Information on EC 1.8.3.2 - thiol oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.8.3.2
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RECOMMENDED NAME
GeneOntology No.
thiol oxidase
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gliotoxin biosynthesis
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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 hide
9029-39-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Autographa californica M nuclear polyhedrosis virus
AcMNPV
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cv Jack
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
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the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
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-
?
2 R-SH + FAD
R-S-S-R + FADH2
show the reaction diagram
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-
-
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?
2-mercaptoethanol + O2
? + H2O
show the reaction diagram
2-nitro-5-thiobenzoic acid + O2
? + H2O
show the reaction diagram
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
show the reaction diagram
bis-(2-mercaptoethyl)sulfone + O2
? + H2O
show the reaction diagram
-
-
-
-
?
cysteamine + O2
? + H2O
show the reaction diagram
cysteine + O2
cystine + H2O2
show the reaction diagram
artificial in vitro substrate
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ir
D-Cys + O2
? + H2O
show the reaction diagram
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-
-
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?
D-penicillamine + O2
? + H2O
show the reaction diagram
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33% of the activity with dithiothreitol
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?
dithioerythritol + O2
? + H2O
show the reaction diagram
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-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
dithiothreitol + O2
? + H2O2
show the reaction diagram
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-
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?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
dithiothreitol + reduced cytochrome c
dithiothreitol disulfide + oxidized cytochrome c
show the reaction diagram
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cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
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?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Gly-Gly-L-Cys + O2
? + H2O
show the reaction diagram
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-
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?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
show the reaction diagram
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-
-
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?
L-Cys + O2
? + H2O
show the reaction diagram
lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
N-acetyl-EAQCGTS + O2
? + H2O
show the reaction diagram
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
show the reaction diagram
ovalbumin + O2
ovalbumin disulfide + H2O2
show the reaction diagram
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-
-
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?
pancreatic RNase + O2
pancreatic RNase disulfide + H2O2
show the reaction diagram
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ir
protein A1aB1b + O2
protein A1aB1b disulfide + H2O2
show the reaction diagram
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precursor of the soybean seed storage protein glycinin, recombinantly expressed as His-tagged protein in Escherichia coli strain BL21(DE3). Recombinant GmQSOX1 catalyses disulfide-bond formation but is unable to refold the reduced and denatured precursor A1aB1b into a native form
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?
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
show the reaction diagram
protein Mia40 + O2
protein Mia40 disulfide + H2O
show the reaction diagram
protein SfP53 + O2
protein SfP53 disulfide + H2O2
show the reaction diagram
Autographa californica M nuclear polyhedrosis virus
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?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
reduced aldolase + O2
aldolase + H2O
show the reaction diagram
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?
reduced insulin A chain + O2
insulin A chain + H2O
show the reaction diagram
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?
reduced insulin B chain + O2
insulin B chain + H2O
show the reaction diagram
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?
reduced lysozyme + O2
? + H2O
show the reaction diagram
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?
reduced lysozyme + O2
lysozyme + H2O
show the reaction diagram
reduced lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
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ir
reduced ovalbumin + O2
ovalbumin + H2O
show the reaction diagram
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?
reduced pyruvate kinase + O2
pyruvate kinase + H2O
show the reaction diagram
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-
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?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
show the reaction diagram
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?
reduced ribunuclease + O2
renatured ribonuclease + H2O
show the reaction diagram
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?
reduced thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
Autographa californica M nuclear polyhedrosis virus
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r
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
show the reaction diagram
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
show the reaction diagram
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?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
RNasered + O2
? + H2O
show the reaction diagram
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?
rRNaseA + O2
? + H2O2
show the reaction diagram
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?
thioglycolate + O2
? + H2O
show the reaction diagram
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11.1% of the activity with dithiothreitol
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?
thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
tris(2-carboxyethyl)-phosphine + O2
? + H2O
show the reaction diagram
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?
Trx Escherichia coli + O2
? + H2O
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
show the reaction diagram
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
-
-
-
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?
ovalbumin + O2
ovalbumin disulfide + H2O2
show the reaction diagram
-
-
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?
