Literature summary for 1.8.3.2 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.

Search for more literature for 1.8.3.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
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
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]

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

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q8W4J3	isoform Qsox1	-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
QSOx1	-	Arabidopsis thaliana

Cofactor

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

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Release 2023.1 (January 2023)