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Enzyme Nomenclature
Information on EC 1.8.3.2 - thiol oxidase
for references in articles please use BRENDA:EC1.8.3.2
Word Map on EC 1.8.3.2
- 1.8.3.2
- disulfide
- thiols
- hepatocytes
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intermembrane
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oxidases
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relay
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qsoxs
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hepatectomy
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redox-active
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hepatotrophic
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hepatectomized
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oxidoreductins
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fad-binding
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fad-dependent
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flavin-linked
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redox-regulated
- isoalloxazine
- medicine
- nutrition
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3h-tdr
- diagnostics
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.8.3.2
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RECOMMENDED NAME
GeneOntology No.
thiol oxidase
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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
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
enzyme contains a functionally involved redox-active motif YPCCXXC
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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
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
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
I0YJW9;
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
B0UXN0;, F1QJL3;
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
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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; 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
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
thiol:oxygen oxidoreductase
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
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CAS REGISTRY NUMBER
COMMENTARY
9029-39-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
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enzyme QSOX is an evolutionarily conserved protein present in organisms ranging from the smallest free-living eukaryotes to humans
evolution
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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
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; 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
I0YJW9;
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
B0UXN0;, F1QJL3;
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; 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; 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; 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; 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; 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; 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; 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
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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
-
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
-
malfunction
-
substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential
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
physiological function
-
Erv1p is a FAD-dependent sulfhydryl oxidase and is an essential component of the redox regulated Mia40/Erv1 import and assembly pathway used by many of the cysteine-containing intermembrane space proteins
physiological function
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
physiological function
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
-
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 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 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
-
enzymes GmQSOX1a,GmQSOX1b, and GmQSOX2a play important roles in protein folding in the endoplasmic reticulum; 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
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
-
enzyme gene eroA gene is essential for viability. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant; isoform ErvA gene ervA does not have an obvious role in the secretion of native proteins, including glucoamylase. It is able to complement the ERO1 function in the Saccharomyces cerevisiae ero1-1 mutant
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
cysteine + O2
cystine + H2O2
artificial in vitro substrate
-
-
ir
D-penicillamine + O2
? + H2O
-
33% of the activity with dithiothreitol
-
-
?
dithiothreitol + reduced cytochrome c
dithiothreitol disulfide + oxidized cytochrome c
-
cytochrome c is about 100fold more effective than O2 as reducing cosubstrate
-
-
?
insulin A and B chains + O2
disulfide of insulin A and B chains + H2O2
-
-
-
-
?
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 SfP53 + O2
protein SfP53 disulfide + H2O2
-
-
-
?
reduced riboflavin-binding protein + O2
riboflavin-binding protein + H2O
-
-
-
-
?
reduced thioredoxin + O2
thioredoxin disulfide + H2O2
-
-
-
r
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
thioglycolate + O2
? + H2O
-
11.1% of the activity with dithiothreitol
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
-
-
-
?
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + 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-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
-
2-mercaptoethanol + O2
? + H2O
-
3.7% of the activity with dithiothreitol
-
-
?
dithiothreitol + O2
? + H2O
-
anaerobically, the ferricenium ion is a facile alternative electron acceptor
production of H2O2
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
artificial in vitro substrate
-
-
ir
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
-
-
r
dithiothreitol + O2
dithiothreitol disulfide + H2O2
-
intact enzyme and 60-kDa-enzyme fragment
-
-
ir
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
-
disulfide oxidase activity, reduction of flavin to a stable neutral semiquinone, further reduction can occur by addition of dithionite
-
-
?
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
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
best small thiol substrate
-
-
?
glutathione + O2
glutathione disulfide + H2O2
-
Evr2p, not Evr1p
-
-
?
GSH + O2 + O2
GSSG + H2O
-
13.5% of the activity with dithiothreitol
-
-
?
GSH + O2 + O2
GSSG + H2O
-
0.7% of the activity with dithiothreitol
-
?
N-acetylcysteine + O2
? + H2O
-
12.6% of the activity with dithiothreitol
-
-
-
N-acetylcysteine + O2
? + H2O
-
4.6% of the activity with dithiothreitol
-
-
-
N-acetylcysteine + O2
? + H2O
-
4.6% of the activity with dithiothreitol
-
-
?
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
-
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
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
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
-
enzyme plays a role in synaptic strengthening and in redox activities in the brain
-
-
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
-
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
-
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
3 cysteine pairs are required for optimal enzyme function
-
-
?
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
-
intact enzyme, but not 60-kDa-enzyme fragment
-
-
ir
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
-
-
?
thioredoxin + O2
thioredoxin disulfide + H2O2
-
substrate from Escherichia coli
-
-
ir
additional information
?
