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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

Y71H10A.1  -  Protein Y71H10A.1

Caenorhabditis elegans

 
 
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High impact information on phosphofructokinase

  • Purified phosphofructokinase from the earthworm Lumbricus terrestris was phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase from the same organism to an extent of approx. 0.5 mol/mol of subunit [1].
  • Activation by phosphorylation of phosphofructokinase from the annelid Lumbricus terrestris and comparison of phosphorylated sites in invertebrate phosphofructokinases [1].
  • The nucleotide sequence of a full-length cDNA encoding phosphofructokinase (PFK) enzyme from the parasitic nematode Ascaris suum was determined [2].
  • Analyses of the subunit primary structure reveal, as in other eukaryotic PFKs, that the amino-terminal half is homologous to the carboxy-terminal half, supporting the hypothesis that the PFK gene evolved by duplication of the prokaryotic gene and that the allosteric sites arose by mutations at the catalytic site [2].
 

Biological context of phosphofructokinase

References

  1. Activation by phosphorylation of phosphofructokinase from the annelid Lumbricus terrestris and comparison of phosphorylated sites in invertebrate phosphofructokinases. Schaloske, R., Biethinger, M., Fothergill-Gilmore, L.A., Hofer, H.W. Biochem. J. (1996) [Pubmed]
  2. Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum phosphofructokinase. Kulkarni, G., Sabnis, N.A., Bhat, K.S., Harris, B.G. J. Parasitol. (2005) [Pubmed]
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