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- W2024076139 abstract "Steap4 is a cell surface metalloreductase linked to obesity-associated insulin resistance. Initial characterization of its cell surface metalloreductase activity has been reported, but thorough biochemical characterization of this activity is lacking. Here, we report detailed kinetic analysis of the Steap4 cell surface metalloreductase activities. Steap4 shows physiologically relevant Km values for both Fe(3+) and Cu(2+) and retains activity at acidic pH, suggesting it may also function within intracellular organelles to reduce these metals. Flavin-dependent NADPH oxidase activity that was much greater than the equivalent Steap3 construct was observed for the isolated N-terminal oxidoreductase domain. The crystal structure of the Steap4 oxidoreductase domain was determined, providing a structural explanation for these differing activities. Structure-function work also suggested Steap4 utilizes an interdomain flavin-binding site to shuttle electrons between the oxidoreductase and transmembrane domains, and it showed that the disordered N-terminal residues do not contribute to enzymatic activity." @default.
- W2024076139 created "2016-06-24" @default.
- W2024076139 creator A5006370557 @default.
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- W2024076139 creator A5062616405 @default.
- W2024076139 creator A5078424734 @default.
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- W2024076139 date "2013-07-01" @default.
- W2024076139 modified "2023-10-12" @default.
- W2024076139 title "The Crystal Structure of Six-transmembrane Epithelial Antigen of the Prostate 4 (Steap4), a Ferri/Cuprireductase, Suggests a Novel Interdomain Flavin-binding Site" @default.
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- W2024076139 doi "https://doi.org/10.1074/jbc.m113.479154" @default.
- W2024076139 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3711330" @default.
- W2024076139 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23733181" @default.
- W2024076139 hasPublicationYear "2013" @default.
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