Bromid peroksidaza
| Bromid peroksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.11.1.18 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Bromid peroksidaza (EC 1.11.1.18, bromoperoksidaza, haloperoksidaza (nespecifična), eozinofilna peroksidaza) je enzim sa sistematskim imenom bromid:vodonik-peroksid oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- RH + HBr + H2O2 RBr + 2H2O
Ove bromoperoksidaze crvenih i smeđih morskih algi (Rhodophyta i Phaeophyta) sadrže vanadat. One katalizuju brominaciju niza organskih molekula kao što su seskviterpeni, formirajući stabilne C-Br veze. Bromoperoksidaze takođe oksiduju jodide.
Reference
- ↑ De Boer, E., Tromp, M.G.M., Plat, H., Krenn, G.E. and Wever, R (1986). „Vanadium(v) as an essential element for haloperoxidase activity in marine brown-algae - purification and characterization of a vanadium(V)-containing bromoperoxidase from Laminaria saccharina”. Biochim. Biophys. Acta 872: 104-115.
- ↑ Tromp, M.G., Olafsson, G., Krenn, B.E. and Wever, R. (1990). „Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum”. Biochim. Biophys. Acta 1040: 192-198. PMID 2400770.
- ↑ Isupov, M.N., Dalby, A.R., Brindley, A.A., Izumi, Y., Tanabe, T., Murshudov, G.N. and Littlechild, J.A. (2000). „Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis”. J. Mol. Biol. 299: 1035-1049. PMID 10843856.
- ↑ Carter-Franklin, J.N. and Butler, A. (2004). „Vanadium bromoperoxidase-catalyzed biosynthesis of halogenated marine natural products”. J. Am. Chem. Soc. 126: 15060-15066. PMID 15548002.
- ↑ Ohshiro, T., Littlechild, J., Garcia-Rodriguez, E., Isupov, M.N., Iida, Y., Kobayashi, T. and Izumi, Y. (2004). „Modification of halogen specificity of a vanadium-dependent bromoperoxidase”. Protein Sci. 13: 1566-1571. PMID 15133166.
Literatura
- 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.
Vanjske veze
- MeSH Bromide+peroxidase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
