Katehol oksidaza
| Katehol oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.10.3.1 | ||||||||
| CAS broj | 2594228 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Katehol oksidaza (EC 1.10.3.1, difenolna oksidaza, o-difenolaza, polifenolna oksidaza, pirokateholna oksidaza, dopa oksidaza, kateholaza, o-difenol:kiseonik oksidoreduktaza, o-difenolna oksidoreduktaza) je enzim sa sistematskim imenom 1,2-benzendiol:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- 2 katehol + O2 2 1,2-benzohinon + 2H2O
Ovaj enzim je tip 3 bakarni protein koji ekskluzivno katalizuje oksidaciju katehola do o-hinona.
Reference
- ↑ Brown, F.C. and Ward, D.N. (1957). „Preparation of a soluble mammalian tyrosinase”. J. Am. Chem. Soc. 79: 2647-2648.
- ↑ Dawson, C.R. and Tarpley, W.B. (1951). „The copper oxidases”. u: Sumner, J.B. and Myrbäck, K.. The Enzymes. 2 (1st izd.). New York: Academic Press. str. 454-498.
- ↑ Gregory, R.P.F. and Bendall, D.S. (1966). „The purification and some properties of the polyphenol oxidse from tea (Camellia sinensis L.)”. Biochem. J. 101: 569-581.
- ↑ Mason, H.S. (1956). „Structures and functions of the phenolase complex”. Nature (Lond.) 177: 79-81. PMID 13288597.
- ↑ Mayer, A.M. and Harel, E. (1979). „Polyphenol oxidases in plants”. Phytochemistry 18: 193-215.
- ↑ Patil, S.S. and Zucker, M. (1965). „Potato phenolases. Purification and properties”. J. Biol. Chem. 240: 3938-3943. PMID 5842066.
- ↑ Pomerantz, S.H. (1967). „3,4-Dihydroxy-L-phenylalanine as the tyrosinase cofactor. Occurrence in melanoma and binding constant”. J. Biol. Chem. 242: 5308-5314. PMID 4965136.
- ↑ Robb, D.A. (1984). „`Tyrosinase”. u: Lontie, R.. Copper Proteins and Copper Enzymes. 2. Boca Raton, FL: CRC Press. str. 207-240.
- ↑ Gerdemann, C., Eicken, C. and Krebs, B. (2002). „The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins”. Acc. Chem. Res. 35: 183-191. PMID 11900522.
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.
Spoljašnje veze
- MeSH Catechol+oxidase
- 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
