Engineering Rubisco to change its catalytic properties

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Abstract
The initial steps of carbon assimilation and photorespiration are catalysed by ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39). Natural variation in the kinetic properties of the enzyme suggest that it is possible to alter the enzyme to favour the carboxylation activity relative to oxygenation. Mutagenesis in vitro of the gene encoding the large subunit of the enzyme from Anacystis nidulans has been used to modify catalytic properties. Residues at the C-terminal end of loop 6 of the β/α barrel structure of the large subunit influence specificity towards the gaseous substrates, CO2 and O2. None of the residues altered by mutagenesis appear to interact directly with the transition state analogue and their effect on the reaction of the enediolate intermediate with the gaseous substrates and stabilization of the resulting transition state intermediates by lysine 334 must be indirect. Interactions with other parts of the enzyme must also be important in determining substrate specificity. Backbone carbonyl groups close to lysine 334 interact with lysine 128; mutation of lysine 128 to residues of less positive polarity reduces enzyme activity and favours oxygenation relative to carboxylation. The likely effects on assimilation rates of altering the kinetic properties of Rubisco have been modelled. A leaf with cyanobacterial Rubisco may out-perform a higher plant Rubisco at elevated CO2 and cool temperatures.

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