Structural Studies of Ribulose-1, 5-Bisphosphate Carboxylase/Oxygenase from Spinach
Ribulose-1, 5-bisphosphate carboxylase/oxygenase, Rubisco, plays an important role in photosynthesis as well as in photorespiration. In photosynthesis, the carboxylase activity of the enzyme catalyzes the condensation of carbon dioxide and ribulose-1, 5-bisphosphate to yield two moles of 3-D-phosphoglycerate (Miziorko and Lorimer, 1983; Andrews and Lorimer, 1987). In addition, Rubisco has an oxygenase activity whereby oxygen is added to ribulose 1, 5-bisphosphate to yield 3-D-phosphoglycerate and 2-phosphoglycolate, the major substrate for photorespiration. As a result of the subsequent metabolism of phosphoglycolate one of the carbon atoms is oxidized to carbon dioxide and the released energy is lost as heat. Up to 50% of the photosynthetically reduced carbon may be oxidized through this pathway. The possibility to increase the carboxylase/oxygenase ratio has therefore attracted substantial interest. An understanding of the structural basis for the two activities would greatly facilitate the successful use of site directed mutagenesis techniques towards this end.
KeywordsAlpha Helix Metal Binding Site Triose Phosphate Isomerase Beta Strand Glycolate Oxidase
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