Aspartokinase III, a new isozyme in Bacillus subtilis 168.
A previously undetected Bacillus subtilis aspartokinase isozyme, which we have called aspartokinase III, has been characterized. The new isozyme was most readily detected in extracts of cells grown with lysine, which repressed aspartokinase II and induced aspartokinase III, or in extracts of strain VS11, a mutant lacking aspartokinase II. Antibodies against aspartokinase II did not cross-react with aspartokinase III. Aspartokinases II and III coeluted on gel filtration chromatography at Mr 120,000, which accounts for the previous inability to detect it. Aspartokinase III was induced by lysine and repressed by threonine. It was synergistically inhibited by lysine and threonine. Aspartokinase III activity, like aspartokinase II activity, declined rapidly in B. subtilis cells that were starved for glucose. In contrast, the specific activity of aspartokinase I, the diaminopimelic acid-inhibitable isozyme, was constant under all growth conditions examined.
Graves
L M
LM
Department of Biochemistry, University of Illinois, Urbana 61801.
Switzer
R L
RL
D000596:Amino Acids / Q000494:pharmacology; D001222:Aspartate Kinase / Q000032:analysis*; D001412:Bacillus subtilis / Q000201:enzymology* / Q000254:growth & development; D007527:Isoenzymes / Q000032:analysis*; D008239:Lysine / Q000494:pharmacology; D010770:Phosphotransferases / Q000032:analysis*
D000596:Amino Acids; D007527:Isoenzymes; D010770:Phosphotransferases; D001222:Aspartate Kinase; D008239:Lysine