Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SCHUCH, R; BRUMMEL, M; SPENER, F.
MEDIUM-CHAIN ACYL-ACP THIOESTERASE IS NOT THE EXCLUSIVE ENZYME RESPONSIBLE FOR EARLY CHAIN-LENGTH TERMINATION IN MEDIUM-CHAIN FATTY-ACID SYNTHESIS
GRASAS ACEITES. 1993; 44(2): 126-128.
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- Co-Autor*innen der Med Uni Graz
- Spener Friedrich
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- Abstract:
- With the aim to elucidate the regulating mechanisms involved in the biosynthesis of medium-chain fatty acids we investigated the substrate specificity of the beta-ketoacyl-ACP synthases (KAS) in extracts obtained from developing seeds of Cuphea lanceolata, a crop producing up to 90% decanoic acid in seed triacylglycerols. Reactions of beta-ketoacyl-ACP synthases were carried out in absence and presence of cerulenin (100 muM) and started by addition of a primer, either acetyl-CoA or acyl-ACPs of chain-lengths varying from C2 to C16. The elongation was monitored by the criterion of incorporation of radioactively labelled malonate from [2-C-14]malonyl-CoA into acyl-ACPs. The reaction products were separated by 2.5 M urea-PAGE, electroblotted onto a PVDF-membrane and visualised by autoradiography. The elongation of each primer was quantitatively evaluated by densitometrically scanning of the autoradiograms. The results show that KAS III of C. lanceolata has a high preference for acetyl-CoA, but can, though in small amounts, catalyse elongation reactions of acyl-ACPs up to C6. Experiments in absence of cerulenin show that in C. lanceolata seed extracts beta-ketoacyl-ACP synthases as a whole hardly elongate C10-ACP, a special feature that can be attributed to a low specificity of KAS I for this substrate.
- Find related publications in this database (Keywords)
- CONDENSING ENZYMES
- CUPHEA
- CUPHEA-LANCEOLATA
- BETA-KETOACYL-ACP SYNTHASES