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The acetate kinase of Clostridum acetobutylicum strain P262.

Authors :
Diez-Gonzalez, Francisco
Russell, James
Hunter, Jean
Source :
Archives of Microbiology; Dec1996, Vol. 166 Issue 6, p418-420, 3p
Publication Year :
1996

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 for acetate of 160 mM, and a k of 16,800 min. 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03028933
Volume :
166
Issue :
6
Database :
Complementary Index
Journal :
Archives of Microbiology
Publication Type :
Academic Journal
Accession number :
72942938
Full Text :
https://doi.org/10.1007/BF01682990