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Engineering plant alternative oxidase function in mammalian cells: substitution of the motif-like sequence ENV for QDT diminishes catalytic activity of Arum concinnatum AOX1a expressed in HeLa cells.
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Alternative oxidase (AOX) is a nonproton motive quinol-oxygen oxidoreductase which is a component of the mitochondrial respiratory chain in higher plants. In this study, we have characterized the catalytic activity and regulatory behaviors of Arum concinnatum AOX isoforms, namely AcoAOX1a and
A novel functional element in the N-terminal region of Arum concinnatum alternative oxidase is indispensable for catalytic activity of the enzyme in HeLa cells.
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Alternative oxidase (AOX) is a quinol-oxygen oxidoreductase, which is known to possess a dicarboxylate diiron reaction center held in structurally postulated alpha-helical bundle. However, little is known about the structural or functional features of its N-terminal region in any organism, with the
Degradation of mitochondrial alternative oxidase in the appendices of Arum maculatum
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Cyanide-resistant alternative oxidase (AOX) is a nuclear-encoded quinol oxidase located in the inner mitochondrial membrane. Although the quality control of AOX proteins is expected to have a role in elevated respiration in mitochondria, it remains unclear whether thermogenic plants possess
Structure-guided identification of antimicrobial peptides in the spathe transcriptome of the non-model plant, arum lily (Zantedeschia aethiopica).
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Antimicrobial peptides (AMPs) are small molecules present in all living beings. Despite their huge sequence variability, AMPs present great structural conservation, mainly in cysteine-stabilized families. Moreover, in non-model plants, it is possible to detect cysteine-stabilized AMPs (cs-AMPs) with
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