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2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
reaction mechanism
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
ter bi substituted mechanism, O2 binds first
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif YPCCXXC
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
mechanistic scheme
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
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
the N-terminal cysteine pair of the enzyme is essential for in vivo activity and interacts with the primary redox centre
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
catalytic mechanism model using DTT and O2, overview. Stabilization of mixed disulfide intermediates in enzyme sfALR
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
electron transfer pathway through QSOX domains, overview. Two electrons are accepted from the substrate by the CXXC motif of the QSOX Trx1 domain, within the oxidoreductase module of QSOX. From the Trx1 domain, the electrons are transferred to the sulfhydryl oxidase module of the QSOX enzyme, first to the CXXC motif of the Erv domain, then to the FAD cofactor. Ultimately, the two electrons are transferred to molecular oxygen, the terminal electron acceptor
-
-
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
-
-
-
-
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2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
2 D-Cys + O2
D-cystine + H2O2
2 D-cysteine + O2
D-cystine + H2O2
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
2 glutathione + O2
glutathione disulfide + H2O2
2 L-Cys + O2
L-cystine + H2O2
2 R'C(R)SH + O2
R'C(R)S-S(R)CR' + H2O2
-
the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide
-
-
?
2 R-SH + FAD
R-S-S-R + FADH2
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
2-nitro-5-thiobenzoic acid + O2
? + H2O
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
bis-(2-mercaptoethyl)sulfone + O2
? + H2O
-
-
-
-
?
cysteine + O2
cystine + H2O2
artificial in vitro substrate
-
-
ir
D-Cys + O2
? + H2O
-
-
-
-
?
D-penicillamine + O2
? + H2O
-
33% of the activity with dithiothreitol
-
-
?
dithioerythritol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
dithiothreitol + O2
? + H2O2
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
dithiothreitol + reduced cytochrome c
dithiothreitol disulfide + oxidized cytochrome c
-
cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
-
-
?
gamma-glutamylcysteine + O2
?
glutathione + O2
glutathione disulfide + H2O2
Gly-Gly-L-Cys + O2
? + H2O
-
-
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
N-acetyl-EAQCGTS + O2
? + H2O
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
ovalbumin + O2
ovalbumin disulfide + H2O2
-
-
-
-
?
pancreatic RNase + O2
pancreatic RNase disulfide + H2O2
-
-
-
-
ir
protein A1aB1b + O2
protein A1aB1b disulfide + H2O2
-
precursor of the soybean seed storage protein glycinin, recombinantly expressed as His-tagged protein in Escherichia coli strain BL21(DE3). Recombinant GmQSOX1 catalyses disulfide-bond formation but is unable to refold the reduced and denatured precursor A1aB1b into a native form
-
-
?
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
protein Mia40 + O2
protein Mia40 disulfide + H2O
protein SfP53 + O2
protein SfP53 disulfide + H2O2
-
-
-
?
reduced aldolase + O2
aldolase + H2O
-
-
-
-
?
reduced insulin A chain + O2
insulin A chain + H2O
-
-
-
-
?
reduced insulin B chain + O2
insulin B chain + H2O
-
-
-
-
?
reduced lysozyme + O2
? + H2O
-
-
-
-
?
reduced lysozyme + O2
lysozyme disulfide + H2O2
reduced ovalbumin + O2
ovalbumin + H2O
-
-
-
-
?
reduced pyruvate kinase + O2
pyruvate kinase + H2O
-
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
-
-
-
-
?
reduced ribonuclease + O2
ribonuclease + H2O
reduced ribunuclease + O2
renatured ribonuclease + H2O
-
-
-
?
reduced thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
r
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
RNasered + O2
? + H2O
-
-
-
-
?
rRNaseA + O2
? + H2O2
-
-
-
?
thioglycolate + O2
? + H2O
-
11.1% of the activity with dithiothreitol
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
tris(2-carboxyethyl)-phosphine + O2
? + H2O
-
-
-
-
?
Trx Escherichia coli + O2
? + H2O
-
-
-
-
?
additional information
?
-
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
-
-
-
?
2 D-cysteine + O2
D-cystine + H2O2
-
-
-
-
?
2 D-cysteine + O2
D-cystine + H2O2
-
-
-
-
?
2 D-cysteine + O2
D-cystine + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
highest sulfhydryl oxidation activity using dithiothreitol as a substrate
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
the enzyme prefers glutathione as a substrate over cysteine and dithiothreitol
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
-
-
-
?
