Enzyme

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EC Tree
     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.2 With a cytochrome as acceptor
ID:1.3.2.3
Description:L-galactonolactone dehydrogenase.
Alternative Name: L-galactono-gamma-lactone dehydrogenase.
GLDHase.
GLDase.
Galactonolactone dehydrogenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.2.3
BRENDA Enzyme Link: BRENDA 1.3.2.3
KEGG Enzyme Link: KEGG1.3.2.3
BioCyc Enzyme Link: BioCyc 1.3.2.3
ExPASy Enzyme Link: ExPASy1.3.2.3
EC2PDB Enzyme Link: EC2PDB 1.3.2.3
ExplorEnz Enzyme Link: ExplorEnz 1.3.2.3
PRIAM enzyme-specific profiles Link: PRIAM 1.3.2.3
IntEnz Enzyme Link: IntEnz 1.3.2.3
MEDLINE Enzyme Link: MEDLINE 1.3.2.3
MSA:

1.3.2.3;

Phylogenetic Tree:

1.3.2.3;

Uniprot:
M-CSA:
RHEA:32367 4 [Fe(III)cytochrome c] + L-galactono-1,4-lactone = 4 [Fe(II)cytochrome c] + 5 H(+) + L-dehydroascorbate
RULE(radius=1) [*:1]-[CH;+0:2](-[OH;+0:3])-[CH;+0:4](-[*:5])-[OH;+0:6].[Fe+3;H0:7].[Fe+3;H0:8].[Fe+3;H0:9].[Fe+3;H0:10]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:3])-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[Fe+2;H0:7].[Fe+2;H0:8].[Fe+2;H0:9].[Fe+2;H0:10]
Reaction
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References

TitleAuthorsDatePubMed ID
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.Ostergaard J, Persiau G, Davey MW, Bauw G, Van Montagu M1997 Nov 289374475
Purification and properties of L-galactono-gamma-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots.Oba K, Ishikawa S, Nishikawa M, Mizuno H, Yamamoto T1995 Jan7775377
Biological synthesis of L-ascorbic acid: the conversion of L-galactono-gamma-lactone into L-ascorbic acid by plant mitochondria.MAPSON LW, ISHERWOOD FA, CHEN YT1954 Jan13126087
Synthesis of L-ascorbic acid in plants and animals.ISHERWOOD FA, CHEN YT, MAPSON LW1954 Jan13126085