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  • Title: Cloning, expression, and characterization of an acetate kinase from a high rate of biohydrogen bacterial strain Ethanoligenens sp. hit B49.
    Author: Ren NQ, Lin HL, Zhang K, Zheng GX, Duan ZJ, Lin M.
    Journal: Curr Microbiol; 2007 Aug; 55(2):167-72. PubMed ID: 17619101.
    Abstract:
    The acetate kinase (ack) gene from Ethanoligenens sp. hit B49, isolated from a biohydrogen production bioreactor, is a key enzyme and responsible for dephosphorylation of acetyl phosphate with the concomitant production of acetate and ATP; it was cloned, sequenced, and functionally expressed in Escherichia coli BL21(DE3). It contained a 1200-bp open reading frame and encoded a 399-amino-acid protein kinase (molecular weight, 43.22 kDa; isoionic point, pH 5.93) sharing 58% similarity with Thermotoga maritima MSB8 ack. Ack was heterologously expressed in E.coli BL21 (DE3). Ack specific activities of the refolded ack inclusion body from Ethanoligenens sp. hit B49 is 42.12 U at 25 degrees C, and the renaturation percent is 14.36%.
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