TY - JOUR
AU - Harpel, M R
AB -  The importance of D-ribulose-1 ,5-bisphosphate carboxylase/oxygenase (Ru­ bisco, EC 4. 1 . 1 . 39) would be difficult to exaggerate, because it provides the only quantitatively significant link between the pools of inorganic and organic carbon in the biosphere. As catalyst for the net biosynthesis of carbohydrates from atmospheric carbon dioxide, Rubisco enables plants to meet their total life-sustaining requirements for organic carbon; photosyn­ thetic organisms (whether living now or in the past), in tum, provide food, oxygen, and energy for the animal kingdom. Apart from the aura associated with the realization that life is underpinned by a single catalyst, Rubisco has attracted enormous attention for a variety of specific reasons: (a) The enzyme is schizophrenic, catalyzing the oxidative degradation of D-ribulose- 1 ,5-bisphosphate (RuBP) in competition with the biosynthetic carboxylation of RuBP, and is inherently inefficient (low turnover number) as well. These constraints dictate CO2 fixation as the rate-limiting step in the overall photosynthetic assimilation of carbon. Such considerations invite questions of whether Rubisco can be redesigned to increase its kcat or to improve its specificity for CO2 or both. If yes, would a plant transformed with the gene encoding the redesigned enzyme exhibit superior growth and 
TI - Structure, Function, Regulation, and Assembly of D-Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase
JF - Annual Review of Biochemistry
DO - 10.1146/annurev.bi.63.070194.001213
DA - 1994-07-01
UR - https://www.deepdyve.com/lp/annual-reviews/structure-function-regulation-and-assembly-of-d-ribulose-1-5-OaL4UwZLIW
SP - 197
EP - 232
VL - 63
IS - 1
DP - DeepDyve
ER -