Information on EC 1.8.3.2 - thiol oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.8.3.2
-
RECOMMENDED NAME
GeneOntology No.
thiol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
ter bi substituted mechanism, O2 binds first
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
mechanistic scheme
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
the CXXC motif in the active site sequence of Erv2p is catalytically essential, reaction mechanism involving reactive cysteine residues C121 and C124 of the A subunit, and C176 and C178 of the B subunit
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
the N-terminal cysteine pair of the enzyme is essential for in vivo activity and interacts with the primary redox centre
Q12284
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
enzyme contains a functionally involved redox-active motif YPCCXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
reaction mechanism
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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'.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ac92
P41480
gene name
ALR
-
augmenter of liver regeneration
ALR
P55789
-
ALR
Q63042
augmenter of liver regeneration
ALRp
-
-
DTT-oxidase
-
-
-
-
egg white oxidase
-
-
ERV/ALR sulfhydryl oxidase
-
-
Erv1
P55789
-
Erv1
-
-
ERv2p
-
-
-
-
FAD-linked sulfhydryl oxidase ALR
P55789
-
FAD-sulfhydryl oxidase
Q6IUU3
-
flavin adenine dinucleotide-linked sulfhydryl oxidase
-
-
hepatic regenerative stimulator substance
Q63042
-
hepatopoietin
-
-
hepatopoietin
Q63042
-
neuroblastoma-derived sulfhydryl oxidase
-
-
oxidase, thiol
-
-
-
-
QSCN6
O00391
-
QSOX
-
-
QSOX
-
-
QSOX
O00391
-
QSOX
-
-
QSOX
Q585M6
-
QSOx1
Q8W4J3
-
QSOx1
O08841
-
QSOx1
O00391
-
QSOX2
O00391
-
Quiescin Q6
-
-
Quiescin Q6
O00391
-
quiescin Q6 sulfhydryl oxidase
-
-
quiescin Q6/sulfhydryl oxidase
-
-
quiescin sulfhydryl oxidase
O00391
-
quiescin sulfhydryl oxidase
Q585M6
-
quiescin sulhydryl oxidase
-
-
quiescin-like flavin-dependent sulfhydryl oxidase
-
-
Quiescin-sulfhydryl oxidase
-
-
Quiescin-sulfhydryl oxidase
O00391
-
Quiescin-sulfhydryl oxidase
-
-
Quiescin-sulfhydryl oxidase
Q6IUU3
-
Quiescin-sulfhydryl oxidase
-
-
quiescin/sulfhydryl oxidase
-
-
quiescin/sulphydryl oxidase
-
-
Sox1
Q2UA33
-
Sox1
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
Sox2
Q2U4P3
-
Sox2
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
SOXN
-
-
sulfhydryl oxidase
-
-
-
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
Q65163
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
O08841
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
O00391
-
sulfhydryl oxidase
Q8BND5
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
Q63042
-
sulfhydryl oxidase
Q6IUU3
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase
-
-
sulfhydryl oxidase SOx-3
-
-
-
-
sulphydryl oxidase
-
-
thiooxidase
-
-
-
-
mitochondrial FAD-linked sulfhydryl oxidase ERV1
P27882
-
additional information
Q65163
the enzyme belongs to the sulfhydryl oxidases of the Erv/ALR family
additional information
-
the enzyme belongs to the Erv1/Alr sulfhydryl oxidase family
additional information
-
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
additional information
O08841
enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 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
additional information
-
enzyme belongs to the sulfhydryl oxidase/Quiescin Q6 family
additional information
-
enzyme belongs to the sulfhydryl oxidase/Quiescin6 family
additional information
O00391
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
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
Q6IUU3
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
additional information
-
enzyme belongs to the ERV1/ALR family
additional information
-
enzyme is a member of the Quiescin-sulfhydryl oxidase QSOX family
CAS REGISTRY NUMBER
COMMENTARY
9029-39-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform Qsox1
UniProt
Manually annotated by BRENDA team
Aspergillus niger AUMC 4947
-
-
-
Manually annotated by BRENDA team
Aspergillus niger N402
-
-
-
Manually annotated by BRENDA team
Aspergillus oryzae ATCC 42149
-
UniProt
Manually annotated by BRENDA team
Aspergillus oryzae ATCC 42149
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Alrp protein
-
-
Manually annotated by BRENDA team
gene QSOX1
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
adult female and male rats
-
-
Manually annotated by BRENDA team
entry name QSCN6_RAT
SwissProt
Manually annotated by BRENDA team
gene QSOX1
SwissProt
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
2 isozymes Evr1p and Evr2p
-
-
Manually annotated by BRENDA team
several strains, overview
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
Erv1p is a FAD-dependent sulfhydryl oxidase and is an essential component of the redox regulated Mia40/Erv1 import and assembly pathway used by many of the cysteine-containing intermembrane space proteins
physiological function
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
physiological function
P55789
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
Aspergillus niger N402
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
-, Q2U4P3
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
-, Q2UA33
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
-, Q2U4P3
-
-
-
-
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
-, Q2UA33
-
-
-
-
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
-
-
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
-
-
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-, Q2U4P3
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Q585M6, -
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-, Q2UA33
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-, Q2U4P3
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Q585M6, -
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-, Q2UA33
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Aspergillus niger AUMC 4947
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
-, Q2U4P3
-
-
-
-
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
-, Q2UA33
-
-
-
-
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2U4P3
-
-
-
-
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
-
-
2 R-SH + FAD
R-S-S-R + FADH2
show the reaction diagram
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
show the reaction diagram
-
3.7% of the activity with dithiothreitol
-
-
-
2-mercaptoethanol + O2
? + H2O
show the reaction diagram
-
3.7% of the activity with dithiothreitol
-
-
?
