The capacity of plastids from developing pea cotyledons to synthesise acetyl CoA |
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Authors: | Kay Denyer Alison M Smith |
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Institution: | (1) John Innes Institute, Colney Lane, NR4 7UH Norwich, UK |
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Abstract: | In order to determine whether the enzymes required to convert triose phosphate to acetyl CoA were present in pea (Pisum sativum L.) seed plastids, a rapid, mechanical technique was used to isolate plastids from developing cotyledons. The plastids were intact and the extraplastidial contamination was low. The following glycolytic enzymes, though predominantly cytosolic, were found to be present in plastids: glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12), phosphoglycerate kinase (EC 2.7.2.3), and pyruvate kinase(EC 2.7.1.40). Evidence is presented which indicates that plastids also contained low activities of enolase (EC 4.2.1.11) and phosphoglycerate mutase (EC 2.7.5.3). Pyruvate dehydrogenase, although predominantly mitochondrial, was also present in plastids. The plastidial activities of the above enzymes were high enough to account for the rate of lipid synthesis observed in vivo.Abbreviations FPLC
fast protein liquid chromatography
- PPi
pyrophosphate |
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Keywords: | Acetyl CoA Glycolysis (isoenzymes) Pisum (acetyl CoA plastid) Plastid (acetyl CoA) Seed developing |
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