Askorbat ferireduktaza (transmembranska)
(Preusmjereno sa stranice Fe(III):askorbatna oksidorektuktaza (translokacija elektrona))
Askorbat ferireduktaza (transmembranska) (EC 1.16.5.1, citohrom b561 (nespecifična)) je enzim sa sistematskim imenom Fe(III):askorbatna oksidorektuktaza (translokacija elektrona).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Askorbat ferireduktaza (transmembranska) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.16.5.1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- askorbat [strana 1] + Fe(III) [strana 2] monodehidroaskorbat [strana 1] + Fe(II) [strana 2]
Ovaj dihemni citohrom transportuje elektrone kroz membrane, kao što je spoljašnja membrana enterocita.
Reference
uredi- ↑ Flatmark, T. and Terland, O. (1971). „Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome”. Biochim. Biophys. Acta 253: 487-491. PMID 4332308.
- ↑ McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F. and Simpson, R.J. (2001). „An iron-regulated ferric reductase associated with the absorption of dietary iron”. Science 291: 1755-1759. PMID 11230685.
- ↑ Su, D. and Asard, H. (2006). „Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases”. FEBS J. 273: 3722-3734. PMID 16911521.
- ↑ Berczi, A., Su, D. and Asard, H. (2007). „An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability”. FEBS Lett. 581: 1505-1508. PMID 17376442.
- ↑ Wyman, S., Simpson, R.J., McKie, A.T. and Sharp, P.A. (2008). „Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro”. FEBS Lett. 582: 1901-1906. PMID 18498772.
- ↑ Glanfield, A., McManus, D.P., Smyth, D.J., Lovas, E.M., Loukas, A., Gobert, G.N. and Jones, M.K. (2010). „A cytochrome b561 with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum”. PLoS Negl. Trop. Dis. 4: #e884-e884. PMID 21103361.
Literatura
uredi- 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.