Dugolančana 3-oksoacil-KoA sintaza
Изглед
Dugolančana 3-oksoacil-KoA sintaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.3.1.199 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | 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, mikrozomalnog proteinskog kompleksa odgovornog za produžavanje palmitoil-KoA i stearoil-KoA u acil sa veoma dugačkim lancima.
Reference[уреди | уреди извор]
- ^ Toke, D.A. & 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. & 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. & Jaworski, J.G. (2006). „Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases”. Biochem. Biophys. Res. Commun. 346: 583—590. PMID 16765910.
- ^ Denic, V. & 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[уреди | уреди извор]
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze[уреди | уреди извор]
- Very-long-chain+3-oxoacyl-CoA+synthase на US National Library of Medicine Medical Subject Headings (MeSH)