Dugolančana 3-oksoacil-KoA sintaza

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
Pretraga PMC articles PubMed articles NCBI Protein search

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 ${\displaystyle \rightleftharpoons }$ 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

1. 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. 
2. 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. 
3. 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. 
4. 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. 
5. 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. 
6. 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. 
7. 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. 
8. 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

• 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. 

Vanjske veze

• MeSH Very-long-chain+3-oxoacyl-CoA+synthase