• 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
  • Pages
    17
  • From page
    275
  • To page
    291
  • 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
  • Serial Year
    2008
  • Journal title
    Plant Physiology and Biochemistry
  • Record number

    2121817