Incorporation of [32P]- and [14C]-ATP intoEscherichia coli isocitrate lyase |
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Authors: | Jeffrey C Hoyt Henry C Reeves |
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Institution: | (1) Department of Microbiology, Arizona State University, 85287 Tempe, Arizona, USA |
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Abstract: | InEscherichia coli, isocitrate lyase has been shown to be phosphorylated in vitro by -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 -32P]ATP, isocitrate lyase has been found to incorporate radioactive label from -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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