Galactonolactone dehydrogenase

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L-galactonolactone dehydrogenase
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EC no. 1.3.2.3
CAS no. 2603847
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L-galactonolactone dehydrogenase (EC 1.3.2.3, galactonolactone dehydrogenase, L-galactono-gamma-lactone dehydrogenase, L-galactono-gamma-lactone:ferricytochrome-c oxidoreductase, GLDHase, GLDase) is an enzyme with systematic name L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

(1) L-galactono-1,4-lactone + 2 ferricytochrome c L-ascorbate + 2 ferrocytochrome c + 2 H+
(2) L-ascorbate + 2 ferricytochrome c L-dehydroascorbate + 2 ferrocytochrome c + 2 H+ (spontaneous)

This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in plants and other photosynthetic eukaryotes. [6]

Related Research Articles

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<span class="mw-page-title-main">3-dehydro-L-gulonate 2-dehydrogenase</span> InterPro Family

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<span class="mw-page-title-main">Formate dehydrogenase (cytochrome)</span> Type of enzyme

In enzymology, a formate dehydrogenase (cytochrome) (EC 1.2.2.1) is an enzyme that catalyzes the chemical reaction

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Polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.2.6, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl alcohol:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction

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<span class="mw-page-title-main">Nicotinate dehydrogenase (cytochrome)</span>

Nicotinate dehydrogenase (cytochrome) (EC 1.17.2.1, nicotinic acid hydroxylase, nicotinate hydroxylase) is an enzyme with systematic name nicotinate:cytochrome 6-oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction

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References

  1. Mapson, L.W.; Breslow, E. (1957). "Properties of partially purified L-galactono-γ-lactone dehydrogenase". Biochem. J. 65: 29.
  2. Mapson LW, Isherwood FA, Chen YT (January 1954). "Biological synthesis of L-ascorbic acid: the conversion of L-galactono-gamma-lactone into L-ascorbic acid by plant mitochondria". The Biochemical Journal. 56 (1): 21–8. doi:10.1042/bj0560021. PMC   1269564 . PMID   13126087.
  3. Isherwood FA, Chen YT, Mapson LW (January 1954). "Synthesis of L-ascorbic acid in plants and animals". The Biochemical Journal. 56 (1): 1–15. doi:10.1042/bj0560001. PMC   1269562 . PMID   13126085.
  4. Oba K, Ishikawa S, Nishikawa M, Mizuno H, Yamamoto T (January 1995). "Purification and properties of L-galactono-gamma-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots". Journal of Biochemistry. 117 (1): 120–4. doi:10.1093/oxfordjournals.jbchem.a124697. PMID   7775377.
  5. Ostergaard J, Persiau G, Davey MW, Bauw G, Van Montagu M (November 1997). "Isolation of a cDNA coding for L-galactono-gamma-lactone dehydrogenase, an enzyme involved in the biosynthesis of ascorbic acid in plants. Purification, characterization, cDNA cloning, and expression in yeast". The Journal of Biological Chemistry. 272 (48): 30009–16. doi: 10.1074/jbc.272.48.30009 . PMID   9374475.
  6. Wheeler G, Ishikawa T, Pornsaksit V, Smirnoff N (March 2015). "Evolution of alternative biosynthetic pathways for vitamin C following plastid acquisition in photosynthetic eukaryotes". eLife. 4. doi: 10.7554/eLife.06369 . PMC   4396506 . PMID   25768426.