Fructose-diphosphate aldolase of Horseshoe crab (Tachypleus tridentatus)

Abstract

Fructose-diphosphate aldolase [ED 4.1.2.13] was isolated from horseshoe crab ( living fossil) muscle and some molecular and enzymatic properties were examined. The enzyme was a tetramer with a molecular weight of about 160,000. The enzyme activity was inhibited by reduction with borohydride in the presence of the substrate and was inactivated by carboxypeptidase A [EC 3.4.12.2] digestion. The pH optima for fructose-diphosphate (FDP) and fructose-1-phosphate (F1P) activities were 6.5--8 and 7.5--8.2, respectively. The ratio of FDP/F1P activities was 30 and Km values were 1.7 times 10- minus 5 M and 2.5 times 10- minus 3 M, respectively, for the two substrates. The horseshoe crab aldolase was classified as class 1, type A, based on the results obtained. Extensive homology in various properties of the enzyme was observed when it was compared with enzymes from other sources, though some differences could be found in the amino acid composition and in the kinetic properties.