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Information on EC 1.8.3.2 - thiol oxidase and Organism(s) Homo sapiens and UniProt Accession O00391

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     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.3 With oxygen as acceptor
                1.8.3.2 thiol oxidase
IUBMB Comments
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: O00391
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
Ac92, ALR, ALRp, augmenter of liver regeneration, DTT-oxidase, E10R, egg white oxidase, Ero1, Ero1p, ERV/ALR sulfhydryl oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ALRp
247
-
augmenter of liver regeneration
247
-
DTT-oxidase
-
-
-
-
Erv1
299886
-
ERv2p
-
-
-
-
FAD-linked sulfhydryl oxidase ALR
299886
-
flavin-dependent sulfhydryl oxidase
247
-
hepatopoietin
247
-
neuroblastoma-derived sulfhydryl oxidase
247
-
oxidase, thiol
-
-
-
-
QSCN6
277217
-
QSOx1
QSOX2
Quiescin Q6
quiescin Q6 sulfhydryl oxidase 1
277217
-
quiescin sulfhydryl oxidase
277217
-
quiescin sulfhydryl oxidase 1
277217
-
quiescin-like flavin-dependent sulfhydryl oxidase
247
-
Quiescin-sulfhydryl oxidase
sfALR
247
-
SOXN
247
-
sulfhydryl oxidase
sulfhydryl oxidase SOx-3
-
-
-
-
thiooxidase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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 hide
9029-39-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
-
the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
the enzyme forms large amounts of neutral semiquinone, which arises between flavin centers within the dimer, during aerobic turnover with DTT
-
-
ir
dithiothreitol + reduced cytochrome c
dithiothreitol disulfide + oxidized cytochrome c
show the reaction diagram
-
cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
O00391
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
-
the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DTT
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rapid reaction studies show that dithiothreitol generates a transient mixed disulfide intermediate with sfALR signaled by a weak charge-transfer interaction between the thiolate of C145 and the oxidized flavin, reducing the transfer of reducing equivalents and reoxidation of the reduced flavin by molecular oxygen
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 2.1
dithiothreitol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83 - 1.25
dithiothreitol
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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expression analysis of a panel of cDNAs derived from 50 clinically-graded normal and malignant breast tissue samples for the expression of QSOX1 mRNAs, significant correlation between relative transcript level and clinical grade malignant breast tumors
Manually annotated by BRENDA team
high expression level of QSOX1
Manually annotated by BRENDA team
-
immunohistochemical expression of the protein quiescin sulfhydryl oxidase 1 (QSOX1) in samples obtained from untreated neuroblastomas with the patients' clinical and pathological prognostic factors and clinical course. The immunoexpression of QSOX1 correlates with the type of tumor stroma and is higher in Schwannian stroma-rich tumors. Statistically significant correlation between QSOX1 expression and well-differentiated neuroblastomas
Manually annotated by BRENDA team
-
immunohistochemic enzyme localization study in hair follicles and keratine structures in the human hair, overview
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
several cell lines
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
outer, associated
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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the extracellular location of QSOX proteins suggests that they may be involved in the remodelling of the extracellular matrix, particularly because QSOX can catalyse the formation of disulfide bridges, which are needed for the appropriate folding and stability of various matrix proteins. The expression of QSOX1 in neuroblastoma tumors may influence its clinical course because this protein is involved in processes such as the maturation of the extracellular matrix and the induction of apoptosis in these tumors
evolution
malfunction
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substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
physiological function
additional information
-
E143 and E144 are active site residues in the CxxC motif
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
QSOX1_HUMAN
747
1
82578
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
gel filtration
60000
-
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
78000
-
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
dimer
homodimer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
probably
additional information
-
enzyme contains a signal sequence
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial QSOX1 crystal structure reveals a single-chain pseudo-dimer mimicking the quaternary structure of Erv family enzymes. One pseudo-dimer subunit has lost its cofactor and catalytic activity
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C124A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
C15A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C15A/C124A
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site-directed mutagenesis, decreased activity compared to the wild-type enzyme
C15A/C74A/C85A/C124A
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site-directed mutagenesis, increased activity compared to the wild-type enzyme
C74A/C85A
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site-directed mutagenesis, decreased activity compared to the wild-type enzyme
E143K/E144K
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site-directed mutagenesis, substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
R194H
mutation isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant liver enzymes from Escherichia coli strain BL21(DE3)
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
CHO-tPA cell-line stably expressing QSOX1-V5 with a C-terminal KDEL sequence
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expression in Escherichia coli
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gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis
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gene QSOX1, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis, two putative alternative splicing variants might contribute to the differences in expression level between exon 7 and the 3'UTR are QSOX1d and QSOX1e. In QSOX1d the thioredoxin TRX1 domain remains intact, whilst the TRX2 and HRR domains are removed completely, making these isoforms similar to plant QSOXs which lack the second Trx domain but have the same three redox sites. TRX1 is truncated at its C-terminus in QSOX1e and both of the splicing
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genes QSCN6 or QSOX1, and QSOX2, DNA and amino acid sequence determination and analysis, QSCN6 or QSOX1 is located on chromosome 1q25.2, QSOX2 on chromosome 9q34, gene structure
expression of His6-tagged Alrp in Escherichia coli, expression of GFP-fusion enzyme in cell culture
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gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis
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gene SOXN, DNA and amino acid sequence determination, gene maps to chromosome 9q34.3, subcloning in Escherichia coli strain DH10B, in vitro-transcription and -translation
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overexpression of wild-type and mutant liver enzymes in Escherichia coli strain BL21(DE3) with a longer or shorter linker His-tag, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
additional information
-
overexpression of QSOX1a suppresses the lethality of a complete deletion of endoplasmic reticulum oxidase 1 in yeast and restores disulfide bond formation. The enzyme has a minimal role in catalysis of disulfide bonds within the endoplasmic reticulum
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clare, D.A.; Horton, H.R.; Stabel, T.J.; Swaisgood, H.E.; Lecce, J.G.
