and Class II.<ref>Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.</ref> Class I NMOs | + | NMOs are FMN-dependent enzymes that can quickly and efficiently catalyze the oxidation of P3N. They can also oxidize alkyl nitronates but with lower catalytic efficiency in comparison to P3N.<ref> Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.</ref><ref>Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.</ref> Recent structural studies suggest there are two classes of NMOs, Class I and Class II.<ref>Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.</ref> Class I NMOs contain about 450 NMO gene products from bacteria, fungi, and animals. The enzymes in this class only oxidize P3N and nitronate analogues. Class II NMOs consists of small groups of ten fungal gene products and can oxidize nitronate and nitroalkaline analogues. |
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== Disease == | == Disease == | ||
Revision as of 17:29, 22 April 2018
Crystal Structure of yeast nitronate monooxygenase from Cyberlindera saturnas
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References
- ↑ Huerta C, Borek D, Machius M, Grishin NV, Zhang H. Structure and Mechanism of a Eukaryotic FMN Adenylyltransferase. Journal of molecular biology. 2009;389(2):388-400. doi:10.1016/j.jmb.2009.04.022.
- ↑ Francis K, Nishino SF, Spain JC, Gadda G. A novel activity for fungal nitronate monooxygenase: detoxification of the metabolic inhibitor propionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.
- ↑ Gadda G, Francis K. Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.
- ↑ Salvi F, Agniswamy J, Yuan H, et al. The combined structural and kinetic characterization of a bacterial nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes NMO class I and II.J Biol Chem. 2014;289(34):23764–23775.
- ↑ Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101
- ↑ Francis K, Smitherman C, Nishino SF, Spain JC, Gadda G. The bio-chemistry of the metabolic poison propionate 3-nitronate and its conjugate acid, 3-nitropropionate. IUBMB Life. 2013;65(9):759–768.
