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ENZYME entry: EC 1.3.2.3

Accepted Name
L-galactonolactone dehydrogenase.
Alternative Name(s)
Galactonolactone dehydrogenase.
GLDase.
GLDHase.
L-galactono-gamma-lactone dehydrogenase.
Reaction catalysed
L-galactono-1,4-lactone + 4 ferricytochrome c <=> L-dehydroascorbate + 4 ferrocytochrome c + 4 H(+)
Comment(s)
  • Catalyzes the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds.
  • Very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma- lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates.
  • FAD, NAD(+), NADP(+) and O(2) (cf. EC 1.3.3.12) cannot act as electron acceptor.
Cross-references
BRENDA1.3.2.3
EC2PDB1.3.2.3
ExplorEnz1.3.2.3
PRIAM enzyme-specific profiles1.3.2.3
KEGG Ligand Database for Enzyme Nomenclature1.3.2.3
IUBMB Enzyme Nomenclature1.3.2.3
IntEnz1.3.2.3
MEDLINEFind literature relating to 1.3.2.3
MetaCyc1.3.2.3
UniProtKB/Swiss-Prot
Q2RAP0, GLDH1_ORYSJ;  Q2QXY1, GLDH2_ORYSJ;  Q9SU56, GLDH_ARATH;  
O47881, GLDH_BRAOL;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-