Sandbox GGC1
From Proteopedia
(Difference between revisions)
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<StructureSection load='6BKA' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='6BKA' size='340' side='right' caption='Caption for this structure' scene=''> | ||
<scene name='75/752263/Alpha_beta_sheets/1'>This view</scene> shows the alpha helixes and beta pleaded sheets of nitronate monooxygenase. | <scene name='75/752263/Alpha_beta_sheets/1'>This view</scene> shows the alpha helixes and beta pleaded sheets of nitronate monooxygenase. | ||
| - | + | Nitronate Monooxygenase (NMO) is an FMN-dependent (flavin mononucleotide) enzyme that oxidizes the neurotoxin propionate 3-nitronate (P3N). FMN is produced from riboflavin or Vitamin B2 by riboflavin kinase and can function as a prosthetic group for NADH dehydrogenase <ref>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.</ref>. NMO is widely known as the best system for P3N detoxification in many different organisms. | |
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== 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.</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 == | == Relevance == | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| - | 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. | ||
<references/> | <references/> | ||
Revision as of 15:37, 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.
- ↑ 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.
