Abstract
The NADP+-specific glutamate dehydrogenase inEscherichia coli K12 has been shown to be phosphorylated in vivo when the cells are grown in a low-phosphate minimal salts medium containing32P inorganic phosphate. The amount of radioactivity incorporated into the enzyme is different depending on the growth phase of the culture, with the highest level of32P incorporation occurring during the mid-exponential growth phase. Previously reported studies have demonstrated that the enzyme is also phosphorylated in vitro in an ATP-dependent reaction.
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