The Enzyme Database

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EC 1.8.3.2     
Accepted name: thiol oxidase
Reaction: 2 R′C(R)SH + O2 = R′C(R)S-S(R)CR′ + H2O2
Other name(s): sulfhydryl oxidase
Systematic name: thiol:oxygen oxidoreductase
Comments: R may be =S or =O, or a variety of other groups. The enzyme is not specific for R′.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-39-4
References:
1.  Aurbach, G.D. and Jakoby, W.B. The multiple functions of thiooxidase. J. Biol. Chem. 237 (1962) 565–568. [PMID: 13863296]
2.  Neufeld, H.A., Green, L.F., Latterell, F.M. and Weintraub, R.L. Thiooxidase, a new sulfhydryl-oxidizing enzyme from Piricularia oryzae and Polyporus vesicolor. J. Biol. Chem. 232 (1958) 1093–1099. [PMID: 13549489]
3.  Ostrowski, M.C. and Kistler, W.S. Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion. Biochemistry 19 (1980) 2639–2645. [PMID: 7397095]
4.  Hoober, K.L., Joneja, B., White, H.B., 3rd and Thorpe, C. A sulfhydryl oxidase from chicken egg white. J. Biol. Chem. 271 (1996) 30510–30516. [PMID: 8940019]
5.  Jaje, J., Wolcott, H.N., Fadugba, O., Cripps, D., Yang, A.J., Mather, I.H. and Thorpe, C. A flavin-dependent sulfhydryl oxidase in bovine milk. Biochemistry 46 (2007) 13031–13040. [PMID: 17944490]
6.  Sevier, C.S., Cuozzo, J.W., Vala, A., Aslund, F. and Kaiser, C.A. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3 (2001) 874–882. [PMID: 11584268]
7.  Dabir, D.V., Leverich, E.P., Kim, S.K., Tsai, F.D., Hirasawa, M., Knaff, D.B. and Koehler, C.M. A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1. EMBO J. 26 (2007) 4801–4811. [PMID: 17972915]
8.  Farrell, S.R. and Thorpe, C. Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity. Biochemistry 44 (2005) 1532–1541. [PMID: 15683237]
9.  Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C. and Fass, D. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. USA 103 (2006) 299–304. [PMID: 16407158]
10.  de la Motte, R.S. and Wagner, F.W. Aspergillus niger sulfhydryl oxidase. Biochemistry 26 (1987) 7363–7371. [PMID: 3427078]
11.  Riemer, J., Bulleid, N. and Herrmann, J.M. Disulfide formation in the ER and mitochondria: two solutions to a common process. Science 324 (2009) 1284–1287. [PMID: 19498160]
[EC 1.8.3.2 created 1961, modified 2010, modified 2011]
 
 


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