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The acetate kinase of Clostridum acetobutylicum strain P262 (1997)

Diez-Gonzalez, Francisco ; Russell, J. B. ; Hunter, Jean B.

Springer

Archives of microbiology 166 (1997), S. 418-420

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ISSN: 1432-072X

Keywords: Key wordsClostridum acetobutylicum ; Acetate kinase ; Acetate utilization

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract 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 K m for acetate of 160 mM, and a k cat 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01682990

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