Sandbox GGC1: Difference between revisions

Revision as of 16:26, 22 April 2018

Crystal Structure of yeast nitronate monooxygenase from Cyberlindera saturnas

This view 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 ^[1]. NMO is widely known as the best system for P3N detoxification in many different organisms.

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.^[2]^[3]

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. ^[4] 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. ^[5]

Structural highlights

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↑ 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.

References

[1] 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.

[2] 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.

[3] Gadda G, Francis K. Nitronate monooxygenase, a model for anionicflavin semiquinone intermediates in oxidative catalysis. Arch Bio-chem Biophys. 2010;493(1):53–61.

[4] Hipkin CR, Simpson DJ, Wainwright SJ, Salem MA. Nitrification by plants that also fix nitrogen. Nature. 2004;430(6995):98–101

[5] 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.

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[2]

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[4]

[5]

@@ Line 7: / Line 7: @@
 == 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 ==
-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>
+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 ==

Sandbox GGC1: Difference between revisions

Revision as of 16:26, 22 April 2018

Function

Disease

Structural highlights

References

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