caa a22 4500 477084133 CHVBK 20180405111458.0 cr unu---uuuuu 170330e19960501xx s 000 0 eng 10.1007/BF01919314 doi (NATIONALLICENCE)springer-10.1007/BF01919314 Hofer H. Faculty of Biology, University of Konstanz, P.O. Box 5560, M648, D-78434, Konstanz, (Germany) aut Conservation, evolution, and specificity in cellular control by protein phosphorylation [Elektronische Daten] [H. Hofer] 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. Birkhäuser Verlag, 1996 Protein kinase (cAMP-dependent) nationallicence protein phosphatases nationallicence phosphofructokinase nationallicence Ascaris lumbricoides nationallicence evolution of proteins nationallicence substrate specificity nationallicence regulation of glycolysis nationallicence Experientia Birkhäuser-Verlag 52/5(1996-05-01), 449-454 0014-4754 52:5<449 1996 52 18 https://doi.org/10.1007/BF01919314 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01919314 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Hofer H. Faculty of Biology, University of Konstanz, P.O. Box 5560, M648, D-78434, Konstanz, (Germany) aut NATIONALLICENCE 773 0- Experientia Birkhäuser-Verlag 52/5(1996-05-01), 449-454 0014-4754 52:5<449 1996 52 18 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer