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
-
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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-
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reduction
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-
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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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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-SH + FAD
R-S-S-R + FADH2
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
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
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-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Gly-Gly-L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
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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-
-
-
?
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
-
-
-
-
?
pancreatic RNase + O2
pancreatic RNase disulfide + H2O2
show the reaction diagram
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-
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ir
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
show the reaction diagram
protein Mia40 + O2
protein Mia40 disulfide + H2O
show the reaction diagram
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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-
-
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?
reduced insulin B chain + O2
insulin B chain + H2O
show the reaction diagram
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-
-
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?
reduced lysozyme + O2
? + H2O
show the reaction diagram
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-
-
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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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-
-
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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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-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
show the reaction diagram
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-
-
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?
reduced ribunuclease + O2
renatured ribonuclease + H2O
show the reaction diagram
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-
-
?
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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-
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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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-
-
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?
rRNaseA + O2
? + H2O2
show the reaction diagram
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-
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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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-
-
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?
Trx Escherichia coli + O2
? + H2O
show the reaction diagram
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-
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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
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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?
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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?
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
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-
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?
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
-
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
GSSG
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substrate inhibition above 0.8 mM
guanine
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iodoacetamide
iodoacetic acid
KI
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
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
staurosporine aglycone
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-
Triton X-100
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0-0.1% concentration, at most 30% activation
additional information
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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
0.086 - 11.3
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
-
-
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
RNAse A
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pH 8.1, 25°C
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0.36
rRNaseA
pH 7.5, 37°C
-
additional information
additional information
-
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
Gallus gallus
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-
21.3 - 52300
L-Cys
0.7 - 1.5
O2
0.002
RNAse A
Aspergillus niger
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thiol per second
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22
rRNaseA
Trypanosoma brucei
Q585M6
pH 7.5, 37°C
-
additional information
additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7000 - 515000
2-mercaptoethanol
63
3840 - 5980
D-Cys
2269
230 - 128000
dithiothreitol
45
2.3 - 1290000
glutathione
44
7600 - 8560
L-Cys
336
0.0023 - 0.0093
O2
9
180
rRNaseA
Trypanosoma brucei
Q585M6
pH 7.5, 37°C
42634
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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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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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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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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
African swine fever virus (strain Badajoz 1971 Vero-adapted)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14378
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2 * 14378, laser desorption mass spectrometry
15000
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2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
21000
-
SDS-PAGE, under reducing conditions
23000
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SDS-PAGE, under reducing conditions
28760
-
SDS-PAGE
33000
2 * 33000, calculated and crystallization data
42412
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
43959
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
48660
-
method not mentioned
50000
-
1 * 50000 plus 1 * 55000, SDS-PAGE
53000
-
2 * 53000
54300
analytical ultracentrifugation
55000
-
1 * 50000 plus 1 * 55000, SDS-PAGE
60000
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
68000
-
x * 68000, recombinant His-tagged enzyme, SDS-PAGE
85360
MALDI-TOF mass spectrometry
89000
-
x * 89000, SDS-PAGE
93000
-
2 * 93000, SDS-PAGE
100000
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x * 100000, native enzyme, SDS-PAGE
120000
-
gel filtration
202000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
glycoprotein
proteolytic modification
additional information
enzyme contains a signal sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified unlabeled and selenomethionine-labeled pB119L-DELTAC, the protein crystallizes readily under a wide range of conditions, multiple anomalous dispersion, X-ray diffraction structure determination and analysis at 1.9 A resolution
crystal structure to 0.98 A resolution shows a configuration of the active-site cysteine residues and bound cofactor similar to that observed in other Erv sulfhydryl oxidases. Protein has a complex quaternary structural arrangement comprising a dimer of pseudodimers with a striking 40-degree kink in the interface helix between subunits
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
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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
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crystal structures at 2.0 A resolution of the C-terminal domain and at 3.0 A resolution of a C30S/C133S double mutant. The C-terminal domain exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The N-terminal domain is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the N-terminal domain to the C-terminal domain of another subunit. The four-helix bundle of the C-terminal domain forms a wide platform for the electron donor N-terminal domain. Moreover,the amphipathic helix close to the shuttle redox enter may be critical for the recognition of Mia40, the upstream electron donor
Erv2p, X-ray diffraction structure determination and analysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
24 h, more than 80% of initial activity
724654
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
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enzyme retains more than 80% of the initial activity with glutathione after 24 h incubation at 30-60°C
40
24 h, more than 70% of initial activity
57
melting tepmerature
70
-
24 h, 15% resiudal activity
75
melting temperature
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crosslinked immobilized enzyme is very stable to urea
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immobilized enzyme, 10% ethanol, 0.01% H2O2, or in 0.02% sodium azide, loss of only small amounts of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer containing 1 mM EDTA, pH 7.5, stable for at least 1 year
-20°C, purified enzyme from egg white, in 20 mM Tris buffer, stable for months