Evidence for a geranyl-diphosphate synthase located within the plastids of Vitis vinifera L. cultivated in vitro
Identifieur interne : 003997 ( Main/Exploration ); précédent : 003996; suivant : 003998Evidence for a geranyl-diphosphate synthase located within the plastids of Vitis vinifera L. cultivated in vitro
Auteurs : E. Soler [France] ; G. Feron [France] ; M. Clastre [France] ; R. Dargent [France] ; M. Gleizes [France] ; C. Ambid [France]Source :
- Planta [ 0032-0935 ] ; 1992-05-01.
Abstract
Abstract: Intact plastids from cell suspensions of Vitis vinifera L. cv. Muscat de Frontignan, free of detectable contamination by other particles as judged by the distribution of organelle-specific marker enzymes and by electron microscopy, exhibit geranyl-diphosphate synthase activity (EC 2.5.1.1). This synthase activity remains stable after tryptic digestion of unlysed organelles and is enhanced by plastid disruption. We conclude that the enzyme is located within the organelle. The possibility of an isopentenyl diphosphate/dimethylallyl diphosphate translocating system which would play a major role in the regulation of monoterpene metabolism is discussed.
Url:
DOI: 10.1007/BF00201934
Affiliations:
- France
- Aquitaine, Midi-Pyrénées, Nouvelle-Aquitaine, Occitanie (région administrative)
- Talence Cédex, Toulouse Cédex
- Université Toulouse III - Paul Sabatier
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000885
- to stream Istex, to step Curation: 000885
- to stream Istex, to step Checkpoint: 001154
- to stream Main, to step Merge: 003D05
- to stream Main, to step Curation: 003997
Le document en format XML
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<front><div type="abstract" xml:lang="en">Abstract: Intact plastids from cell suspensions of Vitis vinifera L. cv. Muscat de Frontignan, free of detectable contamination by other particles as judged by the distribution of organelle-specific marker enzymes and by electron microscopy, exhibit geranyl-diphosphate synthase activity (EC 2.5.1.1). This synthase activity remains stable after tryptic digestion of unlysed organelles and is enhanced by plastid disruption. We conclude that the enzyme is located within the organelle. The possibility of an isopentenyl diphosphate/dimethylallyl diphosphate translocating system which would play a major role in the regulation of monoterpene metabolism is discussed.</div>
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