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Information on EC 1.8.3.2 - thiol oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8W4J3
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1.8.3.2 thiol oxidaseIUBMB Comments
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
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Word Map
- 1.8.3.2
- hepatocytes
-
intermembrane
- oxidases
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relay
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qsoxs
- thioredoxin
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redox-active
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hepatectomy
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hepatotrophic
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reoxidized
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hepatectomized
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flavoenzyme
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fad-dependent
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fad-binding
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oxidoreductins
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flavin-linked
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redox-regulated
- isoalloxazine
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3h-tdr
- diagnostics
- medicine
- nutrition
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
qsox1, sulfhydryl oxidase, augmenter of liver regeneration, ero1p, thiol oxidase, hepatopoietin, erv2p, erv1p, sulphydryl oxidase, sfalr, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DTT-oxidase
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-
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Erv1
ERv2p
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-
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oxidase, thiol
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-
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sulfhydryl oxidase
sulfhydryl oxidase SOx-3
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thiooxidase
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additional information
the enzyme belongs to the Erv1/Alr sulfhydryl oxidase family
sulfhydryl oxidase
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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
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif YPCCXXC
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
thiol:oxygen oxidoreductase
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
CAS REGISTRY NUMBER
COMMENTARY
9029-39-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cysteine + O2
cystine + H2O2
artificial in vitro substrate
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ir
additional information
?
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no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
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-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
artificial in vitro substrate
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ir
R-SH + O2
R-S-S-R + H2O2
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
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ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
R-SH + O2
R-S-S-R + H2O2
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
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ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
FAD
dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
evolution
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). QSOX1_ARATH
528
1
60087
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C72A/C75A
activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol
additional information
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
additional information
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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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged full length enzyme and C-terminal fragment from Escherichia coli strain BL21 to homogeneity by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis
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
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levitan, A.; Danon, A.; Lisowsky, T.
Unique features of plant mitochondrial sulfhydryl oxidase
J. Biol. Chem.
279
20002-20008
2004
Arabidopsis thaliana (Q8GXX0)
Vitu, E.; Bentzur, M.; Lisowsky, T.; Kaiser, C.A.; Fass, D.
Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide
J. Mol. Biol.
362
89-101
2006
Arabidopsis thaliana, Saccharomyces cerevisiae (Q12284)
Fass, D.
The Erv family of sulfhydryl oxidases
Biochim. Biophys. Acta
1783
557-566
2008
African swine fever virus, Oryza sativa, Vaccinia virus, Saccharomyces cerevisiae (Q12284), Rattus norvegicus (Q63042), Arabidopsis thaliana (Q8GXX0)
Farver, O.; Vitu, E.; Wherland, S.; Fass, D.; Pecht, I.
Electron transfer reactivity of the Arabidopsis thaliana sulfhydryl oxidase AtErv1
J. Biol. Chem.
284
2098-2105
2009
Arabidopsis thaliana (Q8GXX0), Arabidopsis thaliana
Limor-Waisberg, K.; Alon, A.; Mehlman, T.; Fass, D.
Phylogenetics and enzymology of plant quiescin sulfhydryl oxidase
FEBS Lett.
586
4119-4125
2012
Arabidopsis thaliana (Q8W4J3), Arabidopsis thaliana
Limor-Waisberg, K.; Ben-Dor, S.; Fass, D.
Diversification of quiescin sulfhydryl oxidase in a preserved framework for redox relay
BMC Evol. Biol.
13
70
2013
Apis mellifera (A0A7M7FYF7), Arabidopsis thaliana (Q8W4J3), Arabidopsis thaliana (Q9ZU40), Branchiostoma floridae (C3ZHZ6), Coccomyxa subellipsoidea (I0YJW9), Coccomyxa subellipsoidea c-169 (I0YJW9), Danio rerio (B0UXN0), Danio rerio (F1QJL3), Daphnia pulex (E9HEH3), Drosophila melanogaster (C0PVB3), Drosophila melanogaster (Q7JQR3), Drosophila melanogaster (Q9VD61), Drosophila melanogaster (Q9VD62), Gallus gallus (F1P458), Gallus gallus (Q8JGM4), Homo sapiens (O00391), Homo sapiens (Q6ZRP7), Ixodes scapularis (B7PLS2), Micromonas pusilla (C1MIM3), Mus musculus (Q3TMX7), Mus musculus (Q8BND5), Perkinsus marinus, Selaginella moellendorffii (D8TF00), Trichoplax adhaerens (B3RPG3), Trypanosoma brucei (Q25B82), Xenopus tropicalis (Q501L2)
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