Abstract
Ribulose-I, 5-bisphosphate carboxylase/oxygenase (E.4.1.1.39), often referred to as RuBPcase, has been extensively studied both at the structural and at the functional level becasue of its paramount role in the dark fixation of CO2 during photosynthesis. RuBPcase has been purified to electrophoretic homogeneity from a wide variety of plants. It is a multimeric enzyme (MW 550,000) and comprises eight large subunits (MW 55,000) and eight small subunits (MW 12,000-16,000) in higher plants. The carboxylase and oxygenase activities of the enzyme reside in its large subunit, while its small subunit has been assigned a regulatory role in the catalytic activity. The large subunit of RuBPcase is encoded in the chloroplast and translated in situ. The small subunit is encoded in the nucleus and synthesized in the cytoplasm as a precursor polypeptide with a “transit peptide” at the N'-terminus. The transit peptide is responsible for the transport of the small subunit into the chloroplast. The precursor small subunit is processed to maturity in the chloroplast by a stromal enzyme and is then assembled with the large subunit to form the holoenzyme. A high molecular weight binding protein (29 S) is associated with the large subunit and is crucial for the assembly of the large subunits. The transport and assembly of subunits into holoenzyme are energydependent processes.
RuBPcase is regulated at the transcriptional and post-translational level. Transcription of large and small subunit genes are controlled by light and developmentally. The catalytic activity of RuBPcase is modulated by inhibitors and activators. Carbamylation of a lysine residue at the active site results in the activation of the enzyme. RuBPcase activase has been shown to mediate the light-mediated activation of RuBPcase. The substrate RuBP inhibits the activity of decarbaylated RuBPcase in vivo. Carboxy Nicotiana, Panicum, and Solanum. However, this mechanism does not operate in pea, spinach, Cicer, Triticum and Zea mays.
RuBPcase is a phosphoprotein in moss, spinach, pea, and Cicer. In vivo labelling of the enzyme with [32P] has revealed that phosphorylation occurs at the small subunit. The in vitro dephosphorylation of the enzyme with alkaline phosphatase dissociated the small subunit from the large subunit octameric core. Concomitantly, there was a significant decrease in the catalytic activity of RuBPcase. Thus, Phosphorylation seems to be necessary for optimum biological activity of RuBPcase.
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Sachar, R.C., Saluja, D., Murali, P. (1993). Structure, Function and Regulation of Ribulose 1, 5-Bisphosphate Carboxylase in Higher Plants. In: Abrol, Y.P., Mohanty, P., Govindjee (eds) Photosynthesis: Photoreactions to Plant Productivity. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2708-0_11
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