Open AccessL (+)‐lactate dehydrogenase of Clostridium acetobutylicum is activated by fructose‐1,6‐bisphosphate
Author(s) -
Freier D.,
Gottschalk G.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02128.x
Subject(s) - clostridium acetobutylicum , biochemistry , enzyme , dehydrogenase , chemistry , clostridium , lactate dehydrogenase , fructose , pyruvate dehydrogenase complex , biology , bacteria , butanol , ethanol , genetics
Cells of Clostridium acetobutylicum contained an NADH‐dependent L (+)‐lactate dehydrogenase which was activated specifically by fructose‐1,6‐bisphosphate (F‐1,6‐P 2 ), with calcium or magnesium ions as positive effectors. During the purification steps the enzyme was very unstable. The purified enzyme existed in a tetrameric structure (apparent M r of about 159 kDa) and had its pH optimum at pH 5.8. Little activity was left at pH values below 5.0. The enzyme was unidirectional, catalysing only the reduction of pyruvate. The half maximal activation of the reaction velocity with F‐1,6‐P 2 depended on the pyruvate concentration.