| Entry |
|
| Name |
L-galactonolactone dehydrogenase;
galactonolactone dehydrogenase;
L-galactono-gamma-lactone dehydrogenase;
L-galactono-gamma-lactone:ferricytochrome-c oxidoreductase;
GLDHase;
GLDase
|
| Class |
Oxidoreductases;
Acting on the CH-CH group of donors;
With a cytochrome as acceptor
 |
| Sysname |
L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
|
| Reaction(IUBMB) |
L-galactono-1,4-lactone + 4 ferricytochrome c = L-dehydroascorbate + 4 ferrocytochrome c + 4 H+ (overall reaction) [RN: R00640];
(1a) L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c + 2 H+ [RN: R07679];
(1b) L-ascorbate + 2 ferricytochrome c = L-dehydroascorbate + 2 ferrocytochrome c + 2 H+ (spontaneous)
|
| Reaction(KEGG) |
|
| Substrate |
L-galactono-1,4-lactone [CPD: C01115];
ferricytochrome c [CPD: C00125];
L-ascorbate [CPD: C00072]
|
| Product |
|
| Comment |
This enzyme catalyses 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 [5]. The enzyme is 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 [5]. FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor [5].
|
| History |
EC 1.3.2.3 created 1961, modified 2006
|
| Pathway |
| Ascorbate and aldarate metabolism | | Metabolic pathways | | Biosynthesis of secondary metabolites |
|
| Orthology |
| L-galactono-1,4-lactone dehydrogenase |
|
| Genes |
ATH: | | ALY: | | CRB: | | EUS: | | BRP: | | BNA: | | THJ: | | CIT: | | CIC: | | TCC: | | GRA: | | GHI: | | EGR: | | GMX: | | PVU: | | VRA: | | VAR: | | CCAJ: | | MTR: | | CAM: | | ADU: | | AIP: | | LJA: | | LANG: | | FVE: | | PPER: | | PMUM: | | MDM: | | PXB: | | ZJU: | | CSV: | | CMO: | | RCU: | | JCU: | | POP: | | VVI: | | SLY: | | SPEN: | | SOT: | | INI: | | SIND: | | BVG: | | NNU: | | OSA: | | DOSA: | | OBR: | | BDI: | | ZMA: | | SITA: | | PDA: | | EGU: | | MUS: | | ATR: | | SMO: | | PPP: | | CRE: | | VCN: | | OLU: | | OTA: | | BPG: | | MIS: | | MPP: | | CSL: | | CVR: | | APRO: | | CME: | | CCP: | | MBR: | | SRE: | | SMIN: | | PTI: | | FCY: | | TPS: | | AAF: | | NGD: | | PIF: | | PSOJ: | | SPAR: | | EHX: | | GTT: | | » show all
 |
| Reference |
1 |
| Authors |
Mapson, L.W. and Breslow, E. |
| Title |
Properties of partially purified L-galactono-gamma-lactone dehydrogenase. |
| Journal |
Biochem. J. 65 (1957) 29. |
| Reference |
|
| Authors |
MAPSON LW, ISHERWOOD FA, CHEN YT. |
| Title |
Biological synthesis of L-ascorbic acid: the conversion of L-galactono-gamma-lactone into L-ascorbic acid by plant mitochondria. |
| Journal |
Biochem. J. 56 (1954) 21-8. |
| Reference |
|
| Authors |
ISHERWOOD FA, CHEN YT, MAPSON LW. |
| Title |
Synthesis of L-ascorbic acid in plants and animals. |
| Journal |
Biochem. J. 56 (1954) 1-15. |
| Reference |
|
| Authors |
Oba K, Ishikawa S, Nishikawa M, Mizuno H, Yamamoto T. |
| Title |
Purification and properties of L-galactono-gamma-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots. |
| Journal |
J. Biochem. (Tokyo). 117 (1995) 120-4. |
| Reference |
|
| Authors |
Ostergaard J, Persiau G, Davey MW, Bauw G, Van Montagu M. |
| Title |
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. |
| Journal |
J. Biol. Chem. 272 (1997) 30009-16. |
| Sequence |
|
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 9029-02-1 |
| LinkDB |
 |