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thiol oxidase

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In enzymology, a thiol oxidase (EC 1.8.3.2) is an enzyme that catalyzes the chemical reaction

4 R'C(R)SH + O₂

\rightleftharpoons

2 R'C(R)S-S(R)CR' + 2 H₂O

Thus, the two substrates of this enzyme are R'C(R)SH and O₂, whereas its two products are R'C(R)S-S(R)CR' and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is thiol:oxygen oxidoreductase. This enzyme is also called sulfhydryl oxidase.

References

AURBACH GD, JAKOBY WB (1962). "The multiple functions of thiooxidase". J. Biol. Chem. 237: 565–8. PMID 13863296.
NEUFELD HA, GREEN LF, LATTERELL FM, WEINTRAUB RL (1958). "Thioxidase, a new sulfhydryl-oxidizing enzyme from Piricularia oryzae and Polyporus versicolor". J. Biol. Chem. 232 (2): 1093–9. PMID 13549489.

v t e Oxidoreductases: sulfur oxidoreductases (EC 1.8)
1.8.1: NAD or NADP	Dihydrolipoamide dehydrogenase Glutathione reductase Thioredoxin reductase
1.8.2: cytochrome	Sulfite dehydrogenase Thiosulfate dehydrogenase Flavocytochrome c sulfide dehydrogenase
1.8.3: oxygen	Sulfite oxidase
1.8.4: disulfide	Glutathione—homocystine transhydrogenase
1.8.5: quinone	Glutathione dehydrogenase (ascorbate)
1.8.98: Other, known	CoB—CoM heterodisulfide reductase
1.8.99: Other	Sulfite reductase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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