2-nitro-5-thiobenzoic acid + O2
? + H2O
show the reaction diagram
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic 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
-
-
-
-
?
cysteamine + O2
? + H2O
show the reaction diagram
-
-
-
-
-
cysteamine + O2
? + H2O
show the reaction diagram
-
-
-
-
?
cysteine + O2
cystine + H2O2
show the reaction diagram
Q8GXX0
artificial in vitro substrate
-
-
ir
D-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
D-penicillamine + O2
? + H2O
show the reaction diagram
-
33% of the activity with dithiothreitol
-
-
?
dithioerythritol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
? + H2O
show the reaction diagram
Q6IUU3
-
production of H2O2
?
dithiothreitol + O2
? + H2O
show the reaction diagram
-
anaerobically, the ferricenium ion is a facile alternative electron acceptor
production of H2O2
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Q12284
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Q63042
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Q8GXX0
artificial in vitro substrate
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
Evr2p, not Evr1p
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
intact enzyme and 60-kDa-enzyme fragment
-
-
ir
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 + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
low concentrations of dithiothreitol stimulate the import efficiency of Erv1, whereas higher concentrations of dithiothreitol decrease it
-
-
?
dithiothreitol + O2
? + H2O2
show the reaction diagram
Q8W4J3
-
-
-
?
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
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Q6IUU3
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
best small thiol substrate
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
Evr2p, not Evr1p
-
-
?
Gly-Gly-L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
-
production of H2O2
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
0.7% of the activity with dithiothreitol
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
0.7% of the activity with dithiothreitol
-
-
?
GSH + O2 + O2
GSSG + H2O
show the reaction diagram
-
13.5% of the activity with dithiothreitol
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
show the reaction diagram
-
-
-
-
?
L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
L-Cys + O2
? + H2O
show the reaction diagram
-
-
-
-
?
L-Cys + O2
? + H2O
show the reaction diagram
-
20.3% of the activity with dithiothreitol
-
-
-
L-Cys + O2
? + H2O
show the reaction diagram
-
17% of the activity with dithiothreitol
-
-
?
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
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
-
-
-
-
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
4.6% of the activity with dithiothreitol
-
-
-
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
4.6% of the activity with dithiothreitol
-
-
?
N-acetylcysteine + O2
? + H2O
show the reaction diagram
-
12.6% of the activity with dithiothreitol
-
-
-
ovalbumin + O2
ovalbumin disulfide + H2O2
show the reaction diagram
-
-
-
-
?
pancreatic RNase + O2
pancreatic RNase disulfide + H2O2
show the reaction diagram
-
-
-
-
ir
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
show the reaction diagram
-
-
-
-
-
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
show the reaction diagram
-
i.e. PDI
-
-
ir
protein Mia40 + O2
protein Mia40 disulfide + H2O
show the reaction diagram
-
-, recombinantly expressed substrate amino acids 284-403, which is the C-terminal domain of Mia40, electron transfer between the shuttle and active site disulfides of Erv1p. Both intersubunit and intermolecular electron transfer can occur, overview
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q6ZRP7
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q12284
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q8GXX0
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q6IUU3
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
O00391
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q63042
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q8GXX0
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme plays a role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme plays a role in synaptic strengthening and in redox activities in the brain
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q6IUU3
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
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
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q12284
3 cysteine pairs are required for optimal enzyme function
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
best substrates are cysteine residues in reduced proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
disulfide bridge C15-C124 is not required for activity
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
reduced aldolase + O2
aldolase + H2O
show the reaction diagram
-
-
-
-
?
reduced insulin A chain + O2
insulin A chain + H2O
show the reaction diagram
-
-
-
-
?
reduced insulin B chain + O2
insulin B chain + H2O
show the reaction diagram
-
-
-
-
?
reduced lysozyme + O2
lysozyme + H2O
show the reaction diagram
-
-
-
-
?
reduced lysozyme + O2
lysozyme + H2O
show the reaction diagram
-
-
-
-
?
reduced lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
-
-
-
-
ir
reduced lysozyme + O2
? + H2O
show the reaction diagram
-
-
-
-
?
reduced ovalbumin + O2
ovalbumin + H2O
show the reaction diagram
-
-
-
-
?
reduced pyruvate kinase + O2
pyruvate kinase + H2O
show the reaction diagram
-
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
show the reaction diagram
-
-
-
-
?
reduced ribunuclease + O2
renatured ribonuclease + H2O
show the reaction diagram
-
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
show the reaction diagram
-
-
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
show the reaction diagram
-
-
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
show the reaction diagram
-
-
production of H2O2
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
show the reaction diagram
-
reductively denatured pancreatic ribonuclease A
-
-
?
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
show the reaction diagram
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
-
-
-
-
ir
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
Q6IUU3
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
-
low activity
-
-
?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
-
intact enzyme, but not 60-kDa-enzyme fragment
-
-
ir
RNasered + O2
? + H2O
show the reaction diagram
-
-
-
-
?
rRNaseA + O2
? + H2O2
show the reaction diagram
Q585M6, -
-
-
-
?
thioglycolate + O2
? + H2O
show the reaction diagram
-
11.1% of the activity with dithiothreitol
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
-
-
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
-
-
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
Q8GXX0
-
-
-
ir
thioredoxin + O2
thioredoxin disulfide + H2O2
show the reaction diagram
-
substrate from Escherichia coli
-
-
ir
tris(2-carboxyethyl)-phosphine + O2
? + H2O
show the reaction diagram
-
-
-
-
?
Trx Escherichia coli + O2
? + H2O
show the reaction diagram
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
-
Evr1p
-
-
?
additional information
?
-
-
enzyme does not catalyze thiol-disulfide interchange
-
-
-
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
-
additional information
?
-
-
essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic but not of mitochondrial Fe-S proteins
-
-
-
additional information
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
-
additional information
?
-
-
Erv2p functions in the generation of microsomal disulfide bonds acting in parallel with Ero1p, the essential FAD-dependent oxidase of protein disulfide isomerase
-
-
-
additional information
?
-
-
the enzyme may play an important role in the introduction of disulfide bridges in egg white proteins
-
-
-
additional information
?
-
-, O08841
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
-
additional information
?
-
-
possible role for oxidase in protein secretory pathway
-
-
-
additional information
?