2-mercaptoethanol + O2
? + H2O
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
-
-
-
-
?
2-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
-
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + O2
? + H2O
-
-
-
-
?
cysteamine + O2
? + H2O
-
-
-
-
?
cysteamine + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
anaerobically, the ferricenium ion is a facile alternative electron acceptor
production of H2O2
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
production of H2O2
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
? + H2O
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
artificial in vitro substrate
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
r
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
intact enzyme and 60-kDa-enzyme fragment
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
low activity
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
the enzyme forms large amounts of neutral semiquinone, which arises between flavin centers within the dimer, during aerobic turnover with DTT
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
r
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
Evr2p, not Evr1p
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
low concentrations of dithiothreitol stimulate the import efficiency of Erv1, whereas higher concentrations of dithiothreitol decrease it
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
-
r
gamma-glutamylcysteine + O2
?
-
-
-
-
?
gamma-glutamylcysteine + O2
?
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
best small thiol substrate
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
Evr2p, not Evr1p
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
-
-
-
r
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
production of H2O2
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
13.5% of the activity with dithiothreitol
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
0.7% of the activity with dithiothreitol
-
?
GSH + O2 + O2
GSSG + H2O
-
0.7% of the activity with dithiothreitol
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
GSH + O2 + O2
GSSG + H2O
-
-
-
?
L-Cys + O2
? + H2O
-
-
-
-
?
L-Cys + O2
? + H2O
-
-
-
-
?
L-Cys + O2
? + H2O
-
20.3% of the activity with dithiothreitol
-
-
?
L-Cys + O2
? + H2O
-
-
-
-
?
L-Cys + O2
? + H2O
-
17% of the activity with dithiothreitol
-
-
?
L-Cys + O2
? + H2O
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
-
Evr1p
-
-
?
N-acetylcysteine + O2
? + H2O
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
-
12.6% of the activity with dithiothreitol
-
-
?
N-acetylcysteine + O2
? + H2O
-
-
-
-
?
N-acetylcysteine + O2
? + H2O
-
4.6% of the activity with dithiothreitol
-
-
?
N-acetylcysteine + O2
? + H2O
-
-
-
-
?
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
-
i.e. PDI
-
-
ir
protein disulfide isomerase + O2
protein disulfide isomerase disulfide + H2O2
-
-
-
?
protein Mia40 + O2
protein Mia40 disulfide + H2O
-
-
-
-
?
protein Mia40 + O2
protein Mia40 disulfide + H2O
-
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
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a role in synaptic strengthening and in redox activities in the brain
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
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
-
best substrates are cysteine residues in reduced proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
disulfide bridge C15-C124 is not required for activity
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
oxidation of thiols to disulfides with a concomitant reduction of molecular oxygen to peroxide
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in secreted peptide/protein folding in the brain
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
enzyme plays a role in the extracellular matrix as well as in intracellular folding of secreted proteins or hormons like LH and FSH, enzyme acts as an endogenous redox modulator of hormonal secretion, enzyme expression is regulated by estrogens
-
-
ir
R-SH + O2
R-S-S-R + H2O2
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
3 cysteine pairs are required for optimal enzyme function
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
reduced lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
?
reduced lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
?
reduced lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
ir
reduced ribonuclease + O2
ribonuclease + H2O
-
-
-
-
r
reduced ribonuclease + O2
ribonuclease + H2O
-
-
-
-
r
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
reductively denatured pancreatic ribonuclease A
-
-
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
production of H2O2
?
reductively denatured ribonuclease A + O2
renatured ribonuclease + H2O
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
low activity
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
ir
RNase A + O2
RNase A disulfide + H2O2
-
intact enzyme, but not 60-kDa-enzyme fragment
-
-
ir
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
recombinant GmQSOX1 catalyses disulfide-bond formation but is unable to refold the reduced and denatured RNase A into a native form, cooperative refolding of unfolded RNase A by rGmQSOX1 and soybean PDI family proteins of group I and group II, overview. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
ir
thioredoxin + O2
thioredoxin disulfide + H2O2
-
substrate from Escherichia coli
-
-
ir
thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
-
?
additional information
?
-
no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
-
-
?
additional information
?
-
-
low activity with reduced proteins
-
-
?
additional information
?
-
-
peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme
-
-
-
additional information
?
-
-
peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, are not oxidised by the enzyme
-
-
-
additional information
?
