Open AccessChanges in NADP‐isocitrate dehydrogenase isoenzyme levels in Acinetobacter calcoaceticus in response to acetate
Author(s) -
Reeves Henry C.,
O'Neil Susan,
Weitzman P.David J.
Publication year - 1986
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.1574-6968.1986.tb01533.x
Subject(s) - acinetobacter calcoaceticus , isocitrate dehydrogenase , biochemistry , isozyme , allosteric regulation , dehydrogenase , enzyme , biology , idh1 , chemistry , acinetobacter , mutant , gene , antibiotics
During adaptation of Acinetobacter calcoaceticus to growth on acetate the specific activity of NADP‐isocitrate dehydrogenase increased. This response is unique, as in other bacteria grown under the same conditions the activity of the enzyme decreases as a result of covalent phosphorylation. Moreover, A. calcoaceticus is also unusual in containing two distinct isoenzymes of NADP‐isocitrate dehydrogenase. It has here been shown that the adaptation of A. calcoaceticus to acetate is accompanied by an increase in the relative proportion of the larger, allosteric, isoenzyme with a concomitant decrease in the level of the smaller, non‐allosteric, isoenzyme.