Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
BRUCK, FM; SCHUCH, R; SPENER, F.
MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE FROM DEVELOPING SEEDS OF CUPHEA-LANCEOLATA
J PLANT PHYSIOL. JOURNAL OF PLANT PHYSIOLOGY; 143: 550-555.
Doi: 10.1016/S0176-1617(11)81822-5
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- Co-Autor*innen der Med Uni Graz
- Spener Friedrich
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- Abstract:
- Malonyl-CoA:acyl carrier protein (ACP) transacylase (MAT; E.C. 2.3.1.39.) was partially purified from developing seeds of Cuphea lanceolata, a crop accumulating up to 90 % decanoic acid in storage triacylglycerols. Upon treatment of a cell-free seed extract with ammonium sulfate, most of the enzyme activity was precipitated between 40 - 75 % ammonium sulfate saturation. Further purification was accomplished in 4 steps that included gel filtration on Sephacryl S 200 HR, anion exchange chromatography on Mono Q (0.0 to 0.2 M LiBr gradient), rechromatography on Mono Q (0.00 to 0.12M LiBr gradient) and gel filtration on Sephacryl S 100 HR. The MAT-preparation obtained after anion exchange chromatography was free from any beta-ketoacyl-ACP synthase (KAS; E.C. 2.3.1.41.) activity and could be used in the synthesis of malonyl-ACP to study medium-chain fatty acid biosynthesis. The molecular mass of the MAT was 27.5 kDa based on gel filtration and 23.5 kDa based on Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The N-aminoterminal sequence of this enzyme (VAVAELQVE-FI; -, not determined), for the first time determined for a MAT from a higher plant, showed a 25 % homology to the enzyme from Escherichia coli.
- Find related publications in this database (Keywords)
- CUPHEA LANCEOLATA
- AMINO ACID SEQUENCE
- FATTY ACID SYNTHASE
- MALONYL-COA, ACP TRANSACYLASE
- SEED