Rubisco regulation: a role for inhibitors

• Published in: Journal of experimental botany Vol. 59; no. 7; pp. 1569 - 1580
• Main Authors: Parry, Martin A. J., Keys, Alfred J., Madgwick, Pippa J., Carmo-Silva, Ana E., Andralojc, P. John
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.05.2008; Oxford Publishing Limited (England)
• Subjects: Abiotic stress; Active sites; CA1P; Crops, Agricultural - enzymology; Enzyme Induction; Enzymes; Gene expression regulation; inhibitors; Leaves; Photosynthesis; Physiological regulation; Plant biochemistry; Plant physiology; Plants; Protein Binding; Protein isoforms; Ribulose-Bisphosphate Carboxylase - antagonists & inhibitors; Ribulose-Bisphosphate Carboxylase - chemistry; Ribulose-Bisphosphate Carboxylase - genetics; Ribulose-Bisphosphate Carboxylase - metabolism; Rubisco; Rubisco activase; SPECIAL ISSUE REVIEW PAPER; inhibitors; Rubisco; CA1P; Rubisco activase; Abiotic stress
• ISSN: 0022-0957; 1460-2431
• DOI: 10.1093/jxb/ern084

In photosynthesis Rubisco catalyses the assimilation of CO2 by the carboxylation of ribulose-1,5-bisphosphate. However, the catalytic properties of Rubisco are not optimal for current or projected environments and limit the efficiency of photosynthesis. Rubisco activity is highly regulated in response to short-term fluctuations in the environment, although such regulation may not be optimally poised for crop productivity. The regulation of Rubisco activity in higher plants is reviewed here, including the role of Rubisco activase, tight binding inhibitors, and the impact of abiotic stress upon them.