Abstract
It has been proposed that light regulates the activity of RuBP carboxylase by two mechanisms. One is through Activase which has been shown to control the level of carbamylation of enzyme thus controlling the level of activation (1). The other mechanism involves binding of a phosphorylated inhibitor viz 2-carboxy-arabinitol 1-phosphate to the activated form of enzyme at low light intensities and in the dark. Thus after binding with this inhibitor, RuBP carboxylase remains in activated form but is unable to perform catalytic function (2,3,4). This inhibitor along with activase has been shown to match the activity of RuBP carboxylase with RuBP regenerating capacity in vivo (5).
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Abbreviations
- CA1P:
-
2-carboxy-D-arabinitol 1-phosphate
- R-5-P:
-
Ribose-5-phosphate
- RuBP:
-
Ribulose-1 5-bisphosphate
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© 1990 Springer Science+Business Media New York
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Sainis, J.K., Jawali, N. (1990). Reactivation of Dark-Inactivated RuBP Carboxylase from Phaseolus vulgaris in vitro . In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_529
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DOI: https://doi.org/10.1007/978-94-009-0511-5_529
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6716-4
Online ISBN: 978-94-009-0511-5
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