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- W2028397816 endingPage "1933" @default.
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- W2028397816 abstract "The activity of phosphoenolpyruvate carboxylase in leaf extracts of C 4 plants has been shown to be inhibited by the C 4 acids malate and aspartate. The magnitude of inhibition observed with phosphoenolpyruvate carboxylase from Digitaria sanguinalis leaves was dependent on the pH of the assay mixture and the concentration of phosphoenolpyruvate (PEP), Mg 2+ . and the C 4 acid inhibitor. The percentage inhibition decreased with increasing pH up to 8.5. At rate-limiting concentrations of phosphoenolpyruvate the pH optimum of the enzyme was 7.8, whereas the enzyme partially inhibited by malate or aspartate had a pH optimum of roughly 8.3. Malate and aspartate inhibited the enzyme by increasing the apparent K m for phosphoenolpyruvate without altering the maximum velocity, such that inhibition was greatest at rate-limiting concentrations of PEP but was not observed at saturating (3 mM) substrate levels. Glucose-6-P. an activator of PEP carboxylase, decreased the apparent K m for PEP and reversed the inhibition by malate and aspartate. Inhibition was also dependent on the concentration of Mg 2+ . At 1 mM Mg 2+ , 1 mM malate caused 60% inhibition, but at 5 mM Mg 2+ the inhibition was reduced to 15%. Mg 2+ at concentrations from 1 to 5 mM had no effect on the apparent K m for PEP. With Sephadex extracts of PEP carboxylase from leaves of D. sanguinalis, malate and aspartate were equally inhibitory, with roughly 2 mM levels required for 50% inhibition. Both malate and aspartate were inhibitory with PEP carboxylase extracted from leaves of a variety of C 4∙ but not C 3∙ plants. The significance of the observed inhibition and activation of PEP carboxylase by metabolites is discussed in relation to C 4 photosynthesis." @default.
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- W2028397816 date "1975-09-01" @default.
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- W2028397816 title "Inhibition of phosphoenolpyruvate carboxylase from C<sub>4</sub> plants by malate and aspartate" @default.
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- W2028397816 doi "https://doi.org/10.1139/b75-216" @default.
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