Dugolančana 3-oksoacil-KoA sintaza
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| Dugolančana 3-oksoacil-KoA sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.3.1.199 | ||||||||
| 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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Dugolančana 3-oksoacil-KoA sintaza (EC 2.3.1.199, sintaza 3-ketoacil-KoA veoma dugog lanca, sintaza beta-ketoacil-KoA veoma dugog lanca, kondenzacioni enzim, CUT1 (gen), CER6 (gen), FAE1 (gen), KCS (gen), ELO (gen)) je enzim sa sistematskim imenom malonil-KoA:dugolančana acil-KoA maloniltransferaza (dekarboksilacija i tioestarska-hidroliza).[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- acil-KoA veoma dugačkog lanca + malonil-KoA 3-oksoacil-KoA veoma dugačkog lanca + CO2 + koenzim A
Ovaj enzim je prva komponenta elongaze, mikrozomskog proteinskog kompleksa odgovornog za produžavanje palmitoil-KoA i stearoil-KoA u acil sa veoma dugačkim lancima.
Reference[uredi | uredi kod]
- ↑ Toke, D.A. and Martin, C.E. (1996). „Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae”. J. Biol. Chem. 271: 18413-18422. PMID 8702485.
- ↑ Oh, C.S., Toke, D.A., Mandala, S. and Martin, C.E. (1997). „ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation”. J. Biol. Chem. 272: 17376-17384. PMID 9211877.
- ↑ Dittrich, F., Zajonc, D., Huhne, K., Hoja, U., Ekici, A., Greiner, E., Klein, H., Hofmann, J., Bessoule, J.J., Sperling, P. and Schweizer, E. (1998). „Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants”. Eur. J. Biochem. 252: 477-485. PMID 9546663.
- ↑ Millar, A.A., Clemens, S., Zachgo, S., Giblin, E.M., Taylor, D.C. and Kunst, L. (1999). „CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme”. Plant Cell 11: 825-838. PMID 10330468.
- ↑ Ghanevati, M. and Jaworski, J.G. (2002). „Engineering and mechanistic studies of the Arabidopsis FAE1 β-ketoacyl-CoA synthase, FAE1 KCS”. Eur. J. Biochem. 269: 3531-3539. PMID 12135493.
- ↑ Blacklock, B.J. and Jaworski, J.G. (2006). „Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases”. Biochem. Biophys. Res. Commun. 346: 583-590. PMID 16765910.
- ↑ Denic, V. and Weissman, J.S. (2007). „A molecular caliper mechanism for determining very long-chain fatty acid length”. Cell 130: 663-677. PMID 17719544.
- ↑ Tresch, S., Heilmann, M., Christiansen, N., Looser, R. and Grossmann, K. (2012). „Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases”. Phytochemistry 76: 162-171. PMID 22284369.
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.