• Title of article

    FSAB: A new fructose-6-phosphate aldolase from Escherichia coli. Cloning, over-expression and comparative kinetic characterization with FSAA

  • Author/Authors

    Sلnchez-Moreno، نويسنده , , Israel and Nauton، نويسنده , , Lionel and Théry، نويسنده , , Vincent and Pinet، نويسنده , , Agnès and Petit، نويسنده , , Jean-Louis and de Berardinis، نويسنده , , Véronique and Samland، نويسنده , , Anne K. and Guérard-Hélaine، نويسنده , , Christine and Lemaire، نويسنده , , Marielle، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2012
  • Pages
    6
  • From page
    9
  • To page
    14
  • Abstract
    Fructose-6-phosphate aldolase B (FSAB) from Escherichia coli was successfully over-expressed as His-tagged recombinant protein. A decameric protein was observed as for FSAA. Unlike FSAA, FSAB is not thermally stable at temperatures higher than 60 °C. The 70% identity between the two aldolases has allowed the generation of a 3D structure which has shown a high similarity of the two active sites. Full kinetic studies towards several substrates have revealed that FSAB catalytic activity is very close to FSAA activity, corroborated by the similarity of their active sites. FSAB has been able to react with three known donors (dihydroxyacetone, hydroxyacetone and glycolaldehyde) but always slightly slower than FSAA.
  • Keywords
    Recombinant aldolase , Enzyme characterization , Fructose-6-phosphate aldolase B , Substrate Specificity , CC bond formation
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2012
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1717470