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 O-2. 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. (c) 2008 Elsevier Masson SAS. All rights reserved.

Keywords

Rubisco; structure-function studies; CO2/O-2 specificity; evolution; structure-based alignment

Published in

Plant Physiology and Biochemistry
2008, Volume: 46, number: 3, pages: 275-291
Publisher: Elsevier

SLU Authors

• Andersson, Inger

  • Department of Molecular Biology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Environmental Sciences related to Agriculture and Land-use
Forest Science


Publication identifier

DOI: https://doi.org/10.1016/j.plaphy.2008.01.001

Permanent link to this page (URI)

https://res.slu.se/id/publ/31349