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Information on EC 1.8.3.2 - thiol oxidase
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EC Tree
1.8.3.2 thiol oxidaseIUBMB Comments
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
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Word Map
- 1.8.3.2
- hepatocytes
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intermembrane
- oxidases
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relay
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qsoxs
- thioredoxin
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redox-active
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hepatectomy
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hepatotrophic
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reoxidized
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hepatectomized
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flavoenzyme
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fad-dependent
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fad-binding
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oxidoreductins
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flavin-linked
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redox-regulated
- isoalloxazine
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3h-tdr
- diagnostics
- medicine
- nutrition
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
qsox1, sulfhydryl oxidase, augmenter of liver regeneration, ero1p, thiol oxidase, hepatopoietin, erv2p, erv1p, sulphydryl oxidase, sfalr, 
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
ter bi substituted mechanism, O2 binds first
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2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
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2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
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2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
enzyme contains a functionally involved redox-active motif CXXC
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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
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
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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
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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 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
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2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2
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PATHWAY SOURCE
PATHWAYS
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