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pubmed-article:17619101pubmed:abstractTextThe 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%.lld:pubmed
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pubmed-article:17619101pubmed:authorpubmed-author:ZhangKunKlld:pubmed
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pubmed-article:17619101pubmed:year2007lld:pubmed
pubmed-article:17619101pubmed:articleTitleCloning, expression, and characterization of an acetate kinase from a high rate of biohydrogen bacterial strain Ethanoligenens sp. hit B49.lld:pubmed
pubmed-article:17619101pubmed:affiliationSchool of Municipal and Environmental Engineering, Harbin Institute of Technology, Harbin, 150090 People's Republic of China.lld:pubmed
pubmed-article:17619101pubmed:publicationTypeJournal Articlelld:pubmed