Computational analysis for small subunit of RuBisCo in cyanobacteria Meenakshi S.1, Srisudha S. Research Centre, Botany and Microbiology, Lady Doak College, Madurai, Tamilnadu, India 1Corresponding author
Online published on 31 January, 2014. Abstract The key enzyme of the CBB pathway is ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCo). RuBisCo-based CO2 fixation occurs in all cyanobacteria. The availability of internet based tools and servers provide an excellent opportunity to characterize the physicochemical properties of Cyanobacterial RuBisCo as well as their primary, secondary and threedimensional structural properties. The aim of the study was to determine the physicochemical charecteristics of cyanobacterial RuBisCo and to develop the 3D models of selected cyanobacterial RuBisCo. Molecular weight, isoelectric point, aliphatic index, instability, number of residues, GrandAverage Hydropathicity (GRAVY) and disulfide bond were computed. Secondary structure of α-helix and β-sheet of cyanobacterial small subunit of RuBisCo has more predicted value than plant small subunit of RuBisCo. Putative phosphorylation sites also have high range from 69%-96%. The small subunit of RuBisCo can act as an inducer to large subunit but it doesn't have any function separately. These organisms are homologues and may provide useful information in the study of small-subunit function. Top Keywords Ribulose-1, 5-bisphosphate carboxylase/oxygenase, photosynthetic efficiency, computational analysis, Small subunit. Top |