Peroksidaza
| Peroksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.11.1.7 | ||||||||
| CAS broj | 9003-99-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Peroksidaza (EC 1.11.1.7, laktoperoksidaza, gvajakolna peroksidaza, biljna peroksidaza, peroksidaza zrna soje, ekstenzinska peroksidaza, hem peroksidaza, oksiperoksidaza, protohem peroksidaza, pirokateholna peroksidaza, skopoletinska peroksidaza, Coprinus cinereus peroksidaza, Arthromyces ramosus peroksidaza) je enzim sa sistematskim imenom fenolni donor:vodonik-peroksid oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- 2 fenolni donor + H2O2 2 fenoksil radical donora + 2 H2O
Enzimi ove grupe su hemni proteini sa histidinom kao proksimalnim ligandom.
- ↑ Kenten, R.H. and Mann, P.J.G. (1954). „Simple method for the preparation of horseradish peroxidase”. Biochem. J. 57: 347-348. PMID 13172193.
- ↑ Morrison, M., Hamilton, H.B. and Stotz, E. (1957). „The isolation and purification of lactoperoxidase by ion exchange chromatography”. J. Biol. Chem. 228: 767-776. PMID 13475358.
- ↑ Paul, K.G. (1963). „Peroxidases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 8 (2nd izd.). New York: Academic Press. str. 227-274.
- ↑ Tagawa, K., Shin, M. and Okunuki, K. (1959). „Peroxidases from wheat germ”. Nature (Lond.) 183: 111-111. PMID 13622706.
- ↑ Theorell, H. (1943). „The preparation and some properties of crystalline horse-radish peroxidase”. Ark. Kemi Mineral. Geol. 16A No. 2: 1-11.
- ↑ Farhangrazi, Z.S., Copeland, B.R., Nakayama, T., Amachi, T., Yamazaki, I. and Powers, L.S. (1994). „Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase”. Biochemistry 33: 5647-5652. PMID 8180190.
- ↑ Aitken, M.D. and Heck, P.E. (1998). „Turnover capacity of coprinus cinereus peroxidase for phenol and monosubstituted phenol”. Biotechnol. Prog. 14: 487-492. PMID 9622531.
- ↑ Dunford, H.B. (1999). Heme peroxidases. Wiley-VCH, New York. str. 33-218.
- ↑ Torres, E and Ayala, M. (2010). Biocatalysis based on heme peroxidases. Springer, Berlin. str. 7-110.
- 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.