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Regulation of Sedoheptulose-1,7-bisphosphatase by Sedoheptulose-7-phosphate and Glycerate, and of Fructose-1,6-bisphosphatase by Glycerate in Spinach Chloroplasts by Dieter Schimkat; Dieter Heineke; Hans W. Heldt is a Agricultural and Biological Sciences article available to read on EtoBox.

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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 showed that physiological concentrations of sedoheptulose-7-phosphate and glycerate specifically inhibited the enzyme by decreasing its maximal velocity. An inhibition by ribulose-l,5-bisphosphate was also found. The inhibitory effect of sedoheptulose-7-phosphate on the enzyme is discussed in terms of allowing a control of sedoheptulose-l,7-bisphosphate hydrolysis by the demand of the product of this reaction. Subsequent studies with partially purified fructose-l,6-bisphosphatase from spinach chloroplasts showed that glycerate also inhibited this enzyme. With isolated chloroplasts, glycerate was found to inhibit CO2 fixation by blocking the stromal fructose-l,6-bisphosphatase. It is therefore possible that the inhibition of the two phosphatases by glycerate is an important regulatory factor for adjusting the activity of the Calvin cycle to the ATP supply by the light reaction.

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Author

Dieter Schimkat; Dieter Heineke; Hans W. Heldt

Publisher

Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc. (ISSN 0032-0935)

Published

1990

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)