• Title of article

    Molecular Evolution of Amphioxus Fructose-1,6- bisphosphate Aldolase

  • Author/Authors

    Kuba، نويسنده , , Masako and Yatsuki، نويسنده , , Hitomi and Kusakabe، نويسنده , , Takahiro and Takasaki، نويسنده , , Yozo and Nikoh، نويسنده , , Naruo and Miyata، نويسنده , , Takashi and Yamaguchi، نويسنده , , Takao and Hori، نويسنده , , Katsuji، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 1997
  • Pages
    8
  • From page
    329
  • To page
    336
  • Abstract
    The cDNA for amphioxus fructose-1,6-bisphosphate (FBP)-aldolase was isolated and its nucleotide sequence was determined. In the cDNA, there existed a probable open reading frame comprising 1080 bp; hence, 359 amino acid residues were deduced. The amino acid sequence indicates the deletion of 4 residues from N-terminus, in comparison with the sequence of FBP-aldolase isozymes from other sources. There was only one FBP-aldolase gene, and one enzyme species corresponding, in the amphioxus; this is the first report of the existence of a single FBP-aldolase species in animals. Enzymatic studies of both native and the recombinant FBP-aldolase suggest that the amphioxus enzyme belongs to an ancestral class I type which is not discovered among vertebrate aldolase isozymes.
  • Keywords
    Evolution , Amphioxus , aldolase , Isozyme , Purification , characterization
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    1997
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1609670