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Vitamin C. Biosynthesis, recycling and degradation in mammals
Open accessAbstract
Vitamin C, a reducing agent and antioxidant, is a cofactor in reactions catalyzed by Cu(+)-dependent monooxygenases and Fe(2+)-dependent dioxygenases. It is synthesized, in vertebrates having this capacity, from d-glucuronate. The latter is formed through direct hydrolysis of uridine diphosphate (UDP)-glucuronate by enzyme(s) bound to the endoplasmic reticulum membrane, sharing many properties with, and most likely identical to, UDP-glucuronosyltransferases. Non-glucuronidable xenobiotics (aminopyrine, metyrapone, chloretone and others) stimulate the enzymatic hydrolysis of UDP-glucuronate, accounting for their effect to increase vitamin C formation in vivo. Glucuronate is converted to l-gulonate by aldehyde reductase, an enzyme of the aldo-keto reductase superfamily. l-Gulonate is converted to l-gulonolactone by a lactonase identified as SMP30 or regucalcin, whose absence in mice leads to vitamin C deficiency. The last step in the pathway of vitamin C synthesis is the oxidation of l-gulonolactone to l-ascorbic acid by l-gulonolactone oxidase, an enzyme associated with the endoplasmic reticulum membrane and deficient in man, guinea pig and other species due to mutations in its gene. Another fate of glucuronate is its conversion to d-xylulose in a five-step pathway, the pentose pathway, involving identified oxidoreductases and an unknown decarboxylase. Semidehydroascorbate, a major oxidation product of vitamin C, is reconverted to ascorbate in the cytosol by cytochrome b(5) reductase and thioredoxin reductase in reactions involving NADH and NADPH, respectively. Transmembrane electron transfer systems using ascorbate or NADH as electron donors serve to reduce semidehydroascorbate present in neuroendocrine secretory vesicles and in the extracellular medium. Dehydroascorbate, the fully oxidized form of vitamin C, is reduced spontaneously by glutathione, as well as enzymatically in reactions using glutathione or NADPH. The degradation of vitamin C in mammals is initiated by the hydrolysis of dehydroascorbate to 2,3-diketo-l-gulonate, which is spontaneously degraded to oxalate, CO(2) and l-erythrulose. This is at variance with bacteria such as Escherichia coli, which have enzymatic degradation pathways for ascorbate and probably also dehydroascorbate.
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In the citing paper
“So far, the synthesis of vitamin C was documented in all plant species, including algae and photosynthetic protists [1].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
In the citing paper
“They are, therefore, fully dependent on vitamin C intake from the diet [1,2,3].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
In the citing paper
“In contrast to most of the vertebrates, guinea pigs, bats, passeriform birds, and primates, including humans, lack L-gulono-1,4-lactone oxidase, and, hence, cannot synthesize vitamin C.”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
In the citing paper
“The pKa of ascorbic acid is 4.1–4.2. Hence, it is present completely as a monoanion—ascorbate at the physiological pH [1,2,4,68].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
In the citing paper
“2,3-diketo-1-gulonic acid can be spontaneously, but also enzymatically, decomposed to erythrulose and oxalate. This reaction is accelerated by bicarbonate [1,3].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
In the citing paper
“There are apparently redundant pathways mediating the reduction of dehydroascorbic acid to ascorbic acid. They include both direct but slow nonenzymatic reduction by glutathione and enzymatic by a couple of enzymes (e.g., glutaredoxin, glutathione transferase omega 2, or thioredoxin reductase). Of note is that the first two enzymes require glutathione for their activity [1,73].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [1]
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Metadata
- Authors
- Linster, C. L., & Van Schaftingen, E.
- Affiliations
- de Duve Institute (BE)
- ORCID
- Linster, Carole L.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2006-12-06
- Volume
- 274
- Issue
- 1
- Pages
- 1-22
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2065016714
- Cited by
- 757
- References
- 159
- Citations by year
- 2026: 20 · 2025: 42 · 2024: 66 · 2023: 46 · 2022: 49 · 2021: 61 · 2020: 65 · 2019: 36 · 2018: 26 · 2017: 31 · 2016: 34 · 2015: 31 · 2014: 38 · 2013: 44 · 2012: 37
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- green
- orbilu.uni.lu
- Licence
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Libraries (submittedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, cc-by-nc-sa)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Vitamin C and Antioxidants Research
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- vitamin C, ascorbic acid biosynthesis, UDP-glucuronate, UDP-glucuronosyltransferase, aldehyde reductase, aldo-keto reductase superfamily, L-gulonolactone oxidase, SMP30, regucalcin, dehydroascorbic acid, glutathione, vitamin C degradation, scurvy
- MeSH terms
- Animals, Ascorbic Acid, Carbohydrate Dehydrogenases, Escherichia coli, Glucuronates, Humans, Hydrolysis, Mammals, Models, Biological, Pentose Phosphate Pathway, Uridine Diphosphate Glucuronic Acid, L-Gulonolactone Oxidase
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