Regulation of the activation of chloroplast fructose-1,6-bisphosphatase: Inhibition by spermidine and spermine
The activation of chloroplast fructose-1,6-bisphosphatase by fructose-1,6-bisphosphate, Ca2+, DTT and chloroplast thioredoxin-f is prevented by either spermidine or spermine; on the contrary, other amino compounds do not replace polyamines in this reversible effect. On the other hand, neither spermi...
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| Autores principales: | , , |
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| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0006291X_v115_n2_p707_Corley |
| Aporte de: |
| Sumario: | The activation of chloroplast fructose-1,6-bisphosphatase by fructose-1,6-bisphosphate, Ca2+, DTT and chloroplast thioredoxin-f is prevented by either spermidine or spermine; on the contrary, other amino compounds do not replace polyamines in this reversible effect. On the other hand, neither spermidine nor spermine modify the catalysis of chloroplast fructose-1,6-bisphosphatase. The effect of spermidine, but not the effect of spermine, is reversed by increasing the concentration of Ca2+ in the activation; higher concentrations of fructose-1,6-bisphosphate or thioredoxin-f do not restore the control activity. The present results suggest that other regulatory mechanisms may control the activation of fructose-1,6-bisphosphatase in chloroplasts. © 1983 Academic Press, Inc. |
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