Molecular evolution of amphioxus fructose-1,6 bisphosphate aldolase

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

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)329-336
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - Dec 15 1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology


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