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Literature summary extracted from
- Galactonolactone oxidoreductase from Trypanosoma cruzi employs a FAD cofactor for the synthesis of vitamin C (2011), Biochim. Biophys. Acta, 1814, 545-552.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.3.3.12 | pharmacology | because humans lack the capacity to synthesize ascorbate, the trypanosomal enzymes involved in ascorbate biosynthesis are interesting targets for drug therapy | Trypanosoma cruzi |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.3.12 | recombinant expression of the N-terminally His6-tagged enzyme in inclusion bodies in Escherichia coli strain BL21(DE3) | Trypanosoma cruzi |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.3.12 | A113G | site-directed mutagenesis, in the reaction with 1,4-benzoquinone as electron acceptor, the activity of the dimeric formof A113G is about 1.5fold higher compared to the monomer, the specific activity of the A113G variant in the reaction with molecular oxygen is about 2.5-3times lower than with 1,4-benzoquinone | Trypanosoma cruzi |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.3.12 | L-galactono-1,4-lactone + O2 | Trypanosoma cruzi | - |
L-ascorbate + H2O2 | - |
? |  |
| 1.3.3.12 | L-galactono-1,4-lactone + O2 | Trypanosoma cruzi X10/6 | - |
L-ascorbate + H2O2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.3.12 | Trypanosoma cruzi | - |
- |
- |
| 1.3.3.12 | Trypanosoma cruzi X10/6 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.3.3.12 | refolded recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by anion exchange, hydroxyapatite, and hydrophobic interaction chromatography | Trypanosoma cruzi |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 1.3.3.12 | recombinant terminally His6-tagged enzyme refolded from Escherichia coli strain BL21(DE3) inclusion bodies using a reverse micelles system. The refolded enzyme shows native-like secondary structure and is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone | Trypanosoma cruzi |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.3.3.12 | 1.19 | - |
purified recombinant refolded enzyme, substrate D-arabinono-1,4-lactone. pH 8.8, temperature not specified in the publication | Trypanosoma cruzi |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.3.12 | D-arabinono-1,4-lactone + 1,4-benzoquinone | artificial electron acceptor | Trypanosoma cruzi | ? + 1,4-benzoquinol | - |
? | |
| 1.3.3.12 | D-arabinono-1,4-lactone + 1,4-benzoquinone | artificial electron acceptor | Trypanosoma cruzi X10/6 | ? + 1,4-benzoquinol | - |
? | |
| 1.3.3.12 | D-arabinono-1,4-lactone + O2 | - |
Trypanosoma cruzi | ? + H2O2 | - |
? | |
| 1.3.3.12 | D-arabinono-1,4-lactone + O2 | - |
Trypanosoma cruzi X10/6 | ? + H2O2 | - |
? | |
| 1.3.3.12 | L-galactono-1,4-lactone + 1,4-benzoquinone | artificial electron acceptor | Trypanosoma cruzi | L-ascorbate + 1,4-benzoquinol | - |
? | |
| 1.3.3.12 | L-galactono-1,4-lactone + 1,4-benzoquinone | artificial electron acceptor | Trypanosoma cruzi X10/6 | L-ascorbate + 1,4-benzoquinol | - |
? | |
| 1.3.3.12 | L-galactono-1,4-lactone + O2 | - |
Trypanosoma cruzi | L-ascorbate + H2O2 | - |
? | |
| 1.3.3.12 | L-galactono-1,4-lactone + O2 | - |
Trypanosoma cruzi X10/6 | L-ascorbate + H2O2 | - |
? | |
| 1.3.3.12 | additional information | the refolded enzyme is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone | Trypanosoma cruzi | ? | - |
? | |
| 1.3.3.12 | additional information | the refolded enzyme is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone | Trypanosoma cruzi X10/6 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.3.12 | monomer or dimer | - |
Trypanosoma cruzi |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.3.12 | GAL | - |
Trypanosoma cruzi |
| 1.3.3.12 | galactonolactone oxidoreductase | - |
Trypanosoma cruzi |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.3.3.12 | 7.2 | - |
assay at, substrate L-galactono-1,4-lactone | Trypanosoma cruzi |
| 1.3.3.12 | 8.8 | - |
assay at, substrate D-arabinono-1,4-lactone | Trypanosoma cruzi |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.3.12 | FAD | non-covalently bound FAD as redox-active cofactor, FAD-binding domain sequence of TcGAL and comparison to related aldonolactone oxidoreductases, overview | Trypanosoma cruzi | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.3.12 | evolution | the terminal step in ascorbate biosynthesis is catalyzed by flavin-dependent aldonolactone oxidoreductases belonging to the vanillyl-alcohol oxidase (VAO) protein family | Trypanosoma cruzi |
| 1.3.3.12 | metabolism | the enzyme is important in vitamin C biosynthesis | Trypanosoma cruzi |
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