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Literature summary for 1.8.3.2 extracted from

  • Farver, O.; Vitu, E.; Wherland, S.; Fass, D.; Pecht, I.
    Electron transfer reactivity of the Arabidopsis thaliana sulfhydryl oxidase AtErv1 (2009), J. Biol. Chem., 284, 2098-2105.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of a mutant missing the active site disulfide, the mutant also exhibits a fast increase in absorption at 340 nm upon reaction with CO2-, the flavin is reduced directly by the CO2- radicals, and as for WT AtErv1 more disulfides than FAD are reduced, overview. A mutant missing the shuttle disulfide shows fast formation of RSS*R radicals at 340 nm, no intermediate phase of radical disappearance, and radical decay in a much slower pseudo-first order process compared to the structural mutant and the wild-type enzyme, The direct reduction of FAD to the semiquinone is 2fold slower than the disulfide radical formation, overview Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Arabidopsis thaliana 5739
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8GXX0
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
Arabidopsis thaliana

Subunits

Subunits Comment Organism
homodimer
-
Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
Erv1
-
Arabidopsis thaliana
sulfhydryl oxidase
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
9 13 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
FAD dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview Arabidopsis thaliana