Regulation of lysine decarboxylase activity in Escherichia coli K-12.
The biodegradative lysine decarboxylase of E. coli has been reported to attain a higher specific activity when grown to saturation in the presence of excess lysine under conditions of low pH and absence of aeration. In order to examine possible sources of the pH and anaerobic regulation, a series of isogenic strains of E. coli K-12 were constructed. The effects of cadR-, fnr-, cya-, crp- and pgi- mutations on lysine decarboxylase expression were examined. Cultures were grown in a lysine supplemented rich medium at pH 5.5, pH 6.8, and pH 8.0 with and without aeration and the enzyme was assayed from log phase cultures. The results suggested that the pH and air responses were independent and that these known regulatory processes are not responsible for this regulation of the biodegradative lysine decarboxylase.
Auger
E A
EA
Department of Biochemistry, Rice University, Houston, TX 77251.
Bennett
G N
GN
D000693:Anaerobiosis; D002262:Carboxy-Lyases / Q000096:biosynthesis* / Q000235:genetics; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005786:Gene Expression Regulation; D006863:Hydrogen-Ion Concentration; D009154:Mutation
D002262:Carboxy-Lyases; C021520:lysine decarboxylase