Purification and Properties of Dihydroxyacetone Kinase from Gluconobacter suboxydans
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概要
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Different carbon and nitrogen sources had little effect on the level of dihydroxyacetone kinase formed in the cells of Gluconobacter suboxydans. The enzyme was purified to homogeneity from cell-free extract of the organism by ammonium sulfate fractionation and chromatographies on DEAE-cellulose, hydroxyapatite and Sephadex G-200 (60-fold purification, 6% yield). Its molecular weight was 260,000; it was stabilized by addition of ATP, dithiothreitol, 2-mercaptoethanol or EDTA, and it reacted optimally at pH 6.5. D-Glyceraldehyde was equally as effective as DHA as a phosphate acceptor (K_m : 0.30 mM each). UTP showed 15% of the reactivity of ATP as a phosphate donor. K_m values for ATP were 0.33 mM in phosphorylation of dihydroxyacetone and 0.39 mM with D-glyceraldehyde. The enzyme activity was dependent on Mg^<2+> but not on Mn^<2+>. The reaction with dihydroxyacetone as an acceptor was inhibited by D-glyceraldehyde. The inhibition was competitive with respect to dihydroxyacetone (K_i=0.09 mM) and noncompetitive with respective to ATP (K_i=5.7 mM).
- 公益社団法人日本生物工学会の論文
- 1987-02-25
著者
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Tochikura Tatsurokuro
Department Of Agricultural Chemistry Kyoto University
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Tachiki Takashi
Department Of Bioscience & Technology Faculty Of Science & Engineering Ritsumeikan Universit
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CHIGIRI EIKO
Department of Food Science and Technology, Kyoto University
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Chigiri Eiko
Department Of Food Science And Technology Kyoto University
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