Conservation, evolution, and specificity in cellular control by protein phosphorylation.
The glycolytic control enzyme phosphofructokinase from the parasitic nematode Ascaris lumbricoides 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.
Hofer
H W
HW
University of Konstanz, Faculty of Biology, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D017164:Ascaris lumbricoides / Q000201:enzymology; D005075:Biological Evolution; D017124:Conserved Sequence; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006019:Glycolysis; D008322:Mammals; D051379:Mice; D008969:Molecular Sequence Data; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D010766:Phosphorylation; D010802:Phylogeny; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D010732:Phosphofructokinase-1; D017868:Cyclic AMP-Dependent Protein Kinases