Title :
In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family
Author :
Subramani, Boopathi ; Hwa, Kuo-Yuan
Author_Institution :
Inst. of Org. & Polymeric Mater., Nat. Taipei Univ. of Technol., Taipei, Taiwan
Abstract :
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in CO2 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 O2. 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 C3 and C4 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 C3 plants to increase the turnover rate for CO2 fixation that can be important for biomass generation.
Keywords :
biochemistry; biology computing; botany; carbon compounds; enzymes; molecular biophysics; reaction kinetics; C3 plants; C4 plants; CO2; Poaceae family; Rubisco activity; biomass production; carboxylase activity; energy production; enzyme; in silico analysis; kinetic properties; oxygenase; oxygenation; phosphorylation sites; ribulose-1,5-bisphosphate carboxylase; sugar phosphate substrate; Amino acids; Materials; Phylogeny; Proteins; Servers; Thermal stability;
Conference_Titel :
Information Technology Convergence and Services (ITCS), 2010 2nd International Conference on
Conference_Location :
Cebu
Print_ISBN :
978-1-4244-7584-1
Electronic_ISBN :
978-1-4244-7584-1
DOI :
10.1109/ITCS.2010.5581267