-
-
enzyme does not catalyze thiol-disulfide interchange
-
-
?
additional information
?
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
?
additional information
?
-
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
?
additional information
?
-
-
the enzyme may play an important role in the introduction of disulfide bridges in egg white proteins
-
-
?
additional information
?
-
-
possible role for oxidase in protein secretory pathway
-
-
?
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
?
-
-
a 30 kDa enzyme fragment shows no catalytic activity of its own
-
-
?
additional information
?
-
-
preferred substrates are protein or peptide sulfhydryl groups, but not low molecular weight thiols, such as cysteine or glutathione
-
-
?
additional information
?
-
-
recombinant GmQSOX1 expressed in Escherichia coli forms disulfide bonds on reduced and denatured RNase A, but does not show any refolding activity. The reduced and denatured RNase A is effectively refolded by recombinant GmQSOX1 in the presence of the soybean protein disulfide isomerase family protein GmPDIL-2 in the absence of glutathione redox buffer. Low activity withDTT, glutathione is a poor substrate
-
-
?
additional information
?
-
-
the enzyme may provide a crucial switch for the regulation of receptor-Ck-dependent mevalonate pathway
-
-
?
additional information
?
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
?
additional information
?
-
-
enzyme might communicate with the respiratory chain via the mediation of cytochrome c
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
additional information
?
-
-
nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun
-
-
?
additional information
?
-
-
quiescin-sulfhydryl oxidase (QSOX) catalyzes the facile direct introduction of disulfide bonds into unfolded, reduced proteins with the reduction of molecular oxygen to generate hydrogen peroxide. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains, the affinity of QSOX for monomer is significantly lower than that for octamer. QSOX exhibits much lower affinity for N-terminally truncated murine prion protein (PrP89-230) than for the full-length murine prion protein (PrP23-231), suggesting that the N-terminal region of prion protein is critical for the interaction of prion protein with QSOX
-
-
?
additional information
?
-
-
catalytic mechanism of the short, cytokine, form of augmenter of liver regeneration (sfALR) using model thiol substrates of the enzyme. While 2-mercaptoethanol is a very poor substrate of enzyme sfALR, it rapidly generates a mixed disulfide intermediate allowing the thiolate of C145 to form a strong charge-transfer complex with the flavin. Glutathione is unable to form charge-transfer complexes and is no substrate of the oxidase
-
-
?
additional information
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
?
additional information
?
-
redox cycling of the FAD moiety is essential for enzyme activity
-
-
?
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
?
-
-
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
?
-
-
Evr1p is involved in cellular iron homeostasis, physiological role of the ERV1/ALR family enzymes, overview
-
-
?
additional information
?
-
-
the enzyme is involved in mitochondrial biogenesis
-
-
?
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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
redox potentials of TbQSOX-bound FAD and of the CIIIXXCIV proximal disulfide, overview. Determining the redox potential of the CIXXCII motif requires isolating the redox-active TRX domain from the HRR-ERV domains to prevent transfer of reducing equivalents from the CIXXCII dithiol to the CIIIXXCIV and FAD centers of TbQSOX, overview
-
-
?
