Sandbox GGC1
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | NMOs are FMN-dependent enzymes that | + | 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 fungalnitronate monooxygenase: de toxification of the metabolic inhibitorpropionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.</ref><ref>Gadda G, Francis K. Nitronate monooxygenase, a model for anionicflavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.</ref> |
== Disease == | == Disease == | ||
| - | P3N can be considered a toxic compound that is commonly found in legumes, fungi, and leaf beetles. During hydrolysis, P3N is released from esters and acts as an irreversible inhibitor of mitochondrial succinate dehydrogenase. <ref>Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101 | + | P3N can be considered a toxic compound that is commonly found in legumes, fungi, and leaf beetles. During hydrolysis, P3N is released from esters and acts as an irreversible inhibitor of mitochondrial succinate dehydrogenase. <ref>Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101</ref> Succinate dehydrogenase is a key enzyme in the Kreb's cycle and the electron transport chain for oxidative phosphorylation. Because this is inhibited, it can lead to a variety of neurological disorders and even death. <ref>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.</ref> |
| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 16:26, 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 fungalnitronate monooxygenase: de toxification of the metabolic inhibitorpropionate-3-nitronate. Arch Biochem Biophys. 2012;521(1–2):84–89.
- ↑ Gadda G, Francis K. Nitronate monooxygenase, a model for anionicflavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.
- ↑ 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.
