Eugenol sintaza
(Preusmjereno sa stranice LtCES1)
Eugenol sintaza (EC 1.1.1.318, LtCES1, EGS1, EGS2) je enzim sa sistematskim imenom eugenol:NADP+ oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
Eugenol sintaza | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 1.1.1.318 | ||||||||
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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- eugenol + a karboksilat + NADP+ koniferil ester + NADPH + H+
Ovaj enzim deluje u suprotnom smeru. Enzimi iz biljki Ocimum basilicum (bosiljak), Clarkia breweri i Petunia hybrida jedino deluju na koniferil acetat i formiraju eugenol. Enzim iz Pimpinella anisum formira anol (iz 4-cumaril acetata) in vivo, mada rekombinantni enzim može da formira eugenol iz koniferil acetata. Enzim iz Larrea tridentata takođe formira havikol iz cumarilnog estra i može da koristi NADH.
Reference
uredi- ↑ Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. (2006). „Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester”. Proc. Natl. Acad. Sci. USA 103: 10128-10133. PMID 16782809.
- ↑ Vassão, D.G., Kim, S.J., Milhollan, J.K., Eichinger, D., Davin, L.B. and Lewis, N.G. (2007). „A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeugenol”. Arch. Biochem. Biophys. 465: 209-218. PMID 17624297.
- ↑ Louie, G.V., Baiga, T.J., Bowman, M.E., Koeduka, T., Taylor, J.H., Spassova, S.M., Pichersky, E. and Noel, J.P. (2007). „Structure and reaction mechanism of basil eugenol synthase”. PLoS One 2: e993-. PMID 17912370.
- ↑ Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. (2008). „The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages”. Plant J. 54: 362-374. PMID 18208524.
- ↑ Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. (2009). „Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain”. Plant Physiol. 149: 384-394. PMID 18987218.
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.