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drug target
-
QSOX is a potential target for blocking parasite transmission
drug target
-
QSOX is a potential target for blocking parasite transmission
-
evolution
-
augmenter of liver regeneration is a member of the ERV family of small flavin-dependent sulfhydryl oxidases that contain a redox-active CxxC disulfide bond in redox communication with the isoalloxazine ring of bound FAD
evolution
-
enzyme QSOX is an evolutionarily conserved protein present in organisms ranging from the smallest free-living eukaryotes to humans
evolution
-
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
evolution
-
mechanistic parallels between the eukaryotic QSOX enzymes and the DsbA/B system catalyzing disulfide bond generation in the bacterial periplasm are detected suggesting that the strategy of linked disulfide exchanges may be exploited in other catalysts of oxidative protein folding
evolution
the enzyme belongs to a family of flavin adenine dinucleotide (FAD)-dependent sulfhydryl oxidases
evolution
-
based on the analysis of 33 fungal genomes, sulfhydryl oxidase (SOX) encoding genes are close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, the enzyme (AtSOX) is evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin (GliT, HlmI and DepH) are evolutionary closely related to AtSOX whereas fungal thioreductases are more distant
evolution
-
evolutionary and phylogenetic analysis analysis of QSOX, detailed overview. QSOX CXXC motifs display on the neighbor-joining phylogenetic tree. The psiErv/Erv module, strongly characteristic of QSOX, contrasts with a Trx module only weakly differentiated from PDI family domains. QSOX redox-active motifs differ between Metazoa and Viridiplantae and show enhanced diversity among paralogues. Conservation at the Trx-Erv domain interface suggests a conserved electron transfer mechanism. Intron positions do not reveal a common imprint between Viridiplantae and Metazoa
-
evolution
-
based on the analysis of 33 fungal genomes, sulfhydryl oxidase (SOX) encoding genes are close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, the enzyme (AtSOX) is evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin (GliT, HlmI and DepH) are evolutionary closely related to AtSOX whereas fungal thioreductases are more distant
-
malfunction
silencing Sfp53 expression does not rescue the ability of an ac92-knockout virus to produce infectious virus. Similarly, ac92 expression does not affect SfP53-stimulated caspase activity or the localization of SfP53. Although Ac92 binds to SfP53 during AcMNPV replication and oxidizes SfP53 in vitro, no effects of this interaction on AcMNPV replication in cultured cells can be detected. Overexpression or silencing of Ac92 during virus infection does not affect SfP53 accumulation
malfunction
-
substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
malfunction
mutations at a cis-proline in QSOX1 that is conserved across the thioredoxin superfamily result in QSOX1 variants that showed a striking detrimental effect when added exogenously to fibroblasts. They severely disrupt the extracellular matrix and cell adhesion, even in the presence of naturally secreted, wild-type enzyme (QSOX1)
malfunction
-
Pbqsox deletion (DELTApbqsox) does not affect asexual intraerythrocytic development, but reduces exflagellation of male gametocytes as well as formation and maturation of ookinetes. Pbqsox deletion also leads to a significant increase in the reduced thiol groups of ookinete surface proteins
malfunction
-
Pbqsox deletion (DELTApbqsox) does not affect asexual intraerythrocytic development, but reduces exflagellation of male gametocytes as well as formation and maturation of ookinetes. Pbqsox deletion also leads to a significant increase in the reduced thiol groups of ookinete surface proteins
-
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
physiological function
-
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
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
-
enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum
physiological function
-
quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins. Quiescin-sulfhydryl oxidase inhibits formation of prions, infectious glycoproteins that cause a group of fatal transmissible diseases in animals and humans, in vitro. QSOX inhibits human prion propagation in protein misfolding cyclic amplification reactions and murine prion propagation in scrapie-infected neuroblastoma cells. Enzyme QSOX preferentially binds the scrapie isoform prion PrPSc from prion-infected human brains, but not PrPC from uninfected brains
physiological function
the Autographa californica M nucleopolyhedrovirus (AcMNPV) sulfhydryl oxidase Ac92 is essential for production of infectious virions. Ac92 also interacts with human protein p53 and enhances human p53-induced apoptosis in insect cell. Enzyme Ac92 interacts with protein SfP53 from Spodoptera frugiperda in infected Sf9 cells and oxidizes SfP53 in vitro. Ac92 does not affect the cellular localization of SfP53 and partially co-localizes with SfP53 in Sf9 cells. Ac92 does not interact with or oxidize a mutant of SfP53 predicted to lack DNA binding. Ac92 possibly prevents DNA binding of SfP53. Ac92 expression does not stimulate significant caspase activity on its own, nor does it stimulate HA-SfP53-mediated caspase activation above levels induced by SfP53 alone or with an empty vector in transfected Sf9 cells
physiological function
