Author
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PORTIS JR, ARCHIE |
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Submitted to: Journal of Experimental Botany
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 4/11/1995 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: The activity of Rubisco depends on: conversion of the inactive form (E) to the active form (ECM); the binding of the inhibitors CA1P and RuBP to ECM and E respectively; and the catalytic formation of inhibitory sugar bisphosphates from the ene-diol intermediate that precedes carboxylation/oxygenation. The regulatory protein, Rubisco activase, modulates the activity of Rubisco by kinetically increasing the dissociation rate of these sugar bisphosphates from their respective enzyme forms in a process that requires ATP hydrolysis. The activity of Rubisco activase is determined by the ATP/ADP ratio. The activity also appears to be influenced by thylakoid membranes in a light dependent manner, but only a few details of this effect are currently understood. A species dependence in the interaction between heterologous Rubisco and Rubisco activase proteins has been observed. Whether the regulation of Rubisco is a constraint to crop productivity is debatable and will only be decided by detailed study of plants transformed with appropriately modified Rubisco activase and/or Rubisco proteins. |
