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] Recent structural studies suggest there are two classes of NMOs, Class I and Class II.[4] 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.[5]
In Class I NMOs, the enzyme mechanism is first initiated by a single electron transfer from P3N to
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. [6] 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 can even cause death. [7]
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
