The acetate kinase of Clostridum acetobutylicum strain P262

Francisco Diez-Gonzalez, James B. Russell, Jean B. Hunter

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Clostridum acetobutylicum strain P262 fermented glucose, pyruvate, or lactate, and the butyrate production was substrate-dependent. Differences in butyrate yield could not be explained by changes in butyrate kinase activities, but the butyrate production was inversely related to acetate kinase activity. The acetate kinase had a pH optimum of 8.0, a Km for acetate of 160 mM, and a kcat of 16,800 min-1. The enyzme had a native molecular mass of 78 kDa; the size of 42 kDa on SDS-PAGE indicated that the acetate kinase of strain P262 was a homodimer.

Original languageEnglish (US)
Pages (from-to)418-420
Number of pages3
JournalArchives of Microbiology
Issue number6
StatePublished - Dec 1 1996


  • Acetate kinase
  • Acetate utilization
  • Clostridum acetobutylicum


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