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 | ||||||||
| StrukturePBP | RCSB PDBPDBePDBjPDBsum | ||||||||
| |||||||||
Tiol oksidaza(EC1.8.3.2,sulfhidrilna oksidaza) jeenzimsa sistematskim imenomtiol:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10][11]Ovaj enzimkatalizujesledećuhemijsku reakciju:
- 2 R'C(R)SH + O2R'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.PMID13863296.
- ^Neufeld, H.A., Green, L.F., Latterell, F.M. and Weintraub, R.L. (1958).„Thiooxidase, a new sulfhydryl-oxidizing enzyme fromPiricularia oryzaeandPolyporus vesicolor”.J. Biol. Chem.232:1093—1099.PMID13549489.
- ^Ostrowski, M.C. & Kistler, W.S. (1980). „Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion”.Biochemistry.19:2639—2645.PMID7397095.
- ^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.PMID8940019.
- ^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.PMID17944490.
- ^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.PMID11584268.
- ^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 cytochromecand cytochromecperoxidase in electron shuttling from Erv1”.EMBO J.26:4801—4811.PMID17972915.
- ^Farrell, S.R. & Thorpe, C. (2005). „Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochromecreductase activity”.Biochemistry.44:1532—1541.PMID15683237.
- ^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.PMID16407158.
- ^de la Motte, R.S. & Wagner, F.W. (1987). „Aspergillus nigersulfhydryl oxidase”.Biochemistry.26:7363—7371.PMID3427078.
- ^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.PMID19498160.
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.ISBN019850229X.
- Eric J. Toone (2006).Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution(Volume 75 изд.). Wiley-Interscience.ISBN0471205036.
- Branden C; Tooze J.Introduction to Protein Structure.New York, NY: Garland Publishing.ISBN0-8153-2305-0.
- Irwin H. Segel.Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems(Book 44 изд.). Wiley Classics Library.ISBN0471303097.
- William P. Jencks (1987).Catalysis in Chemistry and Enzymology.Dover Publications.ISBN0486654605.
Spoljašnje veze
[уреди|уреди извор]- Thiol+oxidaseнаUS National Library of Medicine Medical Subject Headings(MeSH)
