Tiol oksidaza
| Tiol oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.8.3.2 | ||||||||
| CAS broj | 9029-39-4 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
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[уреди | уреди извор]
- ^ Aurbach, G.D. & 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. & 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. & 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. & 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[уреди | уреди извор]
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze[уреди | уреди извор]
- Thiol+oxidase на US National Library of Medicine Medical Subject Headings (MeSH)
