Structure, mechanism, and evolution of the last step in vitamin C biosynthesis

Alessandro Boverio, Neelam Jamil, Barbara Mannucci, Maria Laura Mascotti (), Marco W. Fraaije () and Andrea Mattevi ()
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Alessandro Boverio: University of Groningen
Neelam Jamil: University of Pavia
Barbara Mannucci: University of Pavia
Maria Laura Mascotti: University of Groningen
Marco W. Fraaije: University of Groningen
Andrea Mattevi: University of Pavia

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: Abstract Photosynthetic organisms, fungi, and animals comprise distinct pathways for vitamin C biosynthesis. Besides this diversity, the final biosynthetic step consistently involves an oxidation reaction carried out by the aldonolactone oxidoreductases. Here, we study the origin and evolution of the diversified activities and substrate preferences featured by these flavoenzymes using molecular phylogeny, kinetics, mutagenesis, and crystallographic experiments. We find clear evidence that they share a common ancestor. A flavin-interacting amino acid modulates the reactivity with the electron acceptors, including oxygen, and determines whether an enzyme functions as an oxidase or a dehydrogenase. We show that a few side chains in the catalytic cavity impart the reaction stereoselectivity. Ancestral sequence reconstruction outlines how these critical positions were affixed to specific amino acids along the evolution of the major eukaryotic clades. During Eukarya evolution, the aldonolactone oxidoreductases adapted to the varying metabolic demands while retaining their overarching vitamin C-generating function.

Date: 2024
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DOI: 10.1038/s41467-024-48410-1

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