Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 74:791-794 (1984)
© 1984 American Society of Plant Biologists

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Articles

Variations in the Specific Activity of Ribulose-1,5-bisphosphate Carboxylase between Species Utilizing Differing Photosynthetic Pathways 1

Jeffrey R. Seemann2, Murray R. Badger and Joseph A. Berry

Department of Environmental Biology, Research School of Biological Sciences, Australian National University, Box 475, Canberra 2601 Australia, Department of Plant Biology, Carnegie Institution of Washington, Stanford, California 94305

The in vitro specific activity of ribulose-1,5-bisphosphate carboxylase (RuBPCase) (micromoles CO2 fixed per minute per milligram enzyme) from a number of C3 and C4 species and one green alga were measured. RuBPCases from species which utilize the C4 pathway have a specific activity ~2-fold higher than those from C3 species. RuBPCase from Chlamydomonas reinhardtii has a specific activity similar to the C4 enzyme. Higher specific activity forms of RuBPCase are associated with a decreased enzyme affinity for CO2 (increased Km[CO2]). A small but significant difference in the specific activity of RuBPCase from two C4 decarboxylation types was also observed. The relationship between enzymic properties and the presence or absence of a CO2 concentrating mechanism is discussed.

2 Present address: Department of Plant Biology, Carnegie Institution of Washington, 290 Panama St., Stanford, CA 94305.

1 CIW Publication No. 843.




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