ArticleInsect biochemistry and molecular biology2015
Multicopper oxidase-1 orthologs from diverse insect species have ascorbate oxidase activity.
Article in Insect biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 29 citations in OpenAlex.
- The effects of dietary iron supplementation on bacterial infections inbioRxiv : the preprint server for biology · 2026Article
- The effects of dietary iron supplementation on bacterial infections in Manduca sexta larval hemolymph.PloS one · 2026Article
- Iron Homeostasis in Insects.Annual review of entomology · 2023Review
- Article
- Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.Current biology : CB · 2022Article
- Mosquito metallomics reveal copper and iron as critical factors for Plasmodium infection.PLoS neglected tropical diseases · 2021Article
- A Fungal Ascorbate Oxidase with Unexpected Laccase Activity.International journal of molecular sciences · 2020Article
- RNAi-Mediated Suppression ofFrontiers in physiology · 2020Article
- Anatomy and Physiology of the Digestive Tract ofGenetics · 2018Review
- Iron Sulfur and Molybdenum Cofactor Enzymes Regulate theFrontiers in physiology · 2018Article
- Drosophila melanogaster Models of Metal-Related Human Diseases and Metal Toxicity.International journal of molecular sciences · 2017Review
- Ironing out the Details: Exploring the Role of Iron and Heme in Blood-Sucking Arthropods.Frontiers in physiology · 2017Review
- Multicopper oxidase-1 is required for iron homeostasis in Malpighian tubules of Helicoverpa armigera.Scientific reports · 2015Article
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8 authors at 1 institution in 1 country.
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Abstract
Members of the multicopper oxidase (MCO) family of enzymes can be classified by their substrate specificity; for example, ferroxidases oxidize ferrous iron, ascorbate oxidases oxidize ascorbate, and laccases oxidize aromatic substrates such as diphenols. Our previous work on an insect multicopper oxidase, MCO1, suggested that it may function as a ferroxidase. This hypothesis was based on three lines of evidence: RNAi-mediated knock down of Drosophila melanogaster MCO1 (DmMCO1) affects iron homeostasis, DmMCO1 has ferroxidase activity, and DmMCO1 has predicted iron binding residues. In our current study, we expanded our focus to include MCO1 from Anopheles gambiae, Tribolium castaneum, and Manduca sexta. We verified that MCO1 orthologs have similar expression profiles, and that the MCO1 protein is located on the basal surface of cells where it is positioned to oxidize substrates in the hemolymph. In addition, we determined that RNAi-mediated knock down of MCO1 in A. gambiae affects iron homeostasis. To further characterize the enzymatic activity of MCO1 orthologs, we purified recombinant MCO1 from all four insect species and performed kinetic analyses using ferrous iron, ascorbate and two diphenols as substrates. We found that all of the MCO1 orthologs are much better at oxidizing ascorbate than they are at oxidizing ferrous iron or diphenols. This result is surprising because ascorbate oxidases are thought to be specific to plants and fungi. An analysis of three predicted iron binding residues in DmMCO1 revealed that they are not required for ferroxidase or laccase activity, but two of the residues (His374 and Asp380) influence oxidation of ascorbate. These two residues are conserved in MCO1 orthologs from insects and crustaceans; therefore, they are likely to be important for MCO1 function. The results of this study suggest that MCO1 orthologs function as ascorbate oxidases and influence iron homeostasis through an unknown mechanism.
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