Holin oksidaza
Holin oksidaza (EC 1.1.3.17, holinska oksidaza) je enzim sa sistematskim imenom holin:kiseonik 1-oksidoreduktaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Holin oksidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| Holin oksidaza dimer, Arthrobacter globiformis | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.1.3.17 | ||||||||
| CAS broj | 9028-67-5 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- holin + 2 O2 +H2O betain + 2H2O2 (sveukupna reakcija)
- (1a) holin + O2 betain aldehid +H2O2
- (1b) betain aldehid + O2 +H2O betain +H2O2
Ovaj enzim je flavoprotein (FAD). Kod mnogih bakterija, biljki i životinja, osmoprotektant betain se sintetiše koristeći različite enzime koji katalizuju konverziju: (1) holina u betainski aldehid i (2) betain aldehida u betain.
Reference uredi
- ↑ Ikuta, S., Imamura, S., Misaki, H. and Horiuti, Y. (1977). „Purification and characterization of choline oxidase from Arthrobacter globiformis”. J. Biochem. (Tokyo) 82: 1741-1749. PMID 599154.
- ↑ Rozwadowski, K.L., Khachatourians, G.G. and Selvaraj, G. (1991). „Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli”. J. Bacteriol. 173: 472-478. PMID 1987142.
- ↑ Rand, T., Halkier, T. and Hansen, O.C. (2003). „Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis”. Biochemistry 42: 7188-7194. PMID 12795615.
- ↑ Gadda, G., Powell, N.L. and Menon, P. (2004). „The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase”. Arch. Biochem. Biophys. 430: 264-273. PMID 15369826.
- ↑ Fan, F. and Gadda, G. (2005). „On the catalytic mechanism of choline oxidase”. J. Am. Chem. Soc. 127: 2067-2074. PMID 15713082.
- ↑ Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. (2003). „Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica”. J. Biol. Chem. 278: 4932-4942. PMID 12466265.
- ↑ Fan, F., Ghanem, M. and Gadda, G. (2004). „Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance”. Arch. Biochem. Biophys. 421: 149-158. PMID 14678796.
- ↑ Gadda, G. (2003). „Kinetic mechanism of choline oxidase from Arthrobacter globiformis”. Biochim. Biophys. Acta 1646: 112-118. PMID 12637017.
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.