-
Q6ZRP7
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
?
-
-
Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview
-
-
-
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, even of denatured cytoplasmic proteins, low molecular weight thiols, such as cysteine or glutathione, are poorer substrates
-
-
-
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
-
additional information
?
-
-
a 30 kDa enzyme fragment shows no catalytic activity of its own
-
-
-
additional information
?
-
-
low activity with reduced proteins
-
-
-
additional information
?
-
Q8GXX0
no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
-
-
-
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, but not low molecular weight thiols, such as cysteine or glutathione
-
-
-
additional information
?
-
-
redox cycling of the FAD moiety is essential for enzyme activity
-
-
-
additional information
?
-
-
enzyme regulation, overview
-
-
-
additional information
?
-
-
does not oxidize reduced thioredoxin
-
-
-
additional information
?
-
-
Erv2p is a modest catalyst of disulfide bond formation. None of the monothiols (at 10 mM), including beta-mercaptoethanol, N-acetylcysteamine, reduced glutathione and CoASH, prove detectable substrates of the yeast oxidase at pH 7.5. In contrast, dithiols are significant substrates
-
-
-
additional information
?
-
-
Erv1p contains three conserved disulfide bonds arranged in two CXXC motifs and one CX16C motif, the CX16C disulfide plays an important role in stabilizing the folding of Erv1p, both CXXC disulfides are required for Erv1 oxidase activity, but none of the disulfide is essential for FAD binding, overview
-
-
-
additional information
?
-
Q585M6, -
unfolded reduced proteins are more than 200fold more effective substrates on a per-thiol basis than glutathione, and some 10fold better than the parasite bis-glutathione analog, trypanothione. The CxxC motif in the single Trx domain is crucial for efficient catalysis of the oxidation of both reduced RNase and the model substrate dithiothreitol. The proximal disulfide CIII-CIV, which interacts with the flavin, is catalytically crucial. Turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
ovalbumin + O2
ovalbumin 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
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q6ZRP7
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q12284
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q8GXX0
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme plays a role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
enzyme plays a role in synaptic strengthening and in redox activities in the brain
-
-
ir
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
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
show the reaction diagram
-
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
Q6IUU3
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
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
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
oxidation of protein or peptide sulfhydryl groups to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
show the reaction diagram
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
show the reaction diagram
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
-
additional information
?
-
-
essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic but not of mitochondrial Fe-S proteins
-
-
-
additional information
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
-
additional information
?
-
-
Erv2p functions in the generation of microsomal disulfide bonds acting in parallel with Ero1p, the essential FAD-dependent oxidase of protein disulfide isomerase
-
-
-
additional information
?
-
-
the enzyme may play an important role in the introduction of disulfide bridges in egg white proteins
-
-
-
additional information
?
-
-, O08841
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
-
additional information
?
-
-
possible role for oxidase in protein secretory pathway
-
-
-
additional information
?
-
Q6ZRP7
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
?
-
-
Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview
-
-
-
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, even of denatured cytoplasmic proteins, low molecular weight thiols, such as cysteine or glutathione, are poorer substrates
-
-
-
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
-
additional information
?
-
-
enzyme regulation, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
enzyme from seminal vesicles
FAD
-
enzyme is linked to FAD
FAD
-
contains FAD
FAD
-
firmly attached but nut covalently linked to the protein; one molecule of FAD per subunit
FAD
-
small FAD-binding domain
FAD
-
small FAD-binding domain, 1 molecule per subunit
FAD
O00391
small FAD-binding domain
FAD
Q6IUU3
small FAD-binding domain
FAD
-
small FAD-binding domain
FAD
-
flavoprotein, 1 FAD molecule per enzyme subunit with 1 phosphorus atom per FAD as cofactor of the cofactor
FAD
-
required for activity, binding domain is located on the 60-kDa-enzyme fragment, electron-transfer mechanism in the native enzyme and the 60 kDA enzyme fragment
FAD
Q12284
dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold
FAD
-
noncovalently bound, binding site sequence and structure
FAD
-
bound to the enzyme
FAD
-
dependent on
FAD
-
bound to the enzyme
FAD
-
dependent on
FAD
-
dependent on
FAD
-
dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity
FAD
-
dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin
FAD
-
dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview
FAD
-
dependent on. The three disulfides of the enzyme are not essential for FAD binding
FAD
-, Q65163
flavoenzyme
FAD
Q585M6, -
turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
flavin
Q8W4J3
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
additional information
-
redox-active disulfide involved in catalysis
-
additional information
-
enzyme contains a thioredoxin domain
-
additional information
-
enzyme contains a thioredoxin domain, 1 redox-active disulfide per subunit
-
additional information
O00391
enzyme contains a thioredoxin domain
-
additional information
Q6IUU3
