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Literature summary for 1.2.3.4 extracted from

  • Escutia, M.R.; Bowater, L.; Edwards, A.; Bottrill, A.R.; Burrell, M.R.; Polanco, R.; Vicuna, R.; Bornemann, S.
    Cloning and sequencing of two Ceriporiopsis subvermispora bicupin oxalate oxidase allelic isoforms: implications for the reaction specificity of oxalate oxidases and decarboxylases (2005), Appl. Environ. Microbiol., 71, 3608-3616.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Gelatoporia subvermispora

General Stability

General Stability Organism
enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate (SDS) Gelatoporia subvermispora

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Soluble and active protein obtained only when the enzyme is coexpressed with the chaperones DnaK and DnaJ (G isoform) and when a manganese salt is added to the growth medium (C and G isoform) Gelatoporia subvermispora
SDS enzyme activity of the C isoform is lost in the presence of sodium dodecyl sulfate Gelatoporia subvermispora

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49800
-
C isoform, calculated from protein sequence Gelatoporia subvermispora
56000
-
G isoform, SDS-PAGE Gelatoporia subvermispora

Organism

Organism UniProt Comment Textmining
Gelatoporia subvermispora
-
ATCC 90466, oxalate oxidase allelic isoforms C and G
-

Purification (Commentary)

Purification (Comment) Organism
anion exchange chromatography, pH precipitation, phosphocellulose chromatography, gel filtration Gelatoporia subvermispora

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.2
-
C isoform Gelatoporia subvermispora
20
-
G isoform Gelatoporia subvermispora