Measurements of Flavin‐Containing Monooxygenase (<scp>FMO</scp>) Activities

Rose, Randy L.

doi:10.1002/0471140856.tx0409s13

Cited by 3 publications

(1 citation statement)

References 25 publications

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“…The enzymatic activities of the SeFMOs were assayed by the NADPH oxidation method described previously (Rose, ). In brief, the enzyme–substrate reaction mix contained 500 µl 2 × tricine/KOH buffer, pH 8.5, 10 µl 10 mM NADPH, 50 µl purified FMO enzyme, 10 µl 0.1 M substrate and 430 µl ddH 2 O.…”

Section: Methodsmentioning

confidence: 99%

Molecular characterization, expression pattern and metabolic activity of flavin‐dependent monooxygenases inSpodoptera exigua

Tian

Zhao²,

Guo

et al. 2018

Insect Molecular Biology

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Enhanced detoxification is one of the important mechanisms for insecticide resistance. Most research in this field to date has focused on the role of cytochrome P450s. Our previous work revealed that flavin-dependent monooxygenases (FMOs) were involved in metabolic resistance of Spodoptera exigua. In the present study we investigated the molecular characteristics, expression patterns and oxidative activities of SeFMO on insecticides. Three FMO genes, which encode proteins with the typical FMO motifs, were cloned from S. exigua. The oxidative activities of eukaryotically expressed SeFMO enzymes were verified with the model substrate of FMO. Importantly, the SeFMOs had significantly higher oxidative activities on metaflumizone and lambda-cyhalothrin than on model substrates and other insecticides tested. The three SeFMOs were mainly expressed in the midgut, fat body and Malpighian tubules. The tissues responsible for xenobiotic metabolism and their expression characteristics were similar to those of P450s acting as detoxification genes. The study also revealed that the expression of SeFMOs could be induced by insecticide exposure, and that SeFMOs were over-expressed in a metaflumizone-resistant strain of S. exigua. These results suggest that SeFMOs are important insecticide detoxifying enzymes, and that over-expression of FMO genes may be one of the mechanisms for metabolic resistance in S. exigua.

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Section: Methodsmentioning

confidence: 99%

Molecular characterization, expression pattern and metabolic activity of flavin‐dependent monooxygenases inSpodoptera exigua

Tian

Zhao²,

Guo

et al. 2018

Insect Molecular Biology

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Metformin decreases bacterial trimethylamine production and trimethylamine N-oxide levels in db/db mice

Kuka

Videja

Makrecka-Kūka

et al. 2020

Sci Rep

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The current study aimed to explore whether metformin, the most widely prescribed oral medication for the treatment of type 2 diabetes, alters plasma levels of cardiometabolic disease-related metabolite trimethylamine N-oxide (TMAO) in db/db mice with type 2 diabetes. TMAO plasma concentration was up to 13.2-fold higher in db/db mice when compared to control mice, while in db/db mice fed choline-enriched diet, that mimics meat and dairy product intake, TMAO plasma level was increased 16.8-times. Metformin (250 mg/kg/day) significantly decreased TMAO concentration by up to twofold in both standard and choline-supplemented diet-fed db/db mice plasma. In vitro, metformin significantly decreased the bacterial production rate of trimethylamine (TMA), the precursor of TMAO, from choline up to 3.25-fold in K. pneumoniae and up to 26-fold in P. Mirabilis , while significantly slowing the growth of P. Mirabilis only. Metformin did not affect the expression of genes encoding subunits of bacterial choline-TMA-lyase microcompartment, the activity of the enzyme itself and choline uptake, suggesting that more complex regulation beyond the choline-TMA-lyase is present. To conclude, the TMAO decreasing effect of metformin could be an additional mechanism behind the clinically observed cardiovascular benefits of the drug.

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OSGN-1 is a conserved flavin-containing monooxygenase required to stabilize the intercellular bridge in late cytokinesis

Goupil,

Lacroix,

Brière

et al. 2023

Preprint

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Cytokinesis is the last step of cell division and is regulated by the small GTPase RhoA. RhoA activity is required for all steps of cytokinesis, including prior to abscission when daughter cells are ultimately physically separated. Like germ cells in all animals, theC. elegansembryonic germline founder cell initiates cytokinesis but does not complete abscission, leaving a stable intercellular bridge between the two daughter cells. Here we identify and characterizeC. elegansOSGN-1 as a novel cytokinetic regulator that promotes RhoA activity during late cytokinesis. Sequence analyses and biochemical reconstitutions reveal that OSGN-1 is a flavin-containing monooxygenase. Genetic analyses indicate that the monooxygenase activity of OSGN-1 is required to maintain active RhoA at the end of cytokinesis in the germline founder cell and to stabilize the intercellular bridge. Deletion ofOSGIN1in human cells results in an increase in binucleation as a result of cytokinetic furrow regression, and this phenotype can be rescued by expressing a catalytically-active form ofC. elegansOSGN-1, indicating that OSGN-1 and OSGIN1 are functional orthologs. We propose that OSGN-1 and OSGIN1 are novel, conserved monooxygenase enzymes required to maintain RhoA activity at the intercellular bridge during late cytokinesis and thus promote its stability, enabling proper abscission in human cells and bridge stabilization inC. elegansgerm cells.

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Measurements of Flavin‐Containing Monooxygenase (FMO) Activities

Cited by 3 publications

References 25 publications

Molecular characterization, expression pattern and metabolic activity of flavin‐dependent monooxygenases inSpodoptera exigua

Molecular characterization, expression pattern and metabolic activity of flavin‐dependent monooxygenases inSpodoptera exigua

Metformin decreases bacterial trimethylamine production and trimethylamine N-oxide levels in db/db mice

OSGN-1 is a conserved flavin-containing monooxygenase required to stabilize the intercellular bridge in late cytokinesis

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