Diarilpropan peroksidaza
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| Diarilpropan peroksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.11.1.14 | ||||||||
| CAS broj | 93792-13-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Diarilpropan peroksidaza (EC 1.11.1.14, diarilpropanska oksigenaza, ligninaza I, diarilpropanska peroksidaza, LiP, diarilpropan:kiseonik,vodonik-peroksidna oksidoreduktaza (raskidanje C-C veze)) je enzim sa sistematskim imenom 1,2-bis(3,4-dimetoksifenil)propan-1,3-diol:vodonik-peroksid oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (3,4-dimetoksifenil)metanol + H2O2 3,4-dimetoksibenzaldehid + 2H2O
Ovaj enzim je hemoprotein. On učestvuje u oksidativnom razlaganju lignina gljivama Basidiomycete.
Reference[uredi | uredi kod]
- ↑ Kersten, P.J., Tien, M., Kalyanaraman, B. and Kirk, T.K. (1985). „The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes”. J. Biol. Chem. 260: 2609-2612. PMID 2982828.
- ↑ Paszczynski, A., Huynh, V.-B. and Crawford, R. (1986). „Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium”. Arch. Biochem. Biophys. 244: 750-765. PMID 3080953.
- ↑ Harvey, P.J., Schoemaker, H.E. and Palmer, J.M. (1986). „Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium”. FEBS Lett. 195: 242-246.
- ↑ Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. (1998). „Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis”. Biochemistry 37: 15097-15105. PMID 9790672.
- ↑ Wariishi, H., Marquez, L., Dunford, H.B. and Gold, M.H. (1990). „Lignin peroxidase compounds II and III. Spectral and kinetic characterization of reactions with peroxides”. J. Biol. Chem. 265: 11137-11142. PMID 2162833.
- ↑ Cai, D.Y. and Tien, M. (1990). „Characterization of the oxycomplex of lignin peroxidases from Phanerochaete chrysosporium: equilibrium and kinetics studies”. Biochemistry 29: 2085-2091. PMID 2328240.
- ↑ Khindaria, A., Yamazaki, I. and Aust, S.D. (1995). „Veratryl alcohol oxidation by lignin peroxidase”. Biochemistry 34: 16860-16869. PMID 8527462.
- ↑ Khindaria, A., Yamazaki, I. and Aust, S.D. (1996). „Stabilization of the veratryl alcohol cation radical by lignin peroxidase”. Biochemistry 35: 6418-6424. PMID 8639588.
- ↑ Khindaria, A., Nie, G. and Aust, S.D. (1997). „Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex”. Biochemistry 36: 14181-14185. PMID 9369491.
Literatura[uredi | uredi kod]
- 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.