enzyme contains a thioredoxin domain
-
additional information
-
enzyme contains a thioredoxin and an ERV1 domain
-
additional information
-
enzyme contains a thioredoxin and a ERV1 domain
-
additional information
-
enzyme contains a redox-active cysteine-bridge
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
copper
-
native activity is increased 2fold
copper
-
contains 1 mol copper per subunit, in a binuclear complex
copper
-
involved in catalysis
copper
-
enzyme from kindney and small intestine
Iron
-
contains enzyme-bound iron
Iron
-
iron appears to be required for enzymatic activity
Iron
-
-
Iron
-
enzyme contains a FeS center
Phosphorus
-
6.60 atoms per subunit/FAD, cofactor of the FAD
Zn2+
-, Q2U4P3
1 mM, 95% loss of activity
MgSO4
-
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
additional information
-
no metalloenzyme
additional information
-
metalloenzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bathocuproine disulfonate
-
0.5 mM, 89% inhibition
Bathocuproine disulfonate
-
-
Cu2+
-
modeling of metal binding
diazabicyclooctane
-
-
diethyldithiocarbamate
-
-
dithiothreitol
-
at high concentrations
EDTA
-
5 mM, 93% inhibition
EDTA
-
milk enzyme
EDTA
-
inhibition of enzyme from kidney and small intestine, no inhibition of enzyme from skin and seminal vesivles
GSSG
-
substrate inhibition above 0.8 mM
Guanine
-
-
H2O2
-
0.1 mM, 89% inhibition
iodoacetamide
-
-
iodoacetamide
-
moderate
iodoacetamide
-
-
iodoacetic acid
-
-
iodoacetic acid
-
moderate
KI
-, Q2UA33
1 mM, 65% residual activity
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
-
-
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
-
-
MgSO4
-
1 mM, 55% residual activity
Na2SO4
-, Q2U4P3
1 mM, 66% residual activity
Na2SO4
-, Q2UA33
1 mM, 61% residual activity
NEM
-
1 mM, 86% inhibition
o-Dianisidine
-
-
o-phenylenediamine
-
-
ribonuclease
-
substrate inhibition above 0.04 mM
-
RNAi
-
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
-
sodium dodecylsulfate
-, Q2U4P3
1 mM, 57% residual activity
sodium dodecylsulfate
-, Q2UA33
1 mM, 58% residual activity
Urea
-, Q2UA33
1 mM, 80% residual activity
Zn2+
-
weak binding to the four-electron-reduced enzyme, rapid inhibition, modeling of metal binding
Zn2+
-
upon coordination with Zn2+, full reduction of Erv2p requires 6 electrons. Strongly inhibits Erv2p when assayed using tris(2-carboxyethyl)phosphine as the reducing substrate of the oxidase. Restoration of 1 mM EDTA effects rapid recovery of 80% of the original activity
ZnSO4
-, Q2U4P3
1 mM, 95% loss of activity
ZnSO4
-, Q2UA33
1 mM, complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
H2O2
-
high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein
L-Cys
-
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
staurosporine aglycone
-
-
Triton X-100
-
0-0.1% concentration, at most 30% activation
MgSO4
-
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
additional information
-
enzyme expression in endometrial glandular epithelium is inducible by estradiol in presence of cycloheximide, and by serum deprivation
-
additional information
O00391
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.9
-
2-mercaptoethanol
-, Q2U4P3
pH 7.5, 20C
9.73
-
2-mercaptoethanol
-, Q2UA33
pH 7.5, 20C
54
-
2-mercaptoethanol
-
-
100
-
2-nitro-5-thiobenzoic acid
-
-
1.25
-
cysteamine
-
-
1.6
-
cysteamine
-
-
30
-
cysteamine
-
-
1.33
-
D-Cys
-
-
1.55
-
D-Cys
-, Q2UA33
pH 7.5, 20C
13.1
-
D-Cys
-, Q2U4P3
pH 7.5, 20C
0.086
-
dithiothreitol
Q585M6, -
pH 7.5, 37C
0.15
-
dithiothreitol
-
-
0.51
-
dithiothreitol
-
-
1.3
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C15A
1.7
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C15A/C74A/C85A/C124A
1.8
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C124A
2
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutants C74A/C85A and C15A/C124A
2.1
-
dithiothreitol
-
pH 7.5, 25C, recombinant wild-type enzyme
2.41
-
dithiothreitol
-, Q2UA33
pH 7.5, 20C
4.9
-
dithiothreitol
-, Q2U4P3
pH 7.5, 20C
11.3
-
dithiothreitol
-
-
0.14
-
DTT
-
native enzyme, pH 7.5
0.2
-
DTT
-
7.5, 25C
0.7
-
DTT
Q6IUU3
-
12.5
-
DTT
-
60 kDa enzyme fragment, pH 7.5
0.02
-
glutathione
-
-
2.78
-
glutathione
-, Q2UA33
pH 7.5, 20C
3.7
-
glutathione
-, Q2U4P3
pH 7.5, 20C
4.4
-
glutathione
Q6IUU3
-
6.7
-
glutathione
-
pH 5.5, 25C
6.31
-
Gly-Gly-L-Cys
-
-
0.09
-
GSH
-
-
0.3
-
GSH
-
-
0.34
-
GSH
-
-
0.73
-
GSH
-
-
3.16
-
GSH
-
-
8.16
-
GSH
-
-
0.42
-
L-Cys
-
-
0.8
-
L-Cys
-
-
0.805
-
L-Cys
-
-
0.9
-
L-Cys
-, Q2U4P3
pH 7.5, 20C
0.966
-
L-Cys
-
-
6.11
-
L-Cys
-, Q2UA33
pH 7.5, 20C
1.72
-
N-acetyl-EAQCGTS
-
expressed per thiol basis
1.13
-
N-acetyl-L-Cys
-
-
2.35
-
N-acetyl-L-Cys
-
-
3.85
-
N-acetyl-L-Cys
-
-
3.3
-
N-acetylcysteine
-
-
0.0001
-
O2
-
with 0.3 mM reduced thioredoxin as the substrate of the reductive half-reaction and an initial oxygen concentration of around 0.3 mM such that the reduced thioredoxin would be depleted by 10% during the course of the reaction
0.0004
-
O2
-
in the presence of 12.5 mM dithiothreitol
0.0046
-
O2
-
-
0.018
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.027
-
O2
-
25C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
0.057
-
O2
-
25C, recombinant wild-type enzyme, in presence of 10 mM DTT
0.062
-
O2
-
25C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.087
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
0.77
-
O2
-
-
0.16
-
reduced aldolase
-
expressed per thiol basis
-
0.215
-
reduced insulin A chain
-
expressed per thiol basis
-
0.3
-
reduced insulin B chain
-
expressed per thiol basis
-
0.11
-
reduced lysozyme
-
expressed per thiol basis
-
0.33
-
reduced ovalbumin
-
expressed per thiol basis
-
1.25
-
reduced pyruvate kinase
-
expressed per thiol basis
-
0.23
-
reduced riboflavin-binding protein
-
expressed per thiol basis
-
0.0174
-
Reduced ribonuclease
-
corresponds to a sulfhydryl concentration of 0.14 mM
-
0.115
-
Reduced ribonuclease
-
expressed per thiol basis
-
0.014
-
RNAse A
-
pH 8.1, 25C
-
0.36
-
rRNaseA
Q585M6, -
pH 7.5, 37C
-
10.9
-
L-Cys
-
-
additional information
-
additional information
-
the activity with small thiols is dominated by the Km value
-
additional information
-
additional information
Q6IUU3
