Any feedback?
Information on EC 1.8.3.2 - thiol oxidase and Organism(s) Rattus norvegicus and UniProt Accession Q63042
for references in articles please use BRENDA:EC1.8.3.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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'.
Specify your search results
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: Rattus norvegicus
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 belongs to the quiescin Q6/FAD-dependent sulfhydryl oxidase QSOX family
additional information
-
enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family
additional information
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
?
D-penicillamine + O2
? + H2O
-
33% of the activity with dithiothreitol
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
-
-
?
additional information
?
-
redox cycling of the FAD moiety is essential for enzyme activity
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite
-
-
?
GSH + O2 + O2
GSSG + H2O
-
0.7% of the activity with dithiothreitol
-
?
N-acetylcysteine + O2
? + H2O
-
4.6% of the activity with dithiothreitol
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in the extracellular matrix as well as in intracellular folding of secreted proteins or hormons like LH and FSH, enzyme acts as an endogenous redox modulator of hormonal secretion, enzyme expression is regulated by estrogens
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
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 role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in the extracellular matrix as well as in intracellular folding of secreted proteins or hormons like LH and FSH, enzyme acts as an endogenous redox modulator of hormonal secretion, enzyme expression is regulated by estrogens
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
inhibition of enzyme from kidney and small intestine, no inhibition of enzyme from skin and seminal vesivles
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
-
high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the activity with small thiols is dominated by the Km value
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 8.2
-
oxidation of 5,5'-dithiobis(2-nitrobenzoic acid) and reactivation of ribonuclease
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high expression in neurons producing disulfide-bounded neuropeptides
-
especially in neurons throughout the rostrocaudal extent of the brain as well as in the spinal cord, in olfactory bulbs, isocortex, hippocampus, basal telencephalon, several thalamic and hypothalamic nuclei, cerebellum, and brainstem nuclei
additional information
additional information
-
detailed analysis of cellular and subcellular enzyme localization, overview
additional information
-
in-situ detection of enzyme expression in pituitary gland
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated to basal-lateral region of the plasma membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the extracellular enzyme (QSOX1b) transduces migratory and mitogenic responses in primary vascular smooth muscle cells by distinct pathways. The migratory pathway is triggered by active QSOX1b and depends on hydrogen peroxide from Nox1-derived superoxide. The enzyme has a role in neointima formation in balloon-injured rat carotid
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). ALR_RAT
198
0
22837
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
dimer
crystal structure, stabilization by extensive noncovalent interactions and a network of hydrogen bonds, structure fo the dimer interface
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
two potential sites for N-glycosylation. One of them is used and the 64000 Da purified protein is transformed to 61000 da by the action of endoglycosidase F
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant liver enzyme, native enzyme and selenomethionine enzyme, the latter is produced by microseeding with native enzyme, X-ray diffraction structure determination and analysis at 1.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C62S
site directed mutagenesis, inactive mutant, Cys62 is involved in redox cycling of the FAD moiety
C62S/C65S
site directed mutagenesis, inactive mutant, Cys62 and Cys65 are involved in redox cycling of the FAD moiety
C65S
site directed mutagenesis, inactive mutant, Cys65 is involved in redox cycling of the FAD moiety
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
15 min, 85% loss of activity. 30 min, complete loss of activity
additional information
additional information
-
dithiothreitol, 1 mM, increases the stability to heating
additional information
-
dithiothreitol, 1 mM, increases the stability to heating
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by heat treatment, ethanol precipitation, ion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, gene structure
expression of wild-type and mutant enzymes in Escherichia coli strain BC21
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goldsmith, L.A.
Sulfhydryl oxidase from rat skin
Methods Enzymol.
143
510-515
1987
Rattus norvegicus
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
Lash, L.H.; Jones, D.P.
Characterization of the membrane-associated thiol oxidase activity of rat small-intestinal epithelium
Arch. Biochem. Biophys.
225
344-352
1983
Rattus norvegicus
Lash, L.H.; Jones, D.P.
