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
L-galactonolactone dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.3.2.3 | ||||||||
CAS no. | 2603847 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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- (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]
References
edit- ^ Mapson, L.W.; Breslow, E. (1957). "Properties of partially purified L-galactono-γ-lactone dehydrogenase". Biochem. J. 65: 29.
- ^ 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 13126087.21-8&rft.date=1954-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1269564#id-name=PMC&rft_id=info:pmid/13126087&rft_id=info:doi/10.1042/bj0560021&rft.aulast=Mapson&rft.aufirst=LW&rft.au=Isherwood, FA&rft.au=Chen, YT&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1269564&rfr_id=info:sid/en.wikipedia.org:Galactonolactone dehydrogenase" class="Z3988">
- ^ 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 13126085.1-15&rft.date=1954-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1269562#id-name=PMC&rft_id=info:pmid/13126085&rft_id=info:doi/10.1042/bj0560001&rft.aulast=Isherwood&rft.aufirst=FA&rft.au=Chen, YT&rft.au=Mapson, LW&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1269562&rfr_id=info:sid/en.wikipedia.org:Galactonolactone dehydrogenase" class="Z3988">
- ^ 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 7775377.120-4&rft.date=1995-01&rft_id=info:doi/10.1093/oxfordjournals.jbchem.a124697&rft_id=info:pmid/7775377&rft.aulast=Oba&rft.aufirst=K&rft.au=Ishikawa, S&rft.au=Nishikawa, M&rft.au=Mizuno, H&rft.au=Yamamoto, T&rfr_id=info:sid/en.wikipedia.org:Galactonolactone dehydrogenase" class="Z3988">
- ^ 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 9374475.30009-16&rft.date=1997-11&rft_id=info:doi/10.1074/jbc.272.48.30009&rft_id=info:pmid/9374475&rft.aulast=Ostergaard&rft.aufirst=J&rft.au=Persiau, G&rft.au=Davey, MW&rft.au=Bauw, G&rft.au=Van Montagu, M&rft_id=https://doi.org/10.1074%2Fjbc.272.48.30009&rfr_id=info:sid/en.wikipedia.org:Galactonolactone dehydrogenase" class="Z3988">
- ^ 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.
External links
edit- L-galactonolactone dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)