Conservation,evolution, and specificity in cellular control by protein phosphorylation |
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Authors: | H W Hofer |
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Institution: | (1) Faculty of Biology, University of Konstanz, P.O. Box 5560, M648, D-78434 Konstanz, (Germany) |
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Abstract: | The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis. |
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Keywords: | Protein kinase (cAMP-dependent) protein phosphatases phosphofructokinase Ascaris lumbricoides evolution of proteins substrate specificity regulation of glycolysis |
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