In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in CO_2 fixation. It is an important enzyme for biomass production, especially for alternate energy production. Rubisco is an inefficient catalyst. Its carboxylase activity is compromised by numerous side-reactions including oxygenation of the sugar phosphate substrate by atmospheric O_2. However, naturally occurring enzyme variants with different kinetic properties suggest that it is possible to alter the enzyme to be in favor of the carboxylation activity than of the oxygenation. In this study the C_3 and C_4 plants of Poaceae family with variation in Rubisco activity was phylogenetically analyzed. Our analysis focused on the key regulatory mechanisms such as phosphorylation sites of the enzymes and suggests that these phosphorylation sites can be a putative target site to engineer Rubisco in C_3 plants to increase the turnover rate for CO_2 fixation that can be important for biomass generation.