Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.

Department of Biochemistry, Institute of Agriculture and Natural Resources, University of Nebraska, Lincoln, Nebraska 68588-0664, USA.
Annual review of plant biology (Impact Factor: 18.9). 02/2002; 53:449-75. DOI: 10.1146/annurev.arplant.53.100301.135233
Source: PubMed

ABSTRACT Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes the first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation. The enzyme is notoriously inefficient as a catalyst for the carboxylation of RuBP and is subject to competitive inhibition by O2, inactivation by loss of carbamylation, and dead-end inhibition by RuBP. These inadequacies make Rubisco rate limiting for photosynthesis and an obvious target for increasing agricultural productivity. Resolution of X-ray crystal structures and detailed analysis of divergent, mutant, and hybrid enzymes have increased our insight into the structure/function relationships of Rubisco. The interactions and associations relatively far from the Rubisco active site, including regulatory interactions with Rubisco activase, may present new approaches and strategies for understanding and ultimately improving this complex enzyme.

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