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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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1.8.3.2 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
-
redox-active
-
hepatectomy
-
hepatotrophic
-
reoxidized
-
hepatectomized
-
flavoenzyme
-
fad-dependent
-
fad-binding
-
oxidoreductins
-
flavin-linked
-
redox-regulated
- isoalloxazine
-
3h-tdr
- diagnostics
- medicine
- nutrition
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
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
ALR
DTT-oxidase
-
-
-
-
ERv2p
-
-
-
-
oxidase, thiol
-
-
-
-
QSOX
sulfhydryl oxidase
sulfhydryl oxidase SOx-3
-
-
-
-
thiooxidase
-
-
-
-
additional information
sulfhydryl oxidase
-
-
-
-
additional information
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
additional information
-
enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family
additional information
-
enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family
additional information
enzyme belongs to the sulfhydryl oxidase/Quiescin6 family
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 CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
catalytic mechanism model using DTT and O2, overview. Stabilization of mixed disulfide intermediates in enzyme sfALR
-
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
-
-
-
-
oxidation
-
-
-
-
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
9029-39-4
-
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
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
-
the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
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
-
cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
-
-
?
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
disulfide bridge C15-C124 is not required for activity
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
?
additional information
?
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme might communicate with the respiratory chain via the mediation of cytochrome c
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
additional information
?
-
-
nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun
-
-
?
additional information
?
-
-
quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX
-
-
?
additional information
?
-
-
catalytic mechanism of the short, cytokine, form of augmenter of liver regeneration (sfALR) using model thiol substrates of the enzyme. While 2-mercaptoethanol is a very poor substrate of enzyme sfALR, it rapidly generates a mixed disulfide intermediate allowing the thiolate of C145 to form a strong charge-transfer complex with the flavin. Glutathione is unable to form charge-transfer complexes and is no substrate of the oxidase
-
-
?
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 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
-
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
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
?
additional information
?
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme might communicate with the respiratory chain via the mediation of cytochrome c
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
additional information
?
-
-
nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun
-
-
?
additional information
?
-
-
quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
at a diminutive FAD binding domain, the isoalloxazine ring of the flavin prosthetic group is bound at the mouth of a 4-helix bundle in each subunit with a 5th small helix adjacent to the adenine moiety of FAD. A proximal redox-active disulfide is located adjacent to the C4a position of the isoalloxazine ring
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
-
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
LITERATURE
IMAGE
additional information
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
-
additional information
-
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
redox potential of wild-type and mutant enzymes
-
additional information
additional information
-
binding kinetics of immobilized QSOX to various PrP prion proteins
-
additional information
additional information
-
pre-steady state kinetics and stopped-flow measurements of sfALR using DTT to slow down the reaction velocity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
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
immunohistochemic enzyme localization study in hair follicles and keratine structures in the human hair, overview
prevalent labelling in the granular, transitional and lowermost part of the stratum corneous layer
additional information
additional information
tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads
additional information
-
tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads
additional information
-
enzyme is expressed in a large number of different cell types and tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
QSOX1a-V5 is a glycosylated, transmembrane protein localized to the Golgi apparatus
protein Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
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
-
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
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
the enzyme belongs to a family of flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidases
evolution
-
augmenter of liver regeneration is a member of the ERV family of small flavin-dependent sulfhydryl oxidases that contain a redox-active CxxC disulfide bond in redox communication with the isoalloxazine ring of bound FAD
evolution
-
enzyme QSOX is an evolutionarily conserved protein present in organisms ranging from the smallest free-living eukaryotes to humans
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
physiological function
protein Alr is able to substitute for the function of Saccharomyces cerevisiae Erv1. Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria. The defective accumulation of human Mia40 in mitochondria in a recently identified disease that is caused by amino acid exchange in Alr
physiological function
-
quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins. Quiescin-sulfhydryl oxidase inhibits formation of prions, infectious glycoproteins that cause a group of fatal transmissible diseases in animals and humans, in vitro. QSOX inhibits human prion propagation in protein misfolding cyclic amplification reactions and murine prion propagation in scrapie-infected neuroblastoma cells. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains
physiological function
-
the inability of the relatively bulky glutathione to attain the in-line geometry required for efficient disulfide exchange in sfALR may be physiologically important in preventing the oxidase from catalyzing the potentially harmful oxidation of intracellular glutathione. sfALR protects against hydrogen peroxide and radiation-induced apoptosis
physiological function
epidermal sulfhydryl oxidase mainly cross-links keratins or keratins with other proteins within the corneous core of keratinocytes of the stratum granulare and of the transitional layer. The presence of disulphide bonds in corneocytes and of isopeptide bonds in the cell cornified envelope determines the high chemical, mechanical and antimicrobial resistance of the corneous layer
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_HUMAN
747
1
82578
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
monomers are linked via a disulfide bridge C15-C124, which is not critical for dimer formation, structure modeling using the enzymes crystal structure
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 contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
-
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
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
additional information
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
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
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
C15A/C74A/C85A/C124A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C74A/C85A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
E143K/E144K
-
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
additional information
antisense constructs of the SOXN gene in Tet21N neuroblastoma cells confer resistance to IFN-gamma-induced apoptosis, while ectopic overexpression in sense direction sensitizes the cells to induced cell death
additional information
-
antisense constructs of the SOXN gene in Tet21N neuroblastoma cells confer resistance to IFN-gamma-induced apoptosis, while ectopic overexpression in sense direction sensitizes the cells to induced cell death
additional information
-
the conserved C-terminal domain of the human Alrp can functionally replace the yeast domain in vivo, genetic system to study function of sulfhydryl oxidases, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant liver enzymes from Escherichia coli strain BL21(DE3)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CHO-tPA cell-line stably expressing QSOX1-V5 with a C-terminal KDEL sequence
gene QSOX, isozyme QSOX1 has two splising variants 1a and 1b, DNA and amino acid sequence comparisons and phylogenetic analysis
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
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
-
gene QSOX2, DNA and amino acid sequence comparisons and phylogenetic analysis
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
overexpression of wild-type and mutant liver enzymes in Escherichia coli strain BL21(DE3) with a longer or shorter linker His-tag, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
additional information
diagnostics
QSOX1 is a potential prognostic marker which may prove of use in the staging of breast tumours and the stratification of breast cancer patients
diagnostics
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. The enzyme can be used as a prognostic biomarker to help better discriminate among risk groups
medicine
mutation R194H has been 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
medicine
-
te enzyme might be useful in therapeutic strategies for treating prion diseases
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
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
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
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
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 (O00391), Homo sapiens, Rattus norvegicus (Q6IUU3), Saccharomyces cerevisiae, Trypanosoma brucei
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
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 (Q6ZRP7), Homo sapiens
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
Hofhaus, G.; Lisowsky, T.
Sulfhydryl oxidases as factors for mitochondrial biogenesis
Methods Enzymol.
348
314-324
2002
Saccharomyces cerevisiae, Homo sapiens
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 (O00391), Homo sapiens
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 (O00391), Homo sapiens
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 (P55789), Homo sapiens
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
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 (Q6ZRP7), Homo sapiens
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
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)
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 (O00391), Homo sapiens
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 (O00391), Homo sapiens
Alibardi, L.
Immunocytochemical localization of sulfhydryl oxidase in mammalian epidermis suggests that the enzyme cross-links keratins in the granular and transitional corneous layers
Acta Zool.
98
32-37
2017
Ornithorhynchus anatinus, Osphranter rufus, Mesocricetus auratus (A0A1U7R8Y5), Homo sapiens (Q6ZRP7)
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