the extracellular location of QSOX proteins suggests that they may be involved in the remodelling of the extracellular matrix, particularly because QSOX can catalyse the formation of disulfide bridges, which are needed for the appropriate folding and stability of various matrix proteins. The expression of QSOX1 in neuroblastoma tumors may influence its clinical course because this protein is involved in processes such as the maturation of the extracellular matrix and the induction of apoptosis in these tumors
physiological function
-
the inability of the relatively bulky glutathione to attain the in-line geometry required for efficient disulfide exchange in sfALR may be physiologically important in preventing the oxidase from catalyzing the potentially harmful oxidation of intracellular glutathione. sfALR protects against hydrogen peroxide and radiation-induced apoptosis
physiological function
-
the reduced and denatured RNase A is effectively refolded by recombinant GmQSOX1 in the presence of the soybean protein disulfide isomerase family protein GmPDIL-2 in the absence of glutathione redox buffer. Enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum
physiological function
among other potential functions, QSOX1 supports extracellular matrix assembly in fibroblast cultures
physiological function
-
epidermal sulfhydryl oxidase mainly cross-links keratins or keratins with other proteins within the corneous core of keratinocytes of the stratum granulare and of the transitional layer. The presence of disulphide bonds in corneocytes and of isopeptide bonds in the cell cornified envelope determines the high chemical, mechanical and antimicrobial resistance of the corneous layer
physiological function
epidermal sulfhydryl oxidase mainly cross-links keratins or keratins with other proteins within the corneous core of keratinocytes of the stratum granulare and of the transitional layer. The presence of disulphide bonds in corneocytes and of isopeptide bonds in the cell cornified envelope determines the high chemical, mechanical and antimicrobial resistance of the corneous layer
physiological function
epidermal sulfhydryl oxidase mainly cross-links keratins or keratins with other proteins within the corneous core of keratinocytes of the stratum granulare and of the transitional layer. The presence of disulphide bonds in corneocytes and of isopeptide bonds in the cell cornified envelope determines the high chemical, mechanical and antimicrobial resistance of the corneous layer
physiological function
-
epidermal sulfhydryl oxidase mainly cross-links keratins or keratins with other proteins within the corneous core of keratinocytes of the stratum granulare and of the transitional layer. The presence of disulphide bonds in corneocytes and of isopeptide bonds in the cell cornified envelope determines the high chemical, mechanical and antimicrobial resistance of the corneous layer
physiological function
-
SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides
physiological function
sulfhydryl oxidase P33 is necessary for budded virus (BV) production and multinucleocapsid occlusion-derived virus (ODV) formation
physiological function
-
the enzyme catalyzes the insertion of disulfide bonds into unfolded, reduced proteins. It is required for parasite sexual development especially for ookinete maturation
physiological function
-
the extracellular enzyme (QSOX1b) transduces migratory and mitogenic responses in primary vascular smooth muscle cells by distinct pathways. The migratory pathway is triggered by active QSOX1b and depends on hydrogen peroxide from Nox1-derived superoxide. The enzyme has a role in neointima formation in balloon-injured rat carotid
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
-
physiological function
-
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
-
SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides
-
physiological function
-
the enzyme catalyzes the insertion of disulfide bonds into unfolded, reduced proteins. It is required for parasite sexual development especially for ookinete maturation
-
additional information
-
E143 and E144 are active site residues in the CxxC motif
additional information
-
in the redox center, CXXC motif of the thioredoxin domain is comparatively oxidizing, consistent with an ability to transfer disulfide bonds to a broad range of thiol substrates. In contrast, the proximal CXXC disulfide in the ERV (essential for respiration and vegetative growth) domain of TbQSOX is strongly reducing, representing a major apparent thermodynamic barrier to overall catalysis. Reduction of the oxidizing FAD cofactor is followed by the strongly favorable reduction of molecular oxygen, role of a mixed disulfide intermediate between thioredoxin and ERV domains, overview. Mixed disulfide bond formation is accompanied by the generation of a charge transfer complex with the flavin cofactor providing thermodynamic coupling among the three redox centers of QSOX and avoids the strongly uphill mismatch between the formal potentials of the thioredoxin and ERV disulfides. Domain organization of TbQSOX together with key catalytic steps deduced from studies of both metazoan and protist QSOXs, overview
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?
x * 47000, SDS-PAGE
?
x * 22000, full length enzyme, SDS-PAGE
?
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
?
-
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
-
?
-
x * 90000, may exist in an aggregated molecular form, SDS-PAGE
?
x * 68000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 100000, native enzyme, SDS-PAGE
?
x * 78000, glycosylated enzyme, x * 60000, non-glycosylated enzyme
?
