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Selected Publication:
DORMANN, P; SPENER, F; OHLROGGE, JB.
CHARACTERIZATION OF 2 ACYL-ACYL CARRIER PROTEIN THIOESTERASES FROM DEVELOPING CUPHEA SEEDS SPECIFIC FOR MEDIUM-CHAIN-ACYL AND OLEOYL-ACYL CARRIER PROTEIN
PLANTA. 1993; 189(3): 425-432.
Doi: 10.1007/BF00194441
Web of Science
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- Co-authors Med Uni Graz
- Spener Friedrich
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- Abstract:
- Two acyl-acyl carrier protein (ACP) thioesterases were partially purified from developing seeds of Cuphea lanceolata Ait., a plant with decanoic acid-rich triacylglycerols. The two enzymes differ markedly in their substrate specificity. One is specific for medium-chain acyl-ACPs, the other one for oleoyl-ACP. In addition, these enzymes are distinct with regard to molecular weight, pH optimum and sensitivity to salt. The thioesterases could be separated by Mono Q chromatography or gel filtration. The medium-chain acyl-ACP thioesterase and oleoyl-ACP thioesterase were purified from a crude extract 29- and 180-fold, respectively. In Cuphea wrightii A. Gray, which predominantly contains decanoic and lauric acid in the seeds, two different thioesterases were also found with a similar substrate specificity as in Cuphea lanceolata.
- Find related publications in this database (Keywords)
- ACYL CARRIER PROTEIN
- CUPHEA
- FATTY ACID
- MEDIUM-CHAIN
- HYDROLASE
- THIOESTERASE