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Plant 5-Methylthioribose Kinase

Properties of the Partially Purified Enzyme from Yellow Lupin (Lupinus Luteus L.) Seeds

Institute of Biochemistry, Academy of Agriculture, Wolyska 35, 60-637 Pozna, Poland

Activity of 5-methylthioribose kinase, the enzyme which catalyzes the ATP-dependent formation of 1-phospho-5-methylthioribose, has been revealed in the extracts from various higher plant species. Almost 2,000-fold-purified enzyme has been obtained from yellow lupin (Lupinus luteus L. cv Topaz) seed extract. Molecular weight of the native enzyme is 70,000 as judged by gel filtration. The lupin 5-methylthioribose kinase exhibits a strict requirement for divalent metal ions. Among the ions tested, only Mg²⁺ and Mn²⁺ acted as cofactors. The curve of kinase initial velocity versus pH reaches plateau at pH 10 to 10.5. The K_m values calculated for 5-methylthioribose and ATP are 4.3 and 8.3 micromolar, respectively.

Among nucleoside triphosphates tested as potential phosphate donors, only dATP could substitute in the reaction for ATP. 5-Isobutylthioribose, an analog of 5-methylthioribose, proved to be the -ATP-phosphate acceptor, too. The compound inhibits competitively synthesis of 1-phospho-5-methylthioribose (K_i = 1.4 micromolar). Lupin 5-methylthioribose kinase is completely and irreversibly inhibited by the antisulfhydryl reagent, p-hydroxymercuribenzoate. As in bacteria (Ferro, Barrett, Shapiro 1978 J Biol Chem 253: 6021-6025), the enzyme may be involved in a new, alternative pathway of methionine synthesis in plant tissues.

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