x * 65000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
the viral enzyme uses an alternate dimerization mode compared to other viral sulfhydryl oxidases, overview. The dimer interface involves helices alpha2 and alpha3
dimer
-
2 * 14378, laser desorption mass spectrometry
dimer
-
1 * 50000 plus 1 * 55000, SDS-PAGE
dimer
-
1 * 50000 plus 1 * 55000, SDS-PAGE
-
dimer
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
dimer
-
2 * 42412, MALDI-TOF, mature protein, 2 * 45000, SDS-PAGE
-
dimer
2 * 33000, calculated and crystallization data
dimer
-
2 * 93000, SDS-PAGE
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
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 * 22000, long Erv1p form, SDS-PAGE, 2 * 15000, short Evrp1 form, SDS-PAGE
dimer
Cys30 and Cys33 are involved in dimer formation
dimer
-
2 * 70000, also aggregates to larger multimers, SDS-PAGE
homodimer
-
monomer
-
1 * 14000, SDS-PAGE, in the infected cell
monomer
-
1 * 66000, SDS-PAGE
monomer
1 * 21000, SDS-PAGE, under reducing conditions
monomer
1 * 23000, SDS-PAGE, under reducing conditions
monomer
1 * 54000, SDS-PAGE
additional information
structure determination, comparison, and modelling, overview
additional information
-
structure determination, comparison, and modelling, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
-
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
-
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
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structure
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
-
enzyme contains an N-terminal thioredoxin domain, an intervening domain, and a C-terminal ALR/ERV domain, redox-active motif CXXC
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
-
isozyme domain structure, overview
additional information
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isozyme domain structure, two splicing variants, overview
additional information
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
-
enzyme contains a protein-disulfide-isomerase-type thioredoxin domain and a yeast ERV1 domain
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
structural analysis of the recombinant enzyme
additional information
-
structural analysis of the recombinant enzyme
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
-
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
-
structure, active site structure containinbg a CXXC motif
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
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
-
domain organization of TbQSOX together with key catalytic steps deduced from studies of both metazoan and protist QSOXs, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
additional information
enzyme QSOX is defined by the presence of both a Trx domain and an Erv domain. QSOX secondary structure comparisons, overview
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yes
a truncated pB119L version lacking 16 residues at the carboxy terminus, i.e. pB119L-DELTAC, is a soluble protein
C72A/C75A
activity indistinguishable from wild-type. Contrary to wild-type, mutant is not modified by maleimide-functionalized polyethylene glycol in presence of dithiothreitol
E174A
dimer interface mutant. The kcat-value of the mutant enzyme is 3.1fold lower than the value of the wild-type enyme
E174A/H227A
dimer interface mutant. The kcat-value of the mutant enzyme is 6.8fold lower than the value of the wild-type enyme
E174K
dimer interface mutant. The kcat-value of the mutant enzyme is 6.7fold lower than the value of the wild-type enyme
E183D
salt bridge mutant. The kcat-value of the mutant enzyme is 1.2fold lower than the value of the wild-type enyme
E183R
salt bridge mutant. The kcat-value of the mutant enzyme is 1.1fold higher than the value of the wild-type enyme
H114A
active-site mutant. The occlusion bodies (OBs) of the mutant have a ragged surface and contain mostly occlusion-derived virus with a single nucleocapsid (ODVs). The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. The kcat-value of the mutant enzyme is 4.1fold lower than the value of the wild-type enyme
H161A
active site mutant. kcat value is too low to be reliably quantitated
H227A
dimer interface mutant. The kcat-value of the mutant enzyme is 3.4fold lower than the value of the wild-type enyme
H227D
dimer interface mutant. The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. kcat value is too low to be reliably quantitated
Q235A
active site mutant. kcat value is too low to be reliably quantitated
R127A/E183A
salt bridge mutant. The occlusion bodies (OBs) of the mutant have a ragged surface and contain mostly occlusion-derived virus with a single nucleocapsid (ODVs). The occlusion bodies (OBs) of the mutant contain lower numbers of ODVs and have a significantly reduced oral infectivity in comparison to control virus. The kcat-value of the mutant enzyme is 1.2fold lower than the value of the wild-type enyme
R127E
salt bridge mutant. The kcat-value of the mutant enzyme is 1.4fold lower than the value of the wild-type enyme
R127E/E183R
salt bridge mutant. The kcat-value of the mutant enzyme is 1.1fold lower than the value of the wild-type enyme
C124A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
C15A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C15A/C124A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
C15A/C74A/C85A/C124A
-
site-directed mutagenesis, increased activity compared to the wild-type enzyme
C74A/C85A
-
site-directed mutagenesis, decreased activity compared to the wild-type enzyme
E143K/E144K
-
site-directed mutagenesis, substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
R194H
