Sammanfattning

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.

Nyckelord

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

Publicerad i

Plant Physiology and Biochemistry
2008, Volym: 46, nummer: 3, sidor: 275-291
Utgivare: Elsevier

SLU författare

• Andersson, Inger

  • Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Miljö- och naturvårdsvetenskap
Skogsvetenskap


Publikationens identifierare

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

Permanent länk till denna sida (URI)

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