the activity with small thiols is dominated by the Km value
-
additional information
-
additional information
-
redox potential of wild-type and mutant enzymes
-
additional information
-
additional information
-
oxygen consumption kinetic parameters for the WT and Erv1p mutants, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20.3
-
2-mercaptoethanol
-
-
50
100
2-mercaptoethanol
-, Q2UA33
pH 7.5, 20C
55400
-
2-mercaptoethanol
-, Q2U4P3
pH 7.5, 20C
5950
-
D-Cys
-, Q2UA33
pH 7.5, 20C
78600
-
D-Cys
-, Q2U4P3
pH 7.5, 20C
0.83
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C74A/C85A
0.87
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C15A
0.9
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C124A
0.95
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C15A/C124A
1.1
-
dithiothreitol
-
pH 7.5, 25C, recombinant wild-type enzyme
1.25
-
dithiothreitol
-
pH 7.5, 25C, recombinant mutant C15A/C74A/C85A/C124A
3.43
-
dithiothreitol
-
-
17.2
-
dithiothreitol
-
-
45
-
dithiothreitol
Q585M6, -
pH 7.5, 37C
309000
-
dithiothreitol
-, Q2UA33
pH 7.5, 20C
337800
-
dithiothreitol
-, Q2U4P3
pH 7.5, 20C
3.5
-
DTT
-
3C
20
-
DTT
-
25C
1013
-
DTT
-
native enzyme, pH 7.5
66.67
-
glutathione
-
-
97500
-
glutathione
-, Q2U4P3
pH 7.5, 20C
3600000
-
glutathione
-, Q2UA33
pH 7.5, 20C
23.1
-
GSH
-
-
21.3
-
L-Cys
-
-
6800
-
L-Cys
-, Q2U4P3
pH 7.5, 20C
0.7
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.8
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
1.1
-
O2
-
25C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
1.3
-
O2
-
25C, recombinant wild-type enzyme, in presence of 10 mM DTT
1.5
-
O2
-
25C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.002
-
RNAse A
-
thiol per second
-
22
-
rRNaseA
Q585M6, -
pH 7.5, 37C
-
52300
-
L-Cys
-, Q2UA33
pH 7.5, 20C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7000
-
2-mercaptoethanol
-, Q2U4P3
pH 7.5, 20C
2666
515000
-
2-mercaptoethanol
-, Q2UA33
pH 7.5, 20C
2666
3840
-
D-Cys
-, Q2UA33
pH 7.5, 20C
9121
5980
-
D-Cys
-, Q2U4P3
pH 7.5, 20C
9121
230
-
dithiothreitol
Q585M6, -
pH 7.5, 37C
9992
69230
-
dithiothreitol
-, Q2U4P3
pH 7.5, 20C
9992
128000
-
dithiothreitol
-, Q2UA33
pH 7.5, 20C
9992
2.3
-
glutathione
Q585M6, -
pH 7.5, 37C
10966
26500
-
glutathione
-, Q2U4P3
pH 7.5, 20C
10966
1290000
-
glutathione
-, Q2UA33
pH 7.5, 20C
10966
7600
-
L-Cys
-, Q2U4P3
pH 7.5, 20C
12146
8560
-
L-Cys
-, Q2UA33
pH 7.5, 20C
12146
0.0023
-
O2
-
25C, recombinant wild-type enzyme, in presence of 10 mM DTT
14738
0.0024
-
O2
-
25C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
14738
0.0039
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
14738
0.0041
-
O2
-
25C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
14738
0.0093
-
O2
-
25C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
14738
180
-
rRNaseA
Q585M6, -
pH 7.5, 37C
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0026
-
-
in 6-day newborn serum
10
-
-
-
24
-
-
-
103.8
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
a continuous fluorescence assay for sulfhydryl oxidase
additional information
-
-
several assay methods are used dependent on the substrate, overview
additional information
-
-
-
additional information
-
-
no activity in 60-day calf serum
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
7
-
-
7
-
-
assay at
7
-
Q585M6, -
-
7.5
-
-
-
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
8
8.2
-
oxidation of 5,5'-dithiobis(2-nitrobenzoic acid) and reactivation of ribonuclease
8
-
-
assay at
8
-
-, Q2U4P3
-
8
-
-, Q2UA33
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
11
-
pH 5.0: about 40% of maximal activity, pH 11: about 70% of maximal activity
5
8.5
-, Q2U4P3
more than 80% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9
13
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
35
-
-
-
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
detailed tissue distribution analysis in brain, overview
Manually annotated by BRENDA team
-
highest mRNA contents in cerebellum and diencephalons
Manually annotated by BRENDA team
-
highest enzyme expression in reticular structures, such as the basal forebrain, reticular thalamic nucleus, and reticular nuclei of the brainstem
Manually annotated by BRENDA team
-
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
-
glandular epithelial cells
Manually annotated by BRENDA team
-
specific expression in glandular and luminal epithelial cells
Manually annotated by BRENDA team
Q6IUU3
high content
Manually annotated by BRENDA team
-
endometrial glandular
Manually annotated by BRENDA team
-
secretory, endometrial
Manually annotated by BRENDA team
O00391
high expression level of QSOX1
Manually annotated by BRENDA team
-
embroynic fibroblast
Manually annotated by BRENDA team
-
throughout the rostrocaudal extent of the brain
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
during late embryogenesis
Manually annotated by BRENDA team
-
high expression in neurons producing disulfide-bounded neuropeptides
Manually annotated by BRENDA team
-
during late embryogenesis
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
secretion of enzyme
Manually annotated by BRENDA team
Q6ZRP7
several cell lines
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
throughout the rostrocaudal extent of the brain
Manually annotated by BRENDA team
-
secretory tissue
Manually annotated by BRENDA team
-
fluid, high activity
Manually annotated by BRENDA team
-
fetal and newborn serum
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
small amounts
Manually annotated by BRENDA team
-
epithelial cells
Manually annotated by BRENDA team
additional information
-
wide tissue distribution
Manually annotated by BRENDA team
additional information
O00391
tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads
Manually annotated by BRENDA team
additional information
Q6IUU3
tissue expression and distribution
Manually annotated by BRENDA team
additional information
Q6ZRP7
tissue distribution of enzyme expression
Manually annotated by BRENDA team
additional information
-
detailed analysis of cellular and subcellular enzyme localization, overview
Manually annotated by BRENDA team
additional information
-
in-situ detection of enzyme expression in pituitary gland
