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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
-
-
-
-
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
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
enzyme contains a functionally involved redox-active motif YPCCXXC
-
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
reaction mechanism
-
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; 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; 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; 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; 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; 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; 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; 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; 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
-
-
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2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
2 D-Cys + 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
-
-
?
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 + H2O
reduced lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
ir
reduced ovalbumin + O2
ovalbumin + H2O
-
-
-
-
?
reduced pyruvate kinase + O2
pyruvate kinase + H2O
-
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + 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 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 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
-
-
-
?
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
-
-
-
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
-
-
-
-
?
cysteamine + 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
-
-
-
?
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
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
-
-
-
-
?
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
-
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
-
-
-
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
-
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
-
-
-
?
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
3 cysteine pairs are required for optimal enzyme function
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
reduced lysozyme + O2
lysozyme + H2O
-
-
-
-
?
reduced lysozyme + O2
lysozyme + H2O
-
-
-
-
?
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
?
-
-
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 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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
-
-
-
-
?
lysozyme + O2
lysozyme disulfide + H2O2
-
-
-
-
?
ovalbumin + O2
ovalbumin disulfide + H2O2
-
-
-
-
?
protein Mia40 + O2
protein Mia40 disulfide + H2O
-
-
-
-
?
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
ir
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
-
-
-
-
?
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
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
ir
R-SH + O2
R-S-S-R + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
RNase A + O2
RNase A disulfide + H2O2
-
-
-
-
?
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
?
-
-
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 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
?
-
-
enzyme appears to protect sperm structure and function against damage by endogeneous sulfhydryls
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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7.9 - 54
2-mercaptoethanol
100
2-nitro-5-thiobenzoic acid
-
-
0.03 - 52.2
dithiothreitol
1.72
N-acetyl-EAQCGTS
-
expressed per thiol basis
1.13 - 3.85
N-acetyl-L-Cys
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 - 0.115
Reduced ribonuclease
-
0.36
rRNaseA
pH 7.5, 37°C
-
additional information
additional information
-
7.9
2-mercaptoethanol
pH 7.5, 20°C
9.73
2-mercaptoethanol
pH 7.5, 20°C
1.25
cysteamine
-
-
1.33
D-Cys
-
-
0.03
dithiothreitol
-
mutant CIPHCII, pH 7.0, 25°C
0.086
dithiothreitol
pH 7.5, 37°C
0.17
dithiothreitol
-
wild-type enzyme, pH 7.0, 25°C
0.22
dithiothreitol
-
mutant CIGPCII, pH 7.0, 25°C
1.3
dithiothreitol
-
pH 7.5, 25°C, recombinant mutant C15A
1.7
dithiothreitol
-
pH 7.5, 25°C, recombinant mutant C15A/C74A/C85A/C124A
1.8
dithiothreitol
-
pH 7.5, 25°C, recombinant mutant C124A
2
dithiothreitol
-
pH 7.5, 25°C, recombinant mutants C74A/C85A and C15A/C124A
2.1
dithiothreitol
-
pH 7.5, 25°C, recombinant wild-type enzyme
2.41
dithiothreitol
pH 7.5, 20°C
4.9
dithiothreitol
pH 7.5, 20°C
52.2
dithiothreitol
-
recombinant enzyme, pH 7.4, 25°C
0.14
DTT
-
native enzyme, pH 7.5
12.5
DTT
-
60 kDa enzyme fragment, pH 7.5
0.02
glutathione
-
-
2.78
glutathione
pH 7.5, 20°C
3.7
glutathione
pH 7.5, 20°C
6.7
glutathione
-
pH 5.5, 25°C
0.09
GSH
-
-
0.42
L-Cys
-
-
1.13
N-acetyl-L-Cys
-
-
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
0.018
O2
-
25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.027
O2
-
25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
0.057
O2
-
25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
0.062
O2
-
25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.087
O2
-
25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
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, 25°C
-
0.04
RNAse A
-
mutant CIPHCII, pH 7.0, 25°C
-
0.22
RNAse A
-
recombinant enzyme, pH 7.4, 25°C
-
0.32
RNAse A
-
mutant CIGPCII, pH 7.0, 25°C
-
0.36
RNAse A
-
wild-type enzyme, pH 7.0, 25°C
-
additional information
additional information
-
the activity with small thiols is dominated by the Km value
-
additional information
additional information
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
-
additional information
additional information
-
binding kinetics of immobilized QSOX to various PrP prion proteins
-
additional information
additional information
-
pre-steady state kinetics and stopped-flow measurements of sfALR using DTT to slow down the reaction velocity
-
additional information
additional information
-
stopped-flow kinetic measurements
-
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1.8.3.2 thiol oxidase
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