The light activation of fructose-l,6bisphosphatase (EC 3.1.3.11) and sedoheptulose-1,7-bisphosphatase (EC 3.1.3.37) was inhibited in isolated intact spinach (Spinacia oleracea L.) chloroplasts exposed to reduced osmotic potentials. Decreases in the velocity and magnitude of light activation correlat
Control of CO2 fixation. Changes in the activity of ribulosephosphate kinase and fructose- and sedoheptulose-bisphosphatase in chloroplasts
β Scribed by William A. Laing; Mark Stitt; Hans W. Heldt
- Book ID
- 115717812
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 877 KB
- Volume
- 637
- Category
- Article
- ISSN
- 0005-2728
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Using partially purified sedoheptulose-l,7bisphosphatase from spinach (Spinacia oleracea L.) chloroplasts the effects of metabolites on the dithiothreitoland Mg 2 +-activated enzyme were investigated. A screening of most of the intermediates of the Calvin cycle and the photorespiratory pathway showe
The effect of pH and of Mg(2+) concentration on the light activated form of stromal fructose-1,6-bisphosphatase (FBPase) was studied using the enzyme rapidly extracted from illuminated spinach chloroplasts. The (fructose-1,6-bisphosphate(4-))(Mg(2+)) complex has been identified as the substrate of t