Heterologous hybridization of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) restores the enzyme activities.
The catalytic core (A8) and small subunit (B) of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) were isolated from two species of cyanobacteria (Aphanothece halophytica and Synechococcus ACMM 323) as well as from the photosynthetic purple sulfur bacterium, Chromatium vinosum. The subunit B is essential for the activity of all three enzymes. The heterologous hybridization of RuBisCO molecules from the three organisms was attempted and the reconstitution of the catalytically active hybrid was achieved between A8 derived from either Aphanothece or Synechococcus and subunit B from Aphanothece, Synechococcus or Chromatium. However, reconstitution of the enzymically active hybrid between A8 from Chromatium and B subunits from the cyanobacteria could not be achieved. Experiments by using high performance liquid column chromatography also showed the formation of a heterologous hybrid possessing RuBP carboxylase activity.
D002384:Catalysis; D002844:Chromatium / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000201:enzymology; D010105:Oxygenases / Q000378:metabolism*; D055503:Protein Multimerization; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*
D010105:Oxygenases; D012273:Ribulose-Bisphosphate Carboxylase