1.8.3.2: thiol oxidase This is an abbreviated version! For detailed information about thiol oxidase, go to the full flat file .
Word Map on EC 1.8.3.2
Reaction
2 R'C(R)SH
+
O2 =
R'C(R)S-S(R)CR' +
H2O2
Synonyms Ac92, AcMNPV P33, ALR, ALRp, AtSOX, augmenter of liver regeneration, DTT-oxidase, E10R, egg white oxidase, Ero1, Ero1p, ERV/ALR sulfhydryl oxidase, Erv1, Erv1p, Erv2, ERv2p, FAD-linked sulfhydryl oxidase, FAD-linked sulfhydryl oxidase ALR, FAD-sulfhydryl oxidase, flavin adenine dinucleotide-linked sulfhydryl oxidase, flavin-dependent sulfhydryl oxidase, GmQSOX1, GmQSOX2, hepatic regenerative stimulator substance, hepatopoietin, mitochondrial FAD-linked sulfhydryl oxidase ERV1, More, neuroblastoma-derived sulfhydryl oxidase, oxidase, thiol, P33, pB119L, protein pB119L, QSCN6, QSOX, QSOx1, QSOX1b, QSOX2, QSOX3, Quiescin Q6, quiescin Q6 sulfhydryl oxidase, quiescin Q6 sulfhydryl oxidase 1, quiescin Q6/sulfhydryl oxidase, quiescin sulfhydryl oxidase, quiescin sulfhydryl oxidase 1, quiescin sulhydryl oxidase, quiescin-like flavin-dependent sulfhydryl oxidase, Quiescin-sulfhydryl oxidase, quiescin/sulfhydryl oxidase, quiescin/sulfhydryl oxidase 1b, quiescin/sulphydryl oxidase, rQSOX, sfALR, SOX, Sox1, Sox2, SOXN, sulfhydryl oxidase, sulfhydryl oxidase SOx-3, sulfhydryl oxidase, P33, sulphydryl oxidase, thiol oxidase Erv1, thiooxidase
ECTree
Cofactor
Cofactor on EC 1.8.3.2 - thiol oxidase
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flavin
enzyme shows a typical flavin absorbance spectrum, with a maximum at 456 nm
FAD
-
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FAD
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bound to the enzyme
FAD
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bound to the enzyme
FAD
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enzyme is linked to FAD
FAD
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firmly attached but nut covalently linked to the protein
FAD
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one molecule of FAD per subunit
FAD
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enzyme from seminal vesicles
FAD
dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold
FAD
dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity
FAD
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flavoprotein, 1 FAD molecule per enzyme subunit with 1 phosphorus atom per FAD as cofactor of the cofactor
FAD
noncovalently bound, binding site sequence and structure
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
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small FAD-binding domain
FAD
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small FAD-binding domain
FAD
small FAD-binding domain
FAD
small FAD-binding domain
FAD
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small FAD-binding domain, 1 molecule per subunit
FAD
-
dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin
FAD
dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview
FAD
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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
-
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
-
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
FAD
-
the enzyme contains a non-covalently bound flavin cofactor
additional information
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enzyme contains a redox-active cysteine-bridge
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additional information
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enzyme contains a redox-active cysteine-bridge
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additional information
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enzyme contains a redox-active cysteine-bridge
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additional information
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enzyme contains a thioredoxin and a ERV1 domain
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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 domain
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additional information
enzyme contains a thioredoxin domain
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additional information
enzyme contains a thioredoxin domain
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additional information
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enzyme contains a thioredoxin domain
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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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redox-active disulfide involved in catalysis
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