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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
structural analysis, modeling of the conserved central domain, the plant enzyme contains a unique C-terminally located CXXXXC motif and no N-terminally localized cysteine pair, which is typical for enzymes of the Erv1/Alr sulfhydryl oxidase family
activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol
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
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
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
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
gene AtErv1, DNA and amino acid sequence analysis, subcloning in Escherichia coli strain DH5alpha, expression of full length enzyme and 15 kDa C-terminal fragment as His-tagged proteins in Escherichia coli strain BL21, transient expression of the enzyme fused to GFP in protoplasts of Arabidopsis thaliana and of Physcomitrella patens with localization in the mitochondria, no complementation of the enzyme-defective yeast mutant erv-ts and yeast deletion mutant DELTAerv1