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.
Kuba
M
M
Department of Biochemistry, Saga Medical School, Japan.
Yatsuki
H
H
Kusakabe
T
T
Takasaki
Y
Y
Nikoh
N
N
Miyata
T
T
Yamaguchi
T
T
Hori
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002816:Chordata, Nonvertebrate / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D019143:Evolution, Molecular; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D012333:RNA, Messenger / Q000032:analysis; D011994:Recombinant Proteins / Q000378:metabolism; D017421:Sequence Analysis; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014714:Vertebrates / Q000235:genetics
D012333:RNA, Messenger; D011994:Recombinant Proteins; D005634:Fructose-Bisphosphate Aldolase