Lupeolna sintaza
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Lupeolna sintaza | |||||||||
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Identifikatori | |||||||||
EC broj | 5.4.99.41 | ||||||||
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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Lupeolna sintaza (EC 5.4.99.41, LUPI, BPW, RcLUS) je enzim sa sistematskim imenom (3S)-2,3-epoksi-2,3-dihidroskvalen mutaza (ciklizacija, formira lupeol).[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (3S)-2,3-epoksi-2,3-dihidroskvalen lupeol
Ovaj enzim takođe forms pojedine beta-amirine.
Reference[uredi | uredi kod]
- ↑ Herrera, J.B., Bartel, B., Wilson, W.K. and Matsuda, S.P. (1998). „Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene”. Phytochemistry 49: 1905-1911. PMID 9883589.
- ↑ Shibuya, M., Zhang, H., Endo, A., Shishikura, K., Kushiro, T. and Ebizuka, Y. (1999). „Two branches of the lupeol synthase gene in the molecular evolution of plant oxidosqualene cyclases”. Eur. J. Biochem. 266: 302-307. PMID 10542078.
- ↑ Segura, M.J., Meyer, M.M. and Matsuda, S.P. (2000). „Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene alcohols and a triterpene diol”. Org. Lett. 2: 2257-2259. PMID 10930257.
- ↑ Zhang, H., Shibuya, M., Yokota, S. and Ebizuka, Y. (2003). „Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla var. japonica: molecular evolution of oxidosqualene cyclases in higher plants”. Biol. Pharm. Bull. 26: 642-650. PMID 12736505.
- ↑ Hayashi, H., Huang, P., Takada, S., Obinata, M., Inoue, K., Shibuya, M. and Ebizuka, Y. (2004). „Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra”. Biol. Pharm. Bull. 27: 1086-1092. PMID 15256745.
- ↑ Guhling, O., Hobl, B., Yeats, T. and Jetter, R. (2006). „Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis”. Arch. Biochem. Biophys. 448: 60-72. PMID 16445885.
- ↑ Basyuni, M., Oku, H., Tsujimoto, E., Kinjo, K., Baba, S. and Takara, K. (2007). „Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae”. FEBS J. 274: 5028-5042. PMID 17803686.
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.