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
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