Manually annotated by BRENDA team
additional information
-
enzyme is expressed in a large number of different cell types and tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform EroA is retained in the ER lumen by a C-terminal retention motif
Manually annotated by BRENDA team
Aspergillus niger N402
-
isoform EroA is retained in the ER lumen by a C-terminal retention motif
-
Manually annotated by BRENDA team
-
secretion by fungal mycelium
-
Manually annotated by BRENDA team
O00391
seminal vesicles
-
Manually annotated by BRENDA team
-
secretion of enzyme
-
Manually annotated by BRENDA team
-
enzyme is secreted
-
Manually annotated by BRENDA team
-
both intra- and extracellular
-
Manually annotated by BRENDA team
Aspergillus niger AUMC 4947
-
both intra- and extracellular
-
-
Manually annotated by BRENDA team
-
QSOX1a-V5 is a glycosylated, transmembrane protein localized to the Golgi apparatus
Manually annotated by BRENDA team
-
both intra- and extracellular
Manually annotated by BRENDA team
Aspergillus niger AUMC 4947
-
both intra- and extracellular
-
Manually annotated by BRENDA team
Q585M6, -
type I membrane protein
Manually annotated by BRENDA team
-
Erv1 requires the redox-regulated receptor Mia40 for its import into mitochondria. Interacts via disulfide bonds with Mia40. It does not need two CX2C motifs for import into mitochondria
Manually annotated by BRENDA team
-
associated to basal-lateral region of the plasma membrane
Manually annotated by BRENDA team
Q6ZRP7
outer, associated
Manually annotated by BRENDA team
P55789
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
Manually annotated by BRENDA team
additional information
Q6ZRP7
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
African swine fever virus (strain Badajoz 1971 Vero-adapted)
Autographa californica nuclear polyhedrosis virus
Autographa californica nuclear polyhedrosis virus
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14000
-
-
SDS-PAGE
21000
-
-
SDS-PAGE, under reducing conditions
23000
-
-
SDS-PAGE, under reducing conditions
28000
-
-
SDS-PAGE
28760
-
-
SDS-PAGE
44000
-
-
SDS-PAGE, under non-reducing conditions
47000
-
-
gel filtration
48660
-
-
method not mentioned
54000
-
Q585M6, -
PAGE
54300
-
Q585M6, -
analytical ultracentrifugation
64000
-
-
SDS-PAGE
66000
-
-
gel filtration
66000
-
-
SDS-PAGE
66000
-
-
SDS-PAGE
78000
-
-, Q2U4P3
gel filtration
85000
-
Q6IUU3
SDS-PAGE
85360
-
Q6IUU3
MALDI-TOF mass spectrometry
120000
-
-
gel filtration
202000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 90000, may exist in an aggregated molecular form, SDS-PAGE
?
-
x * 89000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
x * 100000, native enzyme, SDS-PAGE
?
Q6ZRP7
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
?
-
x * 22000, full length enzyme, SDS-PAGE
?
-
x * 70000, SDS-PAGE
?
Q8BND5
x * 65000, recombinant enzyme, SDS-PAGE
?
-
x * 68000, recombinant His-tagged enzyme, SDS-PAGE
?
-, Q2UA33
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
?
Q8W4J3
x * 47000, SDS-PAGE
?
Aspergillus oryzae ATCC 42149
-
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
-
dimer
-
2 * 70000, also aggregates to larger multimers, SDS-PAGE
dimer
-
2 * 93000, SDS-PAGE
dimer
-
2 * 53000
dimer
-
2 * 90000, about
dimer
-
monomers are linked via a disulfide bridge C15-C124, which is not critical for dimer formation, structure modeling using the enzymes crystal structure
dimer
Q12284
Cys30 and Cys33 are involved in dimer formation
dimer
-
-
dimer
-
2 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
dimer
-
crystal structure, stabilization by extensive noncovalent interactions and a network of hydrogen bonds, structure fo the dimer interface
dimer
-
1 * 23000, 1* 21000, SDS-PAGE, under non-reducing conditions
dimer
-
2 * 14378, laser desorption mass spectrometry
dimer
-
2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
-, Q65163
the viral enzyme uses an alternate dimerization mode compared to other viral sulfhydryl oxidases, overview. The dimer interface involves helices alpha2 and alpha3
dimer
-
1 * 50000 plus 1 * 55000, SDS-PAGE
dimer
-, Q2U4P3
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
dimer
P41480
2 * 33000, calculated and crystallization data
dimer
Aspergillus niger AUMC 4947
-
1 * 50000 plus 1 * 55000, SDS-PAGE
-
dimer
Aspergillus oryzae ATCC 42149
-
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE
monomer
Q6IUU3
1 * 65000, about
monomer
-
1 * 21000, SDS-PAGE, under reducing conditions; 1 * 23000, SDS-PAGE, under reducing conditions
monomer
-
1 * 14000, SDS-PAGE, in the infected cell
monomer
Q585M6, -
1 * 54000, SDS-PAGE
additional information
-
structure
additional information
-
structure, active site structure containinbg a CXXC motif
additional information
-
2 enzyme fragments by partial proteolysis: a 30 kDa nonglycosylated monomeric fragment containing a thioredoxin domain with a CXXC motif, and a 60 kDa glycosylated dimeric fragment with bound FAD and catalytic activity, the latter different from intact enzyme activity
additional information
Q6ZRP7
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
-
structural analysis, modeling of the conserved central domain, the plant enzyme contains a unique C-terminally located CXXXXC motif and no N-terminally localized cysteine pair, which is typical for enzymes of the Erv1/Alr sulfhydryl oxidase family
additional information
Q8BND5
structural analysis of the recombinant enzyme
additional information
-
enzyme contains an N-terminal thioredoxin domain, an intervening domain, and a C-terminal ALR/ERV domain, redox-active motif CXXC
additional information
-
Erv1p contains three conserved disulfide bonds arranged in two CXXC motifs and one CX16C motif in the highly conserved central catalytic core. The CX16C disulfide plays an important role in stabilizing the folding of Erv1p, both CXXC disulfides are required for Erv1 oxidase activity, but none of the disulfide is essential for FAD binding, overview
additional information
-, Q65163
structure determination, comparison, and modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
flavoprotein
-, Q65163
-
flavoprotein
-
-
glycoprotein
-, Q2UA33
