Molecular Evolution of Amphioxus Fructose-1,6- bisphosphate Aldolase
Copyright policy )Molecular Evolution of Amphioxus Fructose-1,6- bisphosphate Aldolase
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.
- Kyoto University Japan
- Kumamoto University Japan
- Saga Group United Kingdom
- Saga Medical School Hospital Japan
Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Electrophoresis, Cellulose Acetate, Recombinant Proteins, Evolution, Molecular, Kinetics, Chordata, Nonvertebrate, Fructose-Bisphosphate Aldolase, Vertebrates, Escherichia coli, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Sequence Analysis, Phylogeny, Sequence Deletion
Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Electrophoresis, Cellulose Acetate, Recombinant Proteins, Evolution, Molecular, Kinetics, Chordata, Nonvertebrate, Fructose-Bisphosphate Aldolase, Vertebrates, Escherichia coli, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Sequence Analysis, Phylogeny, Sequence Deletion
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