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- W1995880197 abstract "Pyruvate, Pi dikinase, which is localized in the mesophyll chloroplasts of C4 plants, requires a high adenylate energy charge for conversion of the enzyme from the inactive to the active form. The inactivation process is favored by a low energy charge, being maximal at values below 0.7. Pyruvate and analogs of pyruvate, oxamate and oxalate, strongly inhibit the inactivation process at millimolar levels. The results suggest that light activation of the enzyme invivo may be mediated by an increased adenylate energy charge in the chloroplast. Pyruvate may allow a higher steady-state level of activation to be achieved invivo by inhibiting inactivation." @default.
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- W1995880197 date "1983-09-01" @default.
- W1995880197 modified "2023-09-27" @default.
- W1995880197 title "Control of the activation/inactivation of pyruvate, Pi dikinase from the C4 plant maize by adenylate energy charge, pyruvate, and analogs of pyruvate" @default.
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- W1995880197 doi "https://doi.org/10.1016/s0006-291x(83)80197-1" @default.
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