Skvalen monooksigenaza
| Skvalen monooksigenaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.14.13.132 | ||||||||
| CAS broj | 9029-62-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Skvalen monooksigenaza (EC 1.14.13.132, skvalenska epoksidaza, skvalen-2,3-epoksidna ciklaza, skvalenska 2,3-oksidociklaza, skvalenska hidroksilaza, skvalenska oksidociklaza, skvalen-2,3-epoksidaza) je enzim sa sistematskim imenom skvalen,NADPH:kiseonik oksidoreduktaza (2,3-epoksidacija).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- skvalen + NADPH + H+ + O2 (3S)-2,3-epoksi-2,3-dihidroskvalen + NADP+ + H2O
Ovaj enzim je flavoprotein (FAD).
Reference
- ↑ Corey, E.J., Russey, W.E. and Ortiz de Montellano, P.R. (1966). „2,3-Oxidosqualene, an intermediate in the biological synthesis of sterols from squalene”. J. Am. Chem. Soc. 88: 4750-4751. PMID 5918046.
- ↑ Tchen, T.T. and Bloch, K. (1957). „On the conversion of squalene to lanosterol in vitro”. J. Biol. Chem. 226: 921-930. PMID 13438881.
- ↑ van Tamelen, E.E., Willett, J.D., Clayton, R.B. and Lord, K.E. (1966). „Enzymic conversion of squalene 2,3-oxide to lanosterol and cholesterol”. J. Am. Chem. Soc. 88: 4752-4754. PMID 5918048.
- ↑ Yamamoto, S. and Bloch, K. (1970). „Studies on squalene epoxidase of rat liver”. J. Biol. Chem. 245: 1670-1674. PMID 5438357.
- ↑ Ono, T. and Bloch, K. (1975). „Solubilization and partial characterization of rat liver squalene epoxidase”. J. Biol. Chem. 250: 1571-1579. PMID 234459.
- ↑ Satoh, T., Horie, M., Watanabe, H., Tsuchiya, Y. and Kamei, T. (1993). „Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae”. Biol. Pharm. Bull. 16: 349-352. PMID 8358382.
- ↑ Chugh, A., Ray, A. and Gupta, J.B. (2003). „Squalene epoxidase as hypocholesterolemic drug target revisited”. Prog. Lipid Res. 42: 37-50. PMID 12467639.
- ↑ He, F., Zhu, Y., He, M. and Zhang, Y. (2008). „Molecular cloning and characterization of the gene encoding squalene epoxidase in Panax notoginseng”. DNA Seq 19: 270-273. PMID 17852349.
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 Squalene+monooxygenase
- 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
