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Literature summary for 1.3.3.12 extracted from

  • Kudryashova, E.V.; Leferink, N.G.; Slot, I.G.; van Berkel, W.J.
    Galactonolactone oxidoreductase from Trypanosoma cruzi employs a FAD cofactor for the synthesis of vitamin C (2011), Biochim. Biophys. Acta, 1814, 545-552.
    View publication on PubMed
Search for more literature for 1.3.3.12

Application

Application Comment Organism
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)

Cloned (Comment) Organism
recombinant expression of the N-terminally His6-tagged enzyme in inclusion bodies in Escherichia coli strain BL21(DE3) Trypanosoma cruzi

Protein Variants

Protein Variants Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-galactono-1,4-lactone + O2 Trypanosoma cruzi
-
 L-ascorbate + H2O2
-
 ?
L-galactono-1,4-lactone + O2 Trypanosoma cruzi X10/6
-
 L-ascorbate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi
-
-
-
Trypanosoma cruzi X10/6
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

Renatured (Comment) Organism
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]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-arabinono-1,4-lactone + 1,4-benzoquinone artificial electron acceptor Trypanosoma cruzi ? + 1,4-benzoquinol
-
 ?
D-arabinono-1,4-lactone + 1,4-benzoquinone artificial electron acceptor Trypanosoma cruzi X10/6 ? + 1,4-benzoquinol
-
 ?
D-arabinono-1,4-lactone + O2
-
 Trypanosoma cruzi ? + H2O2
-
 ?
D-arabinono-1,4-lactone + O2
-
 Trypanosoma cruzi X10/6 ? + H2O2
-
 ?
L-galactono-1,4-lactone + 1,4-benzoquinone artificial electron acceptor Trypanosoma cruzi L-ascorbate + 1,4-benzoquinol
-
 ?
L-galactono-1,4-lactone + 1,4-benzoquinone artificial electron acceptor Trypanosoma cruzi X10/6 L-ascorbate + 1,4-benzoquinol
-
 ?
L-galactono-1,4-lactone + O2
-
 Trypanosoma cruzi L-ascorbate + H2O2
-
 ?
L-galactono-1,4-lactone + O2
-
 Trypanosoma cruzi X10/6 L-ascorbate + H2O2
-
 ?
additional information the refolded enzyme is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone Trypanosoma cruzi ?
-
 ?
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

Subunits Comment Organism
monomer or dimer
-
 Trypanosoma cruzi

Synonyms

Synonyms Comment Organism
GAL
-
 Trypanosoma cruzi
galactonolactone oxidoreductase
-
 Trypanosoma cruzi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at, substrate L-galactono-1,4-lactone Trypanosoma cruzi
8.8
-
 assay at, substrate D-arabinono-1,4-lactone Trypanosoma cruzi

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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
metabolism the enzyme is important in vitamin C biosynthesis Trypanosoma cruzi