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Related Experiment Videos

L-ascorbic acid biosynthesis.

N Smirnoff1

  • 1School of Biological Sciences, University of Exeter, Exeter EX4 4PS, United Kingdom.

Vitamins and Hormones
|January 12, 2001
PubMed
Summary
This summary is machine-generated.

Vitamin C (ascorbate) biosynthesis pathways differ across plants, mammals, and yeast. While key enzymes in plants and yeast are known, many mammalian enzymes remain uncharacterized, hindering understanding of ascorbate production.

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Area of Science:

  • Biochemistry
  • Metabolic Pathways
  • Enzymology

Background:

  • L-ascorbate (vitamin C) biosynthesis pathways exhibit significant divergence between plants, mammals, and yeast.
  • Mammalian ascorbate synthesis initiates from UDP-D-glucuronic acid, while plants utilize GDP-D-mannose.
  • Yeast synthesizes D-erythroascorbate, a structural analog, via a pathway similar to plants.

Purpose of the Study:

  • To elucidate the distinct enzymatic steps and precursors involved in L-ascorbate biosynthesis across different species.
  • To identify conserved and divergent features among the terminal enzymes of ascorbate synthesis pathways.
  • To highlight knowledge gaps concerning mammalian ascorbate biosynthesis enzymes and regulatory mechanisms.

Main Methods:

  • Comparative analysis of established biochemical pathways for ascorbate synthesis in plants, mammals, and yeast.

Related Experiment Videos

  • Review of literature on cloned and purified enzymes, including L-gulono-1,4-lactone oxidase and L-galactono-1,4-lactone dehydrogenase.
  • Examination of sequence homology among terminal oxidases/dehydrogenases in different organisms.

    • Main Results:

    • Mammalian ascorbate synthesis involves L-gulonic acid/lactone, oxidized by L-gulono-1,4-lactone oxidase, which is non-functional in species lacking vitamin C synthesis.
    • Plant ascorbate synthesis proceeds via GDP-D-mannose, GDP-L-galactose, L-galactose, and L-galactono-1,4-lactone, with the final step catalyzed by mitochondrial L-galactono-1,4-lactone dehydrogenase.
    • Significant sequence homology exists between the terminal enzymes of ascorbate biosynthesis in plants, mammals, and yeast.
    • Key enzymes in these pathways, particularly in mammals, remain poorly characterized.

    Conclusions:

    • The terminal enzymes of ascorbate biosynthesis pathways share sequence homology, suggesting a common evolutionary origin.
    • Significant gaps in knowledge exist regarding the characterization and regulation of many enzymes involved in ascorbate biosynthesis, especially in mammals.
    • Further research is needed to fully understand the factors controlling flux through these pathways and to identify potential alternative routes.