Tissue distribution of mammalian sulfhydryl oxidase
Arch. Biochem. Biophys.
230
138-145
1984
Bos taurus, Capra hircus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kaul, D.; Dhawan, V.; Kaur, M.
Evidence and nature of a novel thiol-oxidase in human platelets
Mol. Cell. Biochem.
159
81-84
1996
Homo sapiens
Manually annotated by BRENDA team
Raje, S.; Glynn, N.M.; Thorpe, C.
A continuous fluorescence assay for sulfhydryl oxidase
Anal. Biochem.
307
266-272
2002
Bos taurus, Gallus gallus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Thorpe, C.; Hoober, K.L.; Raje, S.; Glynn, N.M.; Burnside, J.; Turi, G.K.; Coppock, D.L.
Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes
Arch. Biochem. Biophys.
405
1-12
2002
Aspergillus niger, Cavia porcellus, Gallus gallus, Homo sapiens, Homo sapiens (O00391), Rattus norvegicus (Q6IUU3), Saccharomyces cerevisiae, Trypanosoma brucei
Manually annotated by BRENDA team
Farrell, S.R.; Thorpe, C.
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity
Biochemistry
44
1532-1541
2005
Homo sapiens
Manually annotated by BRENDA team
Wittke, I.; Wiedemeyer, R.; Pillmann, A.; Savelyeva, L.; Westermann, F.; Schwab, M.
Neuroblastoma-derived sulfhydryl oxidase, a new member of the sulfhydryl oxidase/Quiescin6 family, regulates sensitization to interferon gamma-induced cell death in human neuroblastoma cells
Cancer Res.
63
7742-7752
2003
Homo sapiens, Homo sapiens (Q6ZRP7)
Manually annotated by BRENDA team
Hoober, K.L.; Thorpe, C.
Flavin-dependent sulfhydryl oxidases in protein disulfide bond formation
Methods Enzymol.
348
30-34
2002
Aspergillus niger, Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Hofhaus, G.; Lisowsky, T.
Sulfhydryl oxidases as factors for mitochondrial biogenesis
Methods Enzymol.
348
314-324
2002
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Chakravarthi, S.; Jessop, C.E.; Willer, M.; Stirling, C.J.; Bulleid, N.J.
Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1
Biochem. J.
404
403-411
2007
Homo sapiens, Homo sapiens (O00391)
Manually annotated by BRENDA team
Alon, A.; Heckler, E.J.; Thorpe, C.; Fass, D.
QSOX contains a pseudo-dimer of functional and degenerate sulfhydryl oxidase domains
FEBS Lett.
584
1521-1525
2010
Homo sapiens, Homo sapiens (O00391)
Manually annotated by BRENDA team
Sztolsztener, M.E.; Brewinska, A.; Guiard, B.; Chacinska, A.
Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40
Traffic
14
309-320
2013
Homo sapiens, Homo sapiens (P55789)
Manually annotated by BRENDA team
Zhan, Y.A.; Abskharon, R.; Li, Y.; Yuan, J.; Zeng, L.; Dang, J.; Martinez, M.C.; Wang, Z.; Mikol, J.; Lehmann, S.; Bu, S.; Steyaert, J.; Cui, L.; Petersen, R.B.; Kong, Q.; Wang, G.X.; Wohlkonig, A.; Zou, W.Q.
Quiescin-sulfhydryl oxidase inhibits prion formation in vitro
Aging
8
3419-3429
2016
Homo sapiens
Manually annotated by BRENDA team
Alibardi, L.
Ultrastructural localization of hair keratins, high sulfur keratin-associated proteins and sulfhydryl oxidase in the human hair
Anat. Sci. Int.
92
248-261
2017
Homo sapiens, Homo sapiens (Q6ZRP7)
Manually annotated by BRENDA team
Schaefer-Ramadan, S.; Gannon, S.A.; Thorpe, C.
Human augmenter of liver regeneration probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase
Biochemistry
52
8323-8332
2013
Homo sapiens
Manually annotated by BRENDA team
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 (A0A088A7I5), 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)
Manually annotated by BRENDA team
Araujo, D.G.; Nakao, L.; Gozzo, P.; Souza, C.D.; Balderrama, V.; Gugelmin, E.S.; Kuczynski, A.P.; Olandoski, M.; de Noronha, L.
Expression level of quiescin sulfhydryl oxidase 1 (QSOX1) in neuroblastomas
Eur. J. Histochem.
58
2228
2014
Homo sapiens, Homo sapiens (O00391)
Manually annotated by BRENDA team
Soloviev, M.; Esteves, M.P.; Amiri, F.; Crompton, M.R.; Rider, C.C.
Elevated transcription of the gene QSOX1 encoding quiescin Q6 sulfhydryl oxidase 1 in breast cancer
PLoS ONE
8
e57327
2013
Homo sapiens, Homo sapiens (O00391)
Manually annotated by BRENDA team
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