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
proteolytic modification
-, Q2U4P3
sequence contains a signal peptide of 23 amino acids
glycoprotein
Aspergillus oryzae ATCC 42149
-
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
-
proteolytic modification
Aspergillus oryzae ATCC 42149
-
sequence contains a signal peptide of 23 amino acids
-
glycoprotein
-
contains 11% carbohydrate
glycoprotein
-
-
glycoprotein
-
highly glycosylated
glycoprotein
-
heavy glycosylation of the 60-kDa-enzyme fragment
glycoprotein
Q8BND5
2 putative N-glycosylation sites at residues 133-135 and 246-248
proteolytic modification
Q8BND5
cleavage of 32 amino acids at the proteolytic site
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
glycoprotein
-
-
flavoprotein
-
-
glycoprotein
Q6ZRP7
probably
additional information
Q6ZRP7
enzyme contains a signal sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q65163
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
P41480
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
-
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
-
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
P27882
Erv2p, X-ray diffraction structure determination and analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
-, Q2UA33
24 h, more than 80% of initial activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-
enzyme retains more than 80% of the initial activity with glutathione after 24 h incubation at 30-60C
40
-
-, Q2UA33
24 h, more than 70% of initial activity
50
-
-, Q2U4P3
24 h, 42% residual activity
50
-
-, Q2UA33
1 h, 40% of initial activity
57
-
-, Q2UA33
melting tepmerature
60
-
-
15 min, 85% loss of activity. 30 min, complete loss of activity
60
-
-, Q2U4P3
1 h, 68% residual activity
70
-
-
24 h, 15% resiudal activity
75
-
-, Q2U4P3
melting temperature
additional information
-
-
dithiothreitol, 1 mM, increases the stability to heating
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crosslinked immobilized enzyme is very stable to urea
-
immobilized enzyme, 10% ethanol, 0.01% H2O2, or in 0.02% sodium azide, loss of only small amounts of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, purified enzyme from egg white, in 20 mM Tris buffer, stable for months
-
-20C, stable for months
-
4C, stable for at least 2 weeks
-
-20C, Tris buffer, pH 7.5, 1 mM EDTA, more than 1 year
-
-20C, 50 mM potassium phosphate buffer containing 1 mM EDTA, pH 7.5, stable for at least 1 year
Q585M6, -
4C, 50 mM potassium phosphate buffer containing 1 mM EDTA, pH 7.5, stable for at least 6 months
Q585M6, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glutathione-Sepharose 4B column chromatography
-
pB119L is located in the insoluble fraction, it can be solubilized by addition of arginine, and a truncated version lacking 16 residues at the carboxy terminus is a soluble protein
-, Q65163
recombinant His-tagged full length enzyme and C-terminal fragment from Escherichia coli strain BL21 to homogeneity by nickel affinity chromatography
-
recombinant protein
-, Q2UA33
transient covalent affinity chromatography with cysteinyl-CPG-glass
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel chelate chromatography
-
from egg white form a riboflavin-binding, protein-deficient strain, several steps
-
from egg white, preparation of apoprotein
-
intact enzyme and proteolytically cleaved enzyme in 30 kDa and 60 kDa fragments
-
recombinant His-tagged wild-type and mutant liver enzymes from Escherichia coli strain BL21(DE3)
-
recombinant enzyme from HEK and Pt-K2 cells
Q8BND5
recombinant enzyme from Escherichia coli by heat treatment, ethanol precipitation, ion exchange chromatography, and gel filtration
-
gel filtration
-
glutathione-Sepharose column
-
recobinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain XL-1
-
into the pcDNA3.1+ plasmid vector
-
expression in Escherichia coli
Q8W4J3
gene AtErv1, DNA and amino acid sequence analysis, subcloning in Escherichia coli strain DH5alpha, expression of full length enzyme and 15 kDa C-terminal fragment as His-tagged proteins in Escherichia coli strain BL21, transient expression of the enzyme fused to GFP in protoplasts of Arabidopsis thaliana and of Physcomitrella patens with localization in the mitochondria, no complementation of the enzyme-defective yeast mutant erv-ts and yeast deletion mutant DELTAerv1
-
expression in Trichoderma reesei
-
DNA and amino acid sequence determination and analysis, gene structure
-
gene cpQSOx1, primary gene sequence, DNA and amino acid sequence analysis, stable expression of the wild-type enzyme in MCF-7 cells with intra- and extracellular localization of the recombinant enzyme, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
overexpression in MCF-7 cell lines
-
DNA and amino acid sequence determination and analysis, gene structure
-
CHO-tPA cell-line stably expressing QSOX1-V5 with a C-terminal KDEL sequence
-
expression in Escherichia coli
-
expression of His6-tagged Alrp in Escherichia coli, expression of GFP-fusion enzyme in cell culture
-
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
Q6ZRP7
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
O00391
overexpression of wild-type and mutant liver enzymes in Escherichia coli strain BL21(DE3) with a longer or shorter linker His-tag, overview
-
DNA and amino acid sequence determination and analysis expression in human embryonic kidney HEK cells and in rat kangaroo kidney epithelium Pt-K2 cells
Q8BND5
DNA and amino acid sequence determination and analysis, gene structure
Q6IUU3
expression in Chineses hamster ovary epithelium cells
-
expression of wild-type and mutant enzymes in Escherichia coli strain BC21
-
expressed in Escherichia coli strain B(DE3)pLysS
-
expression in Escherichia coli
-
expression in Escherichia coli strains DH5alpha and BL21(DE3) of wild-type enzyme and a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, expression of full-length point mutants
Q12284
expression of His6-tagged enzyme in Escherichia coli
-
genes ERV1 and ERV2, DNA and amino acid sequence determination and analysis, gene structure, phylogenetic analysis
-
