Open AccessAcetyl‐CoA synthetase from Pseudomonas putida U is the only acyl‐CoA activating enzyme induced by acetate in this bacterium
Author(s) -
AriasBarrau Elsa,
Olivera Elías R.,
Sandoval Ángel,
Naharro Germán,
Luengo José M.
Publication year - 2006
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.1574-6968.2006.00298.x
Subject(s) - pseudomonas putida , catabolism , biochemistry , enzyme , pseudomonadales , bacteria , pseudomonas , mutant , pseudomonadaceae , biology , gene , plasmid , chemistry , genetics
The gene ( acs ) encoding the acetyl‐CoA synthetase (Acs) in Pseudomonas putida U has been cloned, sequenced and expressed in different microbes. The protein has been purified and characterized from a biochemical, structural and evolutionary point of view. Disruption or deletion of acs handicapped the bacterium for growth in a chemically defined medium containing acetate; this ability was regained when P. putida U was transformed with a plasmid carrying this gene. By contrast, all the acs knock‐out mutants could assimilate n ‐alkanoic acids having a carbon length greater than C2, suggesting that other acyl‐CoA activating enzymes (different from Acs) are involved in the catabolism of these compounds. However, these enzymes that can replace the function played by Acs in vivo are not induced by acetate.