Suzuki K, Shiho O, Imahori K
J Biochem. 1975 Feb;77(2):281-9. doi: 10.