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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Available from: Michael E Salvucci, Aug 01, 2015
    • "Plasmids p35S-RbcS-GFP and p35S-RbcS-FLAG were constructed and subsequently used to co-transform rice leaf sheath protoplasts. A RuBisCO complex contains 8 RbcS in vivo (Spreitzer and Salvucci 2002), thus the RbcS-GFP and RbcS-FLAG could interacts in a cotransformed protoplast. The extracts of co-transformed protoplasts , p35S-RbcS-FLAG-transformed protoplasts and untransformed protoplasts were subjected to co-IP assay using anti-GFP antibody, western blot analysis was then performed using anti-FLAG antibody. "
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    • "gene product (573, 595, 599), mitochondrial ATPase (648, 673) and V/A-type ATP synthase (spot 871, 419), which have a central role in oxidative phosphorylation and photosynthesis, significantly decreased under 5 days Cd stress (Table 2 and Fig. 7). As one of the most important enzymes involved in the energy metabolism of all photosynthetic organisms, RuBisCO catalyzes the first step in net photosynthetic CO 2 assimilation and photorespiratory carbon oxidation (Spreitzer and Salvucci, 2002). Previous studies have shown that the amount of RuBisCO large and small subunits was drastically reduced and became fragmented under 250 ␮M Cd treatment of rice leaves (Hajduch et al., 2001). "
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    • "The regeneration of the Rubisco substrate RuBP in the Calvin- Benson-Bassham (CBB) cycle ensures that ample RuBP is available for carbon fixation (Bassham, 1964; Wood, 1966; Beck and Hopf, 1982). Rubisco is a bifunctional enzyme that catalyzes not only RuBP carboxylation but also RuBP oxygenation (Spreitzer and Salvucci, 2002). "
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