Contribution of different amino acids among Geobacillus uridine kinases to the conformational thermo

来源 :The 9th Asian Biophysics Association Symposium (ABA2015)(第九届 | 被引量 : 0次 | 上传用户:bloodsteven
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Enzymes synthesizing various nucleotides will be anticipated to apply for the novel nucleotide analogs such as anti-virus drugs by enzymatic synthesis.From the points of view, we focused to Uridine kinase (UK), which catalyzes the phosphorylation of uridine/ cytidine to UMP/CMP.Though it is expected that UKs from thermophilic Geobacillus bacteria may have high thermostability, but Geobacillus UKs have been unknown yet.In previous study, we cloned and analyzed UK genes from seven Geobacillus bacteria, followed by expressed in E.coli cells, and characterized these recombinant UKs.As results, trimeric G.thermocatenulatus (Gtc) UK was the most thermostable in terms of tertiary and quatemary structures, and it was deduced that the difference in thermostability might be caused by four different amino acids among these UKs(Ser/Phe50, Phe/Leu65, Thr/Ala91, and Met/lie147).In this study, we examined the contribution of Ser50,Phe65, and Met147 to the conformational thermostability of Gtc UK.
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