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Information on EC 1.8.3.2 - thiol oxidase and Organism(s) Mus musculus and UniProt Accession Q3TMX7
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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
-
relay
-
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: Mus musculus
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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ERv2p
-
-
-
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oxidase, thiol
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-
-
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QSOX
sulfhydryl oxidase
sulfhydryl oxidase SOx-3
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-
-
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thiooxidase
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-
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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
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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-
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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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
mutations at a cis-proline in QSOX1 that is conserved across the thioredoxin superfamily result in QSOX1 variants that showed a striking detrimental effect when added exogenously to fibroblasts. They severely disrupt the extracellular matrix and cell adhesion, even in the presence of naturally secreted, wild-type enzyme (QSOX1)
physiological function
among other potential functions, QSOX1 supports extracellular matrix assembly in fibroblast cultures
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). QSOX2_MOUSE
692
1
77775
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
glycoprotein
2 putative N-glycosylation sites at residues 133-135 and 246-248
proteolytic modification
cleavage of 32 amino acids at the proteolytic site
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63.2
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis
DNA and amino acid sequence determination and analysis expression in human embryonic kidney HEK cells and in rat kangaroo kidney epithelium Pt-K2 cells
gene QSOX1, DNA and amino acid sequence comparisons and phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsuba, S.; Suga, Y.; Ishidoh, K.; Hashimoto, Y.; Takamori, K.; Kominami, E.; Wilhelm, B.; Seitz, J.; Ogawa, H.
Sulfhydryl oxidase (SOx) from mouse epidermis: molecular cloning, nucleotide sequence, and expression of recombinant protein in the cultured cells
J. Dermatol. Sci.
30
50-62
2002
Mus musculus (Q8BND5), Mus musculus
Bon, K.; Adami, P.; Esnard, F.; Jouvenot, M.; Versaux-Botteri, C.
Olfactory epithelium destruction by ZnSO4 modified sulfhydryl oxidase expression in mice
NeuroReport
16
179-182
2005
Mus musculus
Chin, K.T.; Kang, G.; Qu, J.; Gardner, L.B.; Coetzee, W.A.; Zito, E.; Fishman, G.I.; Ron, D.
The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load
FASEB J.
25
2583-2591
2011
Mus musculus
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)
Javitt, G.; Grossman-Haham, I.; Alon, A.; Resnick, E.; Mutsafi, Y.
Tal Ilani, and Deborah Fass cis-Proline mutants of quiescin sulfhydryl oxidase 1 with altered redox properties undermine extracellular matrix integrity and cell adhesion in fibroblast cultures
Protein Sci.
28
228-238
2019
Mus musculus (Q8BND5)
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