Journal Article

Distribution of Fallover in the Carboxylase Reaction and Fallover-Inducible Sites among Ribulose 1,5-Bisphosphate Carboxylase/Oxygenases of Photosynthetic Organisms

Koichi Uemura, Hiroshi Tokai, Takashi Higuchi, Hiroshi Murayama, Hiroshi Yamamoto, Yukito Enomoto, Shoko Fujiwara, Jin Hamada and Akiho Yokota

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 2, pages 212-219
Published in print February 1998 | ISSN: 0032-0781
Published online February 1998 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029359
Distribution of Fallover in the Carboxylase Reaction and Fallover-Inducible Sites among Ribulose 1,5-Bisphosphate Carboxylase/Oxygenases of Photosynthetic Organisms

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The biphasic reaction course, fallover, of carboxyla-tion catalysed by ribulose 1,5-bisphosphate carboxylase/ox-ygenase (RuBisCO) has been known as a characteristic of the enzyme from higher land plants. Fallover consists of hysteresis in the reaction seen during the initial several minutes and a very slow suicide inhibition by inhibitors formed from the substrate ribulose-l,5-bisphosphate (RuBP). This study examined the relationship between occurrence of fallover and non-catalytic RuBP-binding sites, and the putative hysteresis-inducible sites (Lys-21 and Lys-30S of the large subunit in spinach RuBisCO) amongst RuBisCOs of a wide variety of photosynthetic organisms. Fallover could be detected by following the course of the carboxylase reaction at 1 mM RuBP and the non-catalytic binding sites by alleviation of fallover at 5 mM RuBP. RuBisCO from Euglena gracilis showed the same linear reaction course at both RuBP concentrations, indicating an association between an absence of fallover and an absence of the non-catalytic binding sites. This was supported by the results of an equilibrium binding assay for this enzyme with a transition state analogue. Green macroalgae and non-green algae contained the plant-type, fallover enzyme. RuBisCOs from Conjugatae, Closterium ehrenbergii, Gona-tozygon monotaenium and Netrium digitus, showed a much smaller decrease in activity at 1 mM RuBP than the spinach enzyme and the reaction courses of these enzymes at 5 mM RuBP were almost linear. RuBisCO of a primitive type Conjugatae, Mesotaenium caldariorum, showed the same linear course at both RuBP concentrations. Sequencing of rbcL of these organisms indicated that Lys-305 was changed into arginine with Lys-21 conserved.

Keywords: Conjugatae; Fallover; Non-catalytic substrate-binding sites; Photosynthetic organisms; Ribulose 1,5-bisphosphate; Ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39)

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Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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