Title of article :
Structure and function of Rubisco
Author/Authors :
Andersson، نويسنده , , Inger and Backlund، نويسنده , , Anders، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Abstract :
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major enzyme assimilating CO2 into the biosphere. At the same time Rubisco is an extremely inefficient catalyst and its carboxylase activity is compromised by an opposing oxygenase activity involving atmospheric O2. The shortcomings of Rubisco have implications for crop yield, nitrogen and water usage, and for the global carbon cycle. Numerous high-resolution crystal structures of different forms of Rubisco are now available, including structures of mutant enzymes. This review uses the information provided in these structures in a structure-based sequence alignment and discusses Rubisco function in the context of structural variations at all levels – amino acid sequence, fold, tertiary and quaternary structure – with an evolutionary perspective and an emphasis on the structural features of the enzyme that may determine its function as a carboxylase.
Keywords :
structure-function studies , Structure-based alignment , CO2/O2 specificity , Evolution , RUBISCO
Journal title :
Plant Physiology and Biochemistry
Journal title :
Plant Physiology and Biochemistry