-
no activity with glutathione, 2-mercaptoethanol, and di(2-mercaptoethanol)
-
-
-
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
?
-
-
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.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
riboflavin-binding protein + O2
riboflavin-binding protein disulfide + H2O2
-
-
-
-
?
R-SH + O2
R-S-S-R + H2O2
Q8GXX0
enzyme is essential for biogenesis of mitochondrial and cytosolic iron sulfur cluster assembly
-
-
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
-
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
-
enzyme might counterbalance the plasmin reductase in extracellular reductive processes
-
-
ir
R-SH + O2
R-S-S-R + H2O2
O00391
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
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
Q6IUU3
enzyme plays a significant role in oxidative folding of a large variety of proteins
-
-
?
additional information
?
-
-
sulfhydryl oxidase Sox-3 can be implicated in the negative cell cycle control
-
-
-
additional information
?
-
O08841
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
?
-
Q6ZRP7
enzyme is involved in regulation/deregulation of MYCN gene expression which is a critical determinant in neuroblastoma progression, enzyme renders the cell sensitive to IFN-gamma-induced apoptosis
-
-
-
additional information
?
-
-
enzyme might communicate with the respiratory chain via the mediation of cytochrome c
-
-
-
additional information
?
-
-
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
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the enzyme is involved in mitochondrial biogenesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
FAD
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firmly attached but nut covalently linked to the protein; one molecule of FAD per subunit
FAD
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flavoprotein, 1 FAD molecule per enzyme subunit with 1 phosphorus atom per FAD as cofactor of the cofactor
FAD
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required for activity, binding domain is located on the 60-kDa-enzyme fragment, electron-transfer mechanism in the native enzyme and the 60 kDA enzyme fragment
FAD
dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold
FAD
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dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity
FAD
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dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin
FAD
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dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview
FAD
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dependent on. The three disulfides of the enzyme are not essential for FAD binding
FAD
turnover is limited by an internal redox step leading to 2-electron reduction of the FAD cofactor
FAD
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at a diminutive FAD binding domain, the isoalloxazine ring of the flavin prosthetic group is bound at the mouth of a 4-helix bundle in each subunit with a 5th small helix adjacent to the adenine moiety of FAD. A proximal redox-active disulfide is located adjacent to the C4a position of the isoalloxazine ring
FAD
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reduction of the oxidizing FAD cofactor is followed by the strongly favorable reduction of molecular oxygen, mixed disulfide bond formation is accompanied by the generation of a charge transfer complex with the flavin cofactor. Generation of a 5-deaza-FAD-substituted enzyme by reconstituting the apoprotein with the flavin analogue. Redox potentials of TbQSOX-bound FAD and of the CIIIXXCIV proximal disulfide, overview
additional information
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enzyme contains a thioredoxin domain, 1 redox-active disulfide per subunit
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additional information
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enzyme contains a thioredoxin and an ERV1 domain
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additional information
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enzyme contains a thioredoxin and a ERV1 domain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Iron
MgSO4
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in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DTT
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rapid reaction studies show that dithiothreitol generates a transient mixed disulfide intermediate with sfALR signaled by a weak charge-transfer interaction between the thiolate of C145 and the oxidized flavin, reducing the transfer of reducing equivalents and reoxidation of the reduced flavin by molecular oxygen
RNAi
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silences QSOX. Survival of QSOX-silenced insects is reduced over controls following blood digestion, most likely due to the compromised ability of mosquitoes to scavenge and/or prevent damage caused by blood meal-derived oxidative stress. Higher lipid peroxidation and mortality in QSOX-silenced mosquitoes may be an indication that the redox balance is altered in these insects after a blood meal
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EDTA
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inhibition of enzyme from kidney and small intestine, no inhibition of enzyme from skin and seminal vesivles
Zn2+
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weak binding to the four-electron-reduced enzyme, rapid inhibition, modeling of metal binding
Zn2+
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upon coordination with Zn2+, full reduction of Erv2p requires 6 electrons. Strongly inhibits Erv2p when assayed using tris(2-carboxyethyl)phosphine as the reducing substrate of the oxidase. Restoration of 1 mM EDTA effects rapid recovery of 80% of the original activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
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high concentrations of H2O2, inducing apoptosis, cause an increase of QSOX1 mRNA and protein
L-Cys
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fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme
MgSO4
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in the absence of MgSO4 in the growth medium, growth is weak and no enzyme activity detected. Highest activity at 0.1% MgSO4 in the medium
soybean PDI family protein
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cooperative refolding of unfolded RNase A by rGmQSOX1 and all tested soybean PDI family proteins of group I and group II, but not of group III. Most effective are GmPDIL-2 and GmPDIL-1 with rGmQSOX1. These PDI family proteins contain two classic CGHC motifs in the a and a' domains, except for the group III PDI family proteins, which have nonclassic active centre CXXC motifs. The combination of rGmQSOX1 and GmPDIL-2 with an a-b-b'-a' domain structure shows the highest level of refolding activity, while the GmPDIL-2 C101A/C104A/C440A/C443A mutant, in which all of the cysteines in the two active centres are replaced with alanines, is devoid of cooperative oxidative refolding activity with rGmQSOX1. The refolding activity of rGmQSOX1 combined with the C104A/C443A mutant is 18% of that of rGmQSOX1 combined with wild-type GmPDIL-2. Analysis of the cooperation mechanism, overview
