Dugolančana 3-oksoacil-CoA sintaza

Dugolančana 3-oksoacil-CoA sintaza
Identifikatori
EC broj	2.3.1.199
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA unos
ExPASy	NiceZyme pregled
KEGG	KEGG unos
MetaCyc	metabolički put
PRIAM	profil
PDB strukture	RCSB PDB PDBj PDBe PDBsum
Pretraga PMC članci PubMed članci NCBI proteini

Dugolančana 3-oksoacil-CoA sintaza (EC 2.3.1.199, sintaza 3-ketoacil-KoA veoma dugog lanca, sintaza beta-ketoacil-KoA veoma dugog lanca, kondenzacijskii enzim, kodirana genima CUT1 CER6, FAE, KCS, ELO) je enzim sa sistematskim imenom malonil-KoA:dugolančana acil-KoA maloniltransferaza (dekarboksilacija i tioestarska-hidroliza)^{[1][2][3][4][5][6][7]} Ovaj enzim katalizira sljedeću hemijsku reakciju

acil-KoA veoma dugačkog lanca + malonil-CoA ${\displaystyle \rightleftharpoons }$ vrlo dugi lanac 3-oksoacil-CoA + CO₂ + koenzim A

Ovaj enzim je prva komponenta elongaze, mikrosomskog proteinskog kompleksa odgovornog za produžavanje palmitoil-KoA i stearoil-KoA u acil sa veoma dugim lancima.

Reference

1. Oh CS, Toke DA, Mandala S, Martin CE (juli 1997). "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation". The Journal of Biological Chemistry. 272 (28): 17376–84. doi:10.1074/jbc.272.28.17376. PMID 9211877.
2. Dittrich F, Zajonc D, Hühne K, Hoja U, Ekici A, Greiner E, Klein H, Hofmann J, Bessoule JJ, Sperling P, Schweizer E (mart 1998). "Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants". European Journal of Biochemistry. 252 (3): 477–85. doi:10.1046/j.1432-1327.1998.2520477.x. PMID 9546663.
3. Millar AA, Clemens S, Zachgo S, Giblin EM, Taylor DC, Kunst L (maj 1999). "CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme". The Plant Cell. 11 (5): 825–38. doi:10.2307/3870817. PMC 144219. PMID 10330468.
4. Ghanevati M, Jaworski JG (juli 2002). "Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS". European Journal of Biochemistry. 269 (14): 3531–9. doi:10.1046/j.1432-1033.2002.03039.x. PMID 12135493.
5. Blacklock BJ, Jaworski JG (juli 2006). "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases". Biochemical and Biophysical Research Communications. 346 (2): 583–90. doi:10.1016/j.bbrc.2006.05.162. PMID 16765910.
6. Denic V, Weissman JS (august 2007). "A molecular caliper mechanism for determining very long-chain fatty acid length". Cell. 130 (4): 663–77. doi:10.1016/j.cell.2007.06.031. PMID 17719544.
7. Tresch S, Heilmann M, Christiansen N, Looser R, Grossmann K (april 2012). "Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases". Phytochemistry. 76: 162–71. doi:10.1016/j.phytochem.2011.12.023. PMID 22284369.

Vanjski linkovi

• Very-long-chain 3-oxoacyl-CoA synthase na US National Library of Medicine Medical Subject Headings (MeSH)