truncated version of Erv2p, without the N-terminal 34 residues, cloned into a pET24(a+) plasmid carrying kanamycin resistance. Amplified in DH5alpha Escherichia coli strain. Expressed from the Escherichia coli strain BL21(DE3) or BL21(DE3 star)
-
DNA and amino acid sequence determination and analysis, gene structure
-
expression in Escherichia coli
Q585M6, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isoform ErvA is slightly downregulated in response to dithiothreitol stress yet up-regulated in response to expression of a heterologous protein
-
isoform EroA is transcriptionally up-regulated in response to endoplasmic reticulum stress
-
isoform ErvA is slightly downregulated in response to dithiothreitol stress yet up-regulated in response to expression of a heterologous protein
Aspergillus niger N402
-
-
isoform EroA is transcriptionally up-regulated in response to endoplasmic reticulum stress
Aspergillus niger N402
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
yes
-, Q65163
a truncated pB119L version lacking 16 residues at the carboxy terminus, i.e. pB119L-DELTAC, is a soluble protein
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
R194H
P55789
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
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
C130S
Q12284
site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain
C130S/C133S
-
site-directed mutagenesis, the active site mutant shows no or very little activity, and the mutant shows a shifted protein-bound FAD spectrum compared to the wild-type enzyme Erv1p, the active site disulfide is located proximal to the isoalloxazine ring of FADa nd the mutation changes bound-FAD absorption slightly, the mutant is active in presence of DTT, but not with tris(2-carboxyethyl)phosphine
C133S
Q12284
site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain
C133S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C159S
Q12284
site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C159S/C176S
-
site-directed mutagenesis, the mutant shows the same protein-bound FAD spectrum as the wild-type enzyme Erv1p
C176S
Q12284
site-directed mutagenesis, about 60% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C30S
Q12284
site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C30S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
-
imported into mitochondria with similar efficiencies as wild-type Erv1
C30S/C33S
-
site-directed mutagenesis, the mutant shows the same protein-bound FAD spectrum as the wild-type enzyme Erv1p
C69S
Q585M6, -
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
C72A/C75A
Q8W4J3
activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol
additional information
-
construction of a mutant missing the active site disulfide, the mutant also exhibits a fast increase in absorption at 340 nm upon reaction with CO2-, the flavin is reduced directly by the CO2- radicals, and as for WT AtErv1 more disulfides than FAD are reduced, overview. A mutant missing the shuttle disulfide shows fast formation of RSS*R radicals at 340 nm, no intermediate phase of radical disappearance, and radical decay in a much slower pseudo-first order process compared to the structural mutant and the wild-type enzyme, The direct reduction of FAD to the semiquinone is 2fold slower than the disulfide radical formation, overview
additional information
Q8W4J3
recombinant enzyme does not apparently transfer electrons from its Trx domain to its Erv domain to accomplish rapid oxidation of highly reducing model dithiol substrates, and the measured sulfhydryl oxidase activity reflects the activity of the Erv domain alone, limited by a high KM for dithiothreitol and likely other thiol substrates
C74A/C85A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
additional information
Q6ZRP7
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
C33S
Q12284
site-directed mutagenesis, about 50% reduced activity in vitro compared to the wild-type enzyme, no complementation of an enzyme-defect mutant strain
additional information
Q12284
construction of a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, the mutant shows in vitro activity similar to the wild-type enzyme, dimerization behaviour of the mutant enzymes, overview
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, enzyme-defective Erv1p mutant shows highly altered mitochondrial membrane morphology with loss of cristae, overview
C72S
Q585M6, -
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
additional information
Q585M6, -
replacement of either cysteine of the proximal disulfide, i.e. CIII or CIV with serine essentially abolishes activity both towards dithiothreitol and rRNase. Mutations of the terminal CxxC disulfide do not show significant loss of activity towards dithiothreitol or rRNase, the visible spectra of both CVS and CVIS mutants are comparable to that of the wild-type protein
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid)
nutrition
-
flavor modification of ultra-high temperature milk
nutrition
-
elimination of cooked flavour in ultra-high temperature commercially sterile milk, may have other applications for flavour modification
medicine
-
protective role of QSOX1 against apoptosis. QSOX1 short transcript overexpression slows down proliferation and protects cells from oxidative stress-induced cell death
analysis
-
development of a fast and reliable qualitative plate test for screening secreted fungal sulfhydryl oxidases. Screening is based on the Ellman's reagent, i.e. 5,5'-dithiobis(2-nitrobenzoic acid). Enzymes could be identified in Aspergillus tubingensis, Chaetomium globusum, Melanocarpus albomyces, Penicillium aurantiogriseum, Penicillium funiculosum, Coniophora puteana and Trametes hirsuta
additional information
-
functions exclusively in the reducing environment of the cytosol and functions in partnership with auxiliary proteins
medicine
P55789
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
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
medicine
-
protective role of QSOX1 against apoptosis
additional information
-
Erv1 represents a substrate of the Mia40-dependent translocation pathway
additional information
-
functions exclusively in the reducing environment of the cytosol and functions in partnership with auxiliary proteins