Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic cyanobacterium Thermosynechococcus elongatus

Photosynth Res. 2008 Jan;95(1):101-9. doi: 10.1007/s11120-007-9240-7. Epub 2007 Oct 6.

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) can be divided into two branches: the "red-like type" of marine algae and the "green-like type" of cyanobacteria, green algae, and higher plants. We found that the "green-like type" rubisco from the thermophilic cyanobacterium Thermosynechococcus elongatus has an almost 2-fold higher specificity factor compared with rubiscos of mesophilic cyanobacteria, reaching the values of higher plants, and simultaneously revealing an improvement in enzyme thermostability. The difference in the activation energies at the transition stages between the oxygenase and carboxylase reactions for Thermosynechococcus elongatus rubisco is very close to that of Galdieria partita and significantly higher than that of spinach. This is the first characterization of a "green-like type" rubisco from thermophilic organism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cyanobacteria / enzymology*
  • Cyanobacteria / genetics
  • Enzyme Stability
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Kinetics
  • Ribulose-Bisphosphate Carboxylase / genetics
  • Ribulose-Bisphosphate Carboxylase / isolation & purification
  • Ribulose-Bisphosphate Carboxylase / metabolism*
  • Substrate Specificity
  • Temperature*

Substances

  • Ribulose-Bisphosphate Carboxylase