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Literature summary for 1.1.3.8 extracted from
- Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes (1982), Biochemistry, 21, 5076-5082.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.007 | - |
L-gulono-1,4-lactone | - |
Gallus gallus |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microsome | - |
Gallus gallus | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
x * 50000, SDS-PAGE | Gallus gallus |
| 400000 | - |
gel filtraton | Gallus gallus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-gulono-1,4-lactone + O2 | Gallus gallus | the enzyme has a configurational specificity for the hydroxyl group at C(2) | L-xylo-hex-3-ulonolactone + H2O2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Gallus gallus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2 | product isomerizes spontaneously to L-ascorbate | Gallus gallus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | - |
Gallus gallus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3.43 | - |
L-ascorbate synthesis | Gallus gallus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-altrono-1,4-lactone + O2 | 16% as active as L-gulono-1,4-lactone | Gallus gallus | ? | - |
? | |
| D-mannono-1,4-lactone + O2 | 64% as active as L-gulono-1,4-lactone | Gallus gallus | ? | - |
? | |
| L-galactono-1,4-lactone + O2 | 90% as active as L-gulono-1,4-lactone | Gallus gallus | L-ascorbic acid + H2O2 | - |
? | |
| L-gulono-1,4-lactone + O2 | the enzyme has a configurational specificity for the hydroxyl group at C-2 | Gallus gallus | L-xylo-hex-3-ulonolactone + H2O2 | product isomerizes spontaneously to L-ascorbate | ? | |
| L-gulono-1,4-lactone + O2 | the enzyme has a configurational specificity for the hydroxyl group at C(2) | Gallus gallus | L-xylo-hex-3-ulonolactone + H2O2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| oligomer | x * 50000, SDS-PAGE | Gallus gallus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Gallus gallus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
in phosphate-citrate buffer | Gallus gallus |
| 8 | - |
in Tris-citrate buffer | Gallus gallus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | 1 mol FAD per protein monomer | Gallus gallus | |
| FAD | 8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis | Gallus gallus | |
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