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Arch Biochem Biophys. 1988 Oct;266(1):10-31.

Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases.

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Biochemisches Institut der Universit├Ąt Z├╝rich, Switzerland.


The amino acid sequence of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster was determined and was compared with those of five vertebrate aldolases on record. The four identical polypeptide chains of the insect enzyme, acetylated at the N-terminus and three residues shorter than the vertebrate chains, contain 360 amino acid residues. Of these 190 (or 53%) are identical in all six enzymes and in addition 33 positions (or 9%) are occupied by homologous residues. Comparison with the muscle-type isoaldolases from man and rabbit and the liver-type isoaldolases from man, rat, and chicken indicates an average sequence identity of 70 and 63%, respectively. Thus, the insect and the vertebrate muscle aldolases are probably coded by orthologous genes. On this basis an average rate of evolution of 3.0 PAM per 10(8) years is calculated, documenting an evolutional divergence slower than that of cytochrome c (4.2 PAM/10(8) years). The rate is also lower than that of the liver isoform (3.6 PAM/10(8) years). Secondary structure prediction analysis for Drosophila aldolase suggests the occurrence of 11-12 helical segments and 8-9 beta-strands. The conspicuous alternation of these structures in all six aldolases, especially in the C-terminal 200 residues, is consistant with the formation of an alpha beta-barrel supersecondary structure as documented for several other glycolytic enzymes.

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