Studies on chimeric fusion proteins of human aldolase isozymes A and B.
Several kinds of fusion proteins between human aldolases A and B were prepared by recombinant DNA technology and their enzymic properties were examined. AB chimeras, which have aldolase A at the N-terminal region and aldolase B at the C-terminal region, were scarcely obtained, while BA chimeras were abundant (Kitajima et al., (1990), J. Biol. Chem., 265, 17493-17498). All the BAB chimeras, aldolase A fragments inserted in aldolase B, showed activity assignable to aldolase B type, which imply an essential role of Tyr residue at the C-terminus of aldolase A in the binding of fructose-1,6-bisphosphate (Fru-1,6-P2). BAB chimeras also showed reactivity to effectors such as fructose-2,6-bisphosphate (Fru-2,6-P2) and pyridoxal 5-phosphate (PLP), in a similar manner to aldolase B. BAB108 has a similarity to the BA108 chimera, but acts differently from other BAB chimeras, suggesting that its structure around active site looks like that of aldolase A.
Takasaki
Y
Y
Department of Biochemistry, Saga Medical School, Japan.
Hori
K
K
D004926:Escherichia coli / Q000235:genetics; D005634:Fructose-Bisphosphate Aldolase / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D005635:Fructosediphosphates / Q000494:pharmacology; D006801:Humans; D007527:Isoenzymes; D011993:Recombinant Fusion Proteins
D005635:Fructosediphosphates; D007527:Isoenzymes; D011993:Recombinant Fusion Proteins; D005634:Fructose-Bisphosphate Aldolase