mutation isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins
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
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
C159S
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
site-directed mutagenesis, about 60% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain
C33S
site-directed mutagenesis, about 50% reduced activity in vitro compared to the wild-type enzyme, no complementation of an enzyme-defect mutant strain
D24A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N131A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N34A
-
enhancement of catalytic activity for GSH, whereas the catalytic activity for gamma-glutamylcysteine remains unchanged. The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
N34Q
-
the mutant enzyme oxidizes GSH more efficiently (201%) than the wild-type enzyme
P129A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
S32A
-
the mutant enzyme oxidizes GSH more efficiently (169%) than the wild-type enzyme. About 1.5fold increase in GSSG production compared to that of the parental ERV1 gene
S32A/N34A
-
the mutant enzyme oxidizes GSH more efficiently (240%) than the wild-type enzyme and shows comparable activity for gamma-glutamylcysteine (96%). The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
S32T
-
the mutant enzyme oxidizes GSH more efficiently (178%) than the wild-type enzyme
S32T/N34A
-
the mutant enzyme shows almost the same activity for GSH (192%) compared to mutant enzyme S32A, S32T, and N34A, and high activity for gamma-glutamylcysteine (161%). The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
W132A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
N131A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
-
N34A
-
enhancement of catalytic activity for GSH, whereas the catalytic activity for gamma-glutamylcysteine remains unchanged. The mutant enzyme shows slightly decreased maximum temperatures at 55°C (compared to 60°C for the wild-type enzyme)
-
P129A
-
the mutant enzyme oxidizes GSH and gamma-glutamylcysteine at much lower rates than the wild-type enzyme
-
S32A
-
the mutant enzyme oxidizes GSH more efficiently (169%) than the wild-type enzyme. About 1.5fold increase in GSSG production compared to that of the parental ERV1 gene
-
S32T
-
the mutant enzyme oxidizes GSH more efficiently (178%) than the wild-type enzyme
-
C69S
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
C72S
about 5% of wild-type activity with substrate dithiothreitol, 0.5% with substrate rRNase
C133S
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
C30S
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
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
-
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
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
additional information
-
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
additional information
construction of a mutant ac92-knockout virus
additional information
-
construction of a mutant ac92-knockout virus
additional information
antisense constructs of the SOXN gene in Tet21N neuroblastoma cells confer resistance to IFN-gamma-induced apoptosis, while ectopic overexpression in sense direction sensitizes the cells to induced cell death
additional information
-
antisense constructs of the SOXN gene in Tet21N neuroblastoma cells confer resistance to IFN-gamma-induced apoptosis, while ectopic overexpression in sense direction sensitizes the cells to induced cell death
additional information
-
the conserved C-terminal domain of the human Alrp can functionally replace the yeast domain in vivo, genetic system to study function of sulfhydryl oxidases, overview
additional information
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
-
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
additional information
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
additional information
-
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
additional information
-
the wild-type CGAC motif in the thioredoxin domain of enzyme TbQSOX is replaced by the more oxidizing CPHC or more reducing CGPC sequence, resulting in mutants CIPHCII and CIGPCII. Construction of a truncated mutant containing only the thioredoxin domain TbQSOX-TRX, corresponding to residues 20-199
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Ornithorhynchus anatinus, Osphranter rufus, Mesocricetus auratus (A0A1U7R8Y5), Homo sapiens (Q6ZRP7)
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Franca, K.C.; Martinez, P.A.; Prado, M.L.; Lo, S.M.; Borges, B.E.; Zanata, S.M.; San Martin, A.; Nakao, L.S.
Quiescin/sulfhydryl oxidase 1b (QSOX1b) induces migration and proliferation of vascular smooth muscle cells by distinct redox pathways
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Aspergillus tubingensis, Aspergillus tubingensis D-85248
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Du, N.; Wei, Z.C.; Deng, Y.Y.; Zhang, Y.; Tang, X.J.; Li, P.; Huang, Y.B.; Zeng, Q.H.; Wang, J.J.; Zhang, M.W.; Liu, G.
Characterization of recombinant rice quiescin sulfhydryl oxidase and its improvement effect on wheat flour-processing quality
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Oryza sativa Japonica Group (Q6AUC6)
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Zheng, W.; Liu, F.; Du, F.; Yang, F.; Kou, X.; He, Y.; Feng, H.; Fan, Q.; Luo, E.; Min, H.; Miao, J.; Cui, L.; Cao, Y.
Characterization of a sulfhydryl oxidase from Plasmodium berghei as a target for blocking parasite transmission
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Javitt, G.; Grossman-Haham, I.; Alon, A.; Resnick, E.; Mutsafi, Y.
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