<i>Rhizomucor miehei</i> triglyceride lipase is synthesized as a precursor

DOI Web Site 被引用文献7件
  • Esper Boel
    Novo Research Institute Novo Allé Bagsvaerd‐Copenhagen DK‐2880 Denmark
  • Birgitte Huge‐Jensen
    Novo Research Institute Novo Allé Bagsvaerd‐Copenhagen DK‐2880 Denmark
  • Mogens Christensen
    Novo Research Institute Novo Allé Bagsvaerd‐Copenhagen DK‐2880 Denmark
  • Lars Thim
    Novo Research Institute Novo Allé Bagsvaerd‐Copenhagen DK‐2880 Denmark
  • Niels P. Fiil
    Novo Research Institute Novo Allé Bagsvaerd‐Copenhagen DK‐2880 Denmark

抄録

<jats:title>Abstract</jats:title><jats:p>A<jats:italic>Rhizomucor miehie</jats:italic> cDNA library constructed in<jats:italic>Escherichia coli</jats:italic> was screened with synthetic oligonucleotides designed from knowledge of a partial amino acid sequence of the secreted triglyceride lipase (triacyl‐glycerol acylhydrolase EC 3.1.1.3) from this fungus. Lipase‐specific recombinants were isolated and their insert sequenced. Unlike characterized bacterial and mammalian triglyceride lipases, the fungal enzyme is synthesized as a precursor, including a 70 amino acid residue propeptide between the 24 amino acid residues of the signal peptide and the 269 residues of the mature enzyme. The precursor processing mechanism, which involves cleavage between a methionine and a serine residue, is unknown. By sequence comparison with other lipases, a serine residue involved in substrate binding was identified in the fungal lipase. The sequence around this residue is well‐conserved among characterized lipases. Conservation of an intron in an isolated cDNA recombinant and immunoprecipitation of in vitro synthesized<jats:italic>R. miehei</jats:italic> translation products indicates that the expression of the lipase gene might involve inefficient mRNA splicing.</jats:p>

収録刊行物

  • Lipids

    Lipids 23 (7), 701-706, 1988-07

    Wiley

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