Molecular evolution of amphioxus fructose-1,6-bisphosphate aldolase

Archives of Biochemistry and Biophysics
M KubaK Hori

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.

Citations

May 25, 2002·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Rebecca F Furlong, Peter W H Holland
May 18, 2006·Parasitology Research·Pyo Yun ChoSung-Jong Hong

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