Holin monooksigenaza
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| Holin monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.15.7 | ||||||||
| CAS broj | 118390-76-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Holin monooksigenaza (EC 1.14.15.7, holinska monooksigenaza) je enzim sa sistematskim imenom holin,redukovani-feredoksin:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju:
- holin + O2 + 2 redukovani feredoksin + 2 H+ betain aldehid hidrat + H2O + 2 oksidovani feredoksin
Enzim iz španaća, koji je lociran u hloroplastima, sadrži Riskijev tip [2Fe-2S] klastera, kao i mononuklearni Fe centar. Za dejstvo ovog enzima je neophodan Mg2+. On katalizuje prvi korak u sintezi glicin betaina. Kod mnogih bakterija, biljiki i životinja, betain se sintetiše u dva koraka: (1) holin do betainskog aldehida i (2) betainski aldehid do betaina.
Reference[uredi | uredi kod]
- ↑ Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. (1989). „Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma”. Plant Physiol. 90: 322-329. PMID 16666757.
- ↑ Burnet, M., Lafontaine, P.J. and Hanson, A.D. (1995). „Assay, purification, and partial characterization of choline monooxygenase from spinach”. Plant Physiol. 108: 581-588. PMID 12228495.
- ↑ Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. (1997). „Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning”. Proc. Natl. Acad. Sci. USA 94: 3454-3458. PMID 9096415.
- ↑ Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. (1998). „Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth”. Plant Physiol. 116: 859-865. PMID 9489025.
- ↑ Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. (1998). „Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply”. Plant J. 16: 101-110.
- ↑ Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. (1998). „The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline”. Plant J. 16: 487-496. PMID 9881168.
- ↑ 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.
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.