Biophysical analysis of the structural evolution of substrate specificity in RuBisCO.

ABSTRACT: Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the most abundant enzyme on Earth. However, its catalytic rate per molecule of protein is extremely slow and the binding of the primary substrate, CO₂, is competitively displaced by O_2. Hence, carbon fixation by RuBisCO is highly inefficient; indeed, in higher C3 plants, about 30% of the time the enzyme mistakes CO₂ for O₂ Using genomic and structural analysis, we identify regions around the catalytic site that play key roles in discriminating between CO₂ and O₂ Our analysis identified positively charged cavities directly around the active site, which are expanded as the enzyme evolved with higher substrate specificity. The residues that extend these cavities have

SUBMITTER: Poudel S 

PROVIDER: S-EPMC7720200 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature