An unusual L2 dimeric form of this enzyme was found in Rhodospirillum rubrum.
An unusual L2 dimeric form of this enzyme was found in Rhodospirillum rubrum. Magnesium ions facilitate the formation of a carbamate about a lysine residue at the active site of this protein. This protein typically consists of eight L and S subunits, and is very prevalent in the pyrenoids of algae. Its namesake activase removes the inhibitor CA1P. This enzyme catalyzes the carboxylation of a five carbon compound, producing two molecules of 3- phosphoglycerate. In the stroma of the chloroplast, this enzyme catalyzes photorespiration when there isn't enough carbon dioxide to fix. For 10 points, name this protein that catalyzes the first step of the Calvin Cycle, the most abundant enzyme on Earth.
An unusual L2 dimeric form of this enzyme was found in Rhodospirillum rubrum.
RuBisCO [or ribulose-1,5-bisphosphate carboxylase oxygenase]