Abstract
InEscherichia coli, isocitrate lyase has been shown to be phosphorylated in vitro by [γ-32P]-ATP on histidine residues. This phosphorylation is believed to be necessary for activity of this enzyme. Previous work has shown that treatment of isocitrate lyase with acid phosphatase leads to a decrease in activity as well as a loss of incorporated [32P]-phosphate in a time-dependent manner. In addition to phosphorylation by [γ-32P]ATP, isocitrate lyase has been found to incorporate radioactive label from [α-32P]ATP and from [14C]ATP. This finding may indicate that more than one type of covalent modification occurs on this enzyme. Isocitrate lyase activity, inE. coli, may be regulated by posttranslational modification in several ways.
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Hoyt, J.C., Reeves, H.C. Incorporation of [32P]- and [14C]-ATP intoEscherichia coli isocitrate lyase. Current Microbiology 18, 257–259 (1989). https://doi.org/10.1007/BF01570302
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DOI: https://doi.org/10.1007/BF01570302