Gene Cloning and Characterization of Fructose-1,6-Bisphosphate Aldolase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis KOD1
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概要
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The fructose-1,6-bisphosphate (FBP) aldolase gene from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 was cloned. The gene encoding FBP aldolase (Tk-fba) was expressed in Escherichia coli and the purified recombinant protein was characterized at high temperature. Tk-Fba is a homodecamer with a subunit molecular mass of 31,283 Da. The amino acid sequence, decameric conformation, formation of a Schiff-base intermediate, and stimulation (286%) of FBP cleavage activity by citrate suggested that Tk-Fba belonged to Class IA, a subtype of the classical Class I aldolases. The specific activity for the FBP cleavage reaction was 18.9 U/mg, which was much higher than those of other Class IA type FBP aldolases. Tk-Fba was extremely thermostable since the optimum temperature seemed to be above 100℃. The optimum pH for Tk-Fba was determined to be 5.0 in the absence of citrate, while it shifted to around 7.0 in the presence of citrate. Tk-Fba accepted FBP and fructose-1-phosphate as substrates and K_m values were determined to be 0.063 mM and 4.37 mM, respectively. In addition to citrate, phosphoenolpyruvate and pyrophosphate were also found to be potent activators of Tk-Fba, enhancing activities up to 346% and 201%, respectively. Erythrose-4-phosphate acted as an inhibitor and caused a decrease in the activity to 49%. Tk-Fba also catalyzed the condensation reaction with a similar activity level (14.9 U/mg) to that for FBP cleavage. However, none of the above compounds seemed to have a significant effect on the condensation reaction by Tk-Fba. These results suggest a regulatory function of Tk-Fba toward the catabolic direction of sugar metabolism in T. kodakaraensis KOD1.
- 社団法人日本生物工学会の論文
- 2002-09-25
著者
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Imanaka Hiroyuki
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
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FUKUI Toshiaki
Department of Bioengineering, Tokyo Institute of Technology
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IMANAKA Tadayuki
Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University
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ATOMI HARUYUKI
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto Un
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Atomi H
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering Kyoto Univ
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Atomi Haruyuki
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chemistr
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Atomi Haruyuki
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering Kyoto Univ
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Biotechnology Faculty Of Eigineering Osaka University
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Imanaka Tadayuki
Department Of Synthetic And Biological Chemistry Graduate School Of Engineering Kyoto University
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Imanaka T
Department Of Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering.kyoto Univ
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Atomi Haruyuki
Dept. Synth. Chem. Biol. Chem. Grad. Sch. Eng. Kyoto Univ.:crest Imanaka Project
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Fukui T
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering Kyoto Univ
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Imanaka T
Dep. Of Biotechnology Coll. Of Life Sciences Ritsumeikan Univ.
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Imanaka Hiroyuki
Department Of Synthetic Chemistry And Biological Chemistry Graduate School Of Engineering Kyoto Univ
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Fukui Toshiaki
Department Of Bioengineering Tokyo Institute Of Technology
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Fukui Toshiaki
Department Of Bioengineering Graduate School Of Bioscience And Biotechnology Tokyo Institute Of Technology
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