Activities of soluble and microsomal farnesyl diphosphatases in Datura stramonium

Activities of soluble and microsomal farnesyl diphosphatases in Datura stramonium

The aim of this study was to investigate the activity of farnesyl diphosphatase (FDPase; EC 3.1.7.1) in Datura stramonium. The results show that FDPase is constitutively expressed at a high level in the soluble and the microsomal fractions of Datura stramonium. Soluble and microsomal FDPase have a s...

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Bibliographic Details
Published in:Biologia plantarum Vol. 47; no. 3; pp. 477 - 479
Main Authors: Ha, S.B, Lee, D.E, Lee, H.J, Song, S.J, Back, K. (Chonnam National Univ., Gwangju (South Korea). Dept. of Biotechnology)
Format: Journal Article
Language:English
Published: 01-11-2003
Subjects:
ACTIVIDAD ENZIMÁTICA
ACTIVITÉ ENZYMATIQUE
ATP
DATURA STRAMONIUM
ENZYME ACTIVITY
ESTERASAS
ESTERASES
ESTÉRASE
EXTRACTOS
EXTRACTS
EXTRAIT
FEUILLE
FLEUR
FLORES
FLOWERS
FRUITS
FRUTAS
HOJAS
LEAVES
RACINE
RAÍCES
ROOTS
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Summary:The aim of this study was to investigate the activity of farnesyl diphosphatase (FDPase; EC 3.1.7.1) in Datura stramonium. The results show that FDPase is constitutively expressed at a high level in the soluble and the microsomal fractions of Datura stramonium. Soluble and microsomal FDPase have a similar pH optimum (5.0-6.0) and a similar substrate specificity. Geranyl diphosphate and geranylgeranyl diphosphate compete for FDP, but isopentenyl diphosphate, ATP, and para-nitrophenyl phosphate do not. Soluble FDPase activity was highest in fruit and flower followed by root, and leaf.
Bibliography:F60
2004000268
ISSN:0006-3134
1573-8264
DOI:10.1023/B:BIOP.0000023901.49409.7b