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Enhanced CO2/O2 specificity of a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase.
The CO2/O2 specificity factor of ribulose-bisphosphate carboxylase/oxygenase partially determines the efficiency of photosynthetic carbon assimilation. Heretofore, engineered alterations of the enzyme have only decreased the selectivity for CO2 utilization. We show that alanyl replacement of active-site Ser-368 of the Rhodospirillum rubrum carboxylase enhances the carboxylation selectivity approximately 1.6-fold over the wild-type level. This enhancement reflects a greater relative decline in oxygenase efficiency than in carboxylase efficiency. In contrast to wild-type enzyme, the carboxylase activity of the Ser-368 mutant protein is not perceptibly inhibited by O2, perhaps indicative of a change in rate-limiting steps in the overall reaction pathway.
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