barrel, and its structure was resolved using its transition state analog (*) CABP.
Recent discoveries suggest that a nano anatase-titanium dioxide complex promotes the formation of this enzyme and its activating complex. That activating enzyme belongs to the AAA+ family of proteins and facilitates the removal of d-hamamelonic acid phosphate. The C-terminal domains of its large subunits exhibit a characteristic ?/? barrel, and its structure was resolved using its transition state analog (*) CABP. The epsilon-amino group of its Lys-334 residue co-ordinates with a magnesium ion stabilizes the transition state of its second partial reaction, wherein an ene-diolate reacts with either of its two common substrates. Organisms exhibiting Kranz anatomy use an analogous protein called PEP Carboxylase instead of this protein. For 10 points, identify this enzyme which facilitates the rate determining step of the Calvin cycle.
Recent discoveries suggest that a nano anatase-titanium dioxide complex promotes the formation of this enzyme and its activating complex.
{Rubisco} [or {Ribulose}-{1,5}-{bisphosphate carboxylase/oxygenase}]