Localization of the membrane-associated thiol oxidase of rat kidney to the basal-lateral plasma membrane
Biochem. J.
203
371-376
1982
Rattus norvegicus
Takamori, K.; Thorpe, J.M.; Goldsmith, L.A.
Skin sulfhydryl oxidase. Purification and some properties
Biochim. Biophys. Acta
615
309-323
1980
Rattus norvegicus
Lash, L.H.; Jones, D.P.; Orrenius, S.
The renal thiol (glutathione) oxidase. Subcellular localization and properties
Biochim. Biophys. Acta
779
191-200
1984
Bos taurus, Rattus norvegicus
Benayoun, B.; Esnard-Feve, A.; Castella, S.; Courty, Y.; Esnard, F.
Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family
J. Biol. Chem.
276
13830-13837
2001
Rattus norvegicus (Q6IUU3)
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
Mairet-Coello, G.; Tury, A.; Esnard-Feve, A.; Fellmann, D.; Risold, P.Y.; Griffond, B.
FAD-linked sulfhydryl oxidase QSOX: topographic, cellular, and subcellular immunolocalization in adult rat central nervous system
J. Comp. Neurol.
473
334-363
2004
Rattus norvegicus
Tury, A.; Mairet-Coello, G.; Poncet, F.; Jacquemard, C.; Risold, P.Y.; Fellmann, D.; Griffond, B.
QSOX sulfhydryl oxidase in rat adenohypophysis: localization and regulation by estrogens
J. Endocrinol.
183
353-363
2004
Rattus norvegicus
Wu, C.K.; Dailey, T.A.; Dailey, H.A.; Wang, B.C.; Rose, J.P.
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase
Protein Sci.
12
1109-1118
2003
Rattus norvegicus (Q6IUU3)
Radom, J.; Colin, D.; Thiebault, F.; Dognin-Bergeret, M.; Mairet-Coello, G.; Esnard-Feve, A.; Fellmann, D.; Jouvenot, M.
Identification and expression of a new splicing variant of FAD-sulfhydryl oxidase in adult rat brain
Biochim. Biophys. Acta
1759
225-233
2006
Rattus norvegicus (Q6IUU3)
Tury, A.; Mairet-Coello, G.; Lisowsky, T.; Griffond, B.; Fellmann, D.
Expression of the sulfhydryl oxidase ALR (Augmenter of Liver Regeneration) in adult rat brain
Brain Res.
1048
87-97
2005
Rattus norvegicus (Q63042)
Tury, A.; Mairet-Coello, G.; Esnard-Feve, A.; Benayoun, B.; Risold, P.Y.; Griffond, B.; Fellmann, D.
Cell-specific localization of the sulphydryl oxidase QSOX in rat peripheral tissues
Cell Tissue Res.
323
91-103
2006
Rattus norvegicus (Q6IUU3)
Mairet-Coello, G.; Tury, A.; Fellmann, D.; Risold, P.Y.; Griffond, B.
Ontogenesis of the sulfhydryl oxidase QSOX expression in rat brain
J. Comp. Neurol.
484
403-417
2005
Rattus norvegicus
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)
Morel, C.; Adami, P.; Musard, J.F.; Duval, D.; Radom, J.; Jouvenot, M.
Involvement of sulfhydryl oxidase QSOX1 in the protection of cells against oxidative stress-induced apoptosis
Exp. Cell Res.
313
3971-3982
2007
Rattus norvegicus, Cavia porcellus (O08841), Cavia porcellus
Franca, K.C.; Martinez, P.A.; Prado, M.L.; Lo, S.M.; Borges, B.E.; Zanata, S.M.; San Martin, A.; Nakao, L.S.
Quiescin/sulfhydryl oxidase 1b (QSOX1b) induces migration and proliferation of vascular smooth muscle cells by distinct redox pathways
Arch. Biochem. Biophys.
679
108220
2020
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 1.8.3.2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
