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Literature summary extracted from

  • Limor-Waisberg, K.; Alon, A.; Mehlman, T.; Fass, D.
    Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase (2012), FEBS Lett., 586, 4119-4125.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 expression in Escherichia coli Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.2 C72A/C75A activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol Arabidopsis thaliana
1.8.3.2 additional information recombinant enzyme does not apparently transfer electrons from its Trx domain to its Erv domain to accomplish rapid oxidation of highly reducing model dithiol substrates, and the measured sulfhydryl oxidase activity reflects the activity of the Erv domain alone, limited by a high KM for dithiothreitol and likely other thiol substrates Arabidopsis thaliana

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.2 47000
-
 x * 47000, SDS-PAGE Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Arabidopsis thaliana Q8W4J3 isoform Qsox1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 dithiothreitol + O2
-
 Arabidopsis thaliana ? + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.3.2 ? x * 47000, SDS-PAGE Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 QSOx1
-
 Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 flavin enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm Arabidopsis thaliana