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additional information
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enzyme expression in endometrial glandular epithelium is inducible by estradiol in presence of cycloheximide, and by serum deprivation
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additional information
enzyme QSOX1 expression in fibroblasts is inducible by serum deprivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
O2
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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
0.018
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.027
O2
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25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
0.057
O2
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25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
0.062
O2
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25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.087
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
0.0174
Reduced ribonuclease
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corresponds to a sulfhydryl concentration of 0.14 mM
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additional information
additional information
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the activity with small thiols is dominated by the Km value
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additional information
additional information
the activity with small thiols is dominated by the Km value
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additional information
additional information
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redox potential of wild-type and mutant enzymes
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additional information
additional information
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oxygen consumption kinetic parameters for the WT and Erv1p mutants, overview
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additional information
additional information
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binding kinetics of immobilized QSOX to various PrP prion proteins
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additional information
additional information
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pre-steady state kinetics and stopped-flow measurements of sfALR using DTT to slow down the reaction velocity
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additional information
additional information
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stopped-flow kinetic measurements
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.8
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
1.1
O2
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25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
1.3
O2
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25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
1.5
O2
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25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0023
O2
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25°C, recombinant wild-type enzyme, in presence of 10 mM DTT
0.0024
O2
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25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT
0.0039
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine
0.0041
O2
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25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine
0.0093
O2
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25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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a continuous fluorescence assay for sulfhydryl oxidase
additional information
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several assay methods are used dependent on the substrate, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
8 - 8.2
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oxidation of 5,5'-dithiobis(2-nitrobenzoic acid) and reactivation of ribonuclease
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
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pH 5.0: about 40% of maximal activity, pH 11: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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expression analysis of a panel of cDNAs derived from 50 clinically-graded normal and malignant breast tissue samples for the expression of QSOX1 mRNAs, significant correlation between relative transcript level and clinical grade malignant breast tumors
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endometrial cells. Enzyme level increases during a serum depletion-induced quiescence, decreases when cells enter the g1 phase after serum stimulation, and is restored during the S and G2/M phases
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immunohistochemic enzyme localization study in hair follicles and keratine structures in the human hair, overview
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high expression in neurons producing disulfide-bounded neuropeptides
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immunohistochemical expression of the protein quiescin sulfhydryl oxidase 1 (QSOX1) in samples obtained from untreated neuroblastomas with the patients' clinical and pathological prognostic factors and clinical course. The immunoexpression of QSOX1 correlates with the type of tumor stroma and is higher in Schwannian stroma-rich tumors. Statistically significant correlation between QSOX1 expression and well-differentiated neuroblastomas
additional information
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highest enzyme expression in reticular structures, such as the basal forebrain, reticular thalamic nucleus, and reticular nuclei of the brainstem
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especially in neurons throughout the rostrocaudal extent of the brain as well as in the spinal cord, in olfactory bulbs, isocortex, hippocampus, basal telencephalon, several thalamic and hypothalamic nuclei, cerebellum, and brainstem nuclei
additional information
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recombinant baculovirus in Spodoptera frugiperda SF9 insect cells
additional information
recombinant baculovirus in Spodoptera frugiperda SF9 insect cells
additional information
tissue expression and distribution, high enzyme concentration in cell types associated with heavy secretory loads
additional information
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enzyme is expressed in a large number of different cell types and tissues
additional information
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detailed analysis of cellular and subcellular enzyme localization, overview
additional information
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in-situ detection of enzyme expression in pituitary gland
additional information
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enzyme is expressed in a large number of different cell types and tissues
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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isoform EroA is retained in the ER lumen by a C-terminal retention motif
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isoform EroA is retained in the ER lumen by a C-terminal retention motif
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