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Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus

A monofunctional prephenate dehydrogenase (PD) from Aquifex aeolicus was expressed as a His-tagged protein in Escherichia coli and was purified by nickel affinity chromatography allowing the first biochemical and biophysical characterization of a thermostable PD. A. aeolicus PD is susceptible to pro...

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書誌詳細
主要な著者: Bonvin, Julie, Aponte, Raphael A., Marcantonio, Maria, Singh, Sasha, Christendat, Dinesh, Turnbull, Joanne L.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 2006
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2265095/
https://ncbi.nlm.nih.gov/pubmed/16731976
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.051942206
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