protein Mia40 + O2
protein Mia40 disulfide + H2O
show the reaction diagram
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-
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?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
show the reaction diagram
-
-
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?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
MgSO4
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in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
Phosphorus
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6.60 atoms per subunit/FAD, cofactor of the FAD
Zn2+
1 mM, 95% loss of activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bathocuproine disulfonate
Cu2+
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modeling of metal binding
diazabicyclooctane
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diethyldithiocarbamate
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dithiothreitol
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at high concentrations
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
GSSG
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substrate inhibition above 0.8 mM
guanine
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iodoacetamide
iodoacetic acid
KI
Q2UA33
1 mM, 65% residual activity
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
MgSO4
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1 mM, 55% residual activity
Na2SO4
o-Dianisidine
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o-phenylenediamine
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ribonuclease
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substrate inhibition above 0.04 mM
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RNAi
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silences QSOX. Survival of QSOX-silenced insects is reduced over controls following blood digestion, most likely due to the compromised ability of mosquitoes to scavenge and/or prevent damage caused by blood meal-derived oxidative stress. Higher lipid peroxidation and mortality in QSOX-silenced mosquitoes may be an indication that the redox balance is altered in these insects after a blood meal
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sodium dodecylsulfate
Urea
Q2UA33
1 mM, 80% residual activity
ZnSO4
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
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high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein
L-Cys
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fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme
MgSO4
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in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
soybean PDI family protein
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cooperative refolding of unfolded RNase A by rGmQSOX1 and all tested soybean PDI family proteins of group I and group II, but not of group III. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1. These PDI family proteins contain two classic CGHC motifs in the a and a' domains, except for the group III PDI family proteins, which have nonclassic active centre CXXC motifs. The combination of rGmQSOX1 and GmPDIL-2 with an a-b-b'-a' domain structure shows the highest level of refolding activity, while the GmPDIL-2 C101A/C104A/C440A/C443A mutant, in which all of the cysteines in the two active centres are replaced with alanines, is devoid of cooperative oxidative refolding activity with rGmQSOX1. The refolding activity of rGmQSOX1 combined with the C104A/C443A mutant is 18% of that of rGmQSOX1 combined with wild-type GmPDIL-2. Analysis of the cooperation mechanism, overview
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staurosporine aglycone
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Triton X-100
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0-0.1% concentration, at most 30% activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.9 - 54
2-mercaptoethanol
100
2-nitro-5-thiobenzoic acid
-
-
1.25 - 30
cysteamine
1.33 - 13.1
D-Cys
0.03 - 52.2
dithiothreitol
0.14 - 12.5
DTT
0.02 - 6.7
glutathione
6.31
Gly-Gly-L-Cys
-
-
0.09 - 20
GSH
0.42 - 10.9
L-Cys
1.72
N-acetyl-EAQCGTS
-
expressed per thiol basis
1.13 - 3.85
N-acetyl-L-Cys
3.3
N-acetylcysteine
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0.0001 - 0.77
O2
0.16
reduced aldolase
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expressed per thiol basis
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0.215
reduced insulin A chain
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expressed per thiol basis
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0.3
reduced insulin B chain
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expressed per thiol basis
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0.11
reduced lysozyme
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expressed per thiol basis
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0.33
reduced ovalbumin
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expressed per thiol basis
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1.25
reduced pyruvate kinase
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expressed per thiol basis
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0.23
reduced riboflavin-binding protein
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expressed per thiol basis
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0.0174 - 0.115
Reduced ribonuclease
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0.014 - 0.36
RNAse A
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0.36
rRNaseA
pH 7.5, 37C
-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.3 - 55400
2-mercaptoethanol
5950 - 78600
D-Cys
0.83 - 337800
dithiothreitol
3.5 - 1013
DTT
66.67 - 3600000
glutathione
23.1
GSH
-
-
21.3 - 52300
L-Cys
0.7 - 1.5
O2
0.002 - 21.9
RNAse A
-
22
rRNaseA
pH 7.5, 37C
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7000 - 515000
2-mercaptoethanol
3840 - 5980
D-Cys
0.266 - 128000
dithiothreitol
2.3 - 1290000
glutathione
7600 - 8560
L-Cys
0.0023 - 0.0093
O2
19.75 - 70.45
RNAse A
-
180
rRNaseA
pH 7.5, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0026
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in 6-day newborn serum
103.8
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
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8 - 8.2
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oxidation of 5,5'-dithiobis(2-nitrobenzoic acid) and reactivation of ribonuclease
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
more than 80% of maximum activity
5 - 11
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pH 5.0: about 40% of maximal activity, pH 11: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 13
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assay at
37
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assay at
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
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egg white
Manually annotated by BRENDA team
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endometrial cells. Enzyme level increases during a serum depletion-induced quiescence, decreases when cells enter the g1 phase after serum stimulation, and is restored during the S and G2/M phases
Manually annotated by BRENDA team
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throughout the rostrocaudal extent of the brain
Manually annotated by BRENDA team
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immunohistochemic enzyme localization study in hair follicles and keratine structures in the human hair, overview
Manually annotated by BRENDA team
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high expression in neurons producing disulfide-bounded neuropeptides
Manually annotated by BRENDA team
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secretion of enzyme
Manually annotated by BRENDA team
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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
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several cell lines
Manually annotated by BRENDA team
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secretory tissue
Manually annotated by BRENDA team
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fetal and newborn serum
Manually annotated by BRENDA team
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small amounts
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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epithelial cells
Manually annotated by BRENDA team
additional information