Tiol oksidaza
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| Tiol oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.8.3.2 | ||||||||
| CAS broj | 9029-39-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Tiol oksidaza (EC 1.8.3.2, sulfhidrilna oksidaza) je enzim sa sistematskim imenom tiol:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10][11] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- 2 R'C(R)SH + O2 R'C(R)S-S(R)CR' +H2O2
R može da bude =S ili =O, kao i niz drugih grupa. Enzim nije specifičan za R'.
Reference[uredi | uredi kod]
- ↑ Aurbach, G.D. and Jakoby, W.B. (1962). „The multiple functions of thiooxidase”. J. Biol. Chem. 237: 565-568. PMID 13863296.
- ↑ Neufeld, H.A., Green, L.F., Latterell, F.M. and Weintraub, R.L. (1958). „Thiooxidase, a new sulfhydryl-oxidizing enzyme from Piricularia oryzae and Polyporus vesicolor”. J. Biol. Chem. 232: 1093-1099. PMID 13549489.
- ↑ Ostrowski, M.C. and Kistler, W.S. (1980). „Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion”. Biochemistry 19: 2639-2645. PMID 7397095.
- ↑ Hoober, K.L., Joneja, B., White, H.B., 3rd and Thorpe, C. (1996). „A sulfhydryl oxidase from chicken egg white”. J. Biol. Chem. 271: 30510-30516. PMID 8940019.
- ↑ Jaje, J., Wolcott, H.N., Fadugba, O., Cripps, D., Yang, A.J., Mather, I.H. and Thorpe, C. (2007). „A flavin-dependent sulfhydryl oxidase in bovine milk”. Biochemistry 46: 13031-13040. PMID 17944490.
- ↑ Sevier, C.S., Cuozzo, J.W., Vala, A., Aslund, F. and Kaiser, C.A. (2001). „A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation”. Nat. Cell Biol. 3: 874-882. PMID 11584268.
- ↑ Dabir, D.V., Leverich, E.P., Kim, S.K., Tsai, F.D., Hirasawa, M., Knaff, D.B. and Koehler, C.M. (2007). „A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1”. EMBO J. 26: 4801-4811. PMID 17972915.
- ↑ Farrell, S.R. and Thorpe, C. (2005). „Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity”. Biochemistry 44: 1532-1541. PMID 15683237.
- ↑ Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C. and Fass, D. (2006). „Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p”. Proc. Natl. Acad. Sci. USA 103: 299-304. PMID 16407158.
- ↑ de la Motte, R.S. and Wagner, F.W. (1987). „Aspergillus niger sulfhydryl oxidase”. Biochemistry 26: 7363-7371. PMID 3427078.
- ↑ Riemer, J., Bulleid, N. and Herrmann, J.M. (2009). „Disulfide formation in the ER and mitochondria: two solutions to a common process”. Science 324: 1284-1287. PMID 19498160.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.