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

Jeffrey R. Seemann | Zendy; Murray R. Badger | Zendy; Joseph A. Berry | Zendy

Open Access

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

Author(s) -

Jeffrey R. Seemann,

Murray R. Badger,

Joseph A. Berry

Publication year - 1984

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.74.4.791

Subject(s) - pyruvate carboxylase , ribulose 1,5 bisphosphate , chlamydomonas reinhardtii , enzyme , biochemistry , rubisco , specific activity , photosynthesis , decarboxylation , chemistry , chlamydomonas , ribulose , carboxy lyases , oxygenase , enzyme assay , biology , catalysis , mutant , gene

The in vitro specific activity of ribulose-1,5-bisphosphate carboxylase (RuBPCase) (micromoles CO(2) fixed per minute per milligram enzyme) from a number of C(3) and C(4) species and one green alga were measured. RuBPCases from species which utilize the C(4) pathway have a specific activity approximately 2-fold higher than those from C(3) species. RuBPCase from Chlamydomonas reinhardtii has a specific activity similar to the C(4) enzyme. Higher specific activity forms of RuBPCase are associated with a decreased enzyme affinity for CO(2) (increased K(m)[CO(2)]). A small but significant difference in the specific activity of RuBPCase from two C(4) decarboxylation types was also observed. The relationship between enzymic properties and the presence or absence of a CO(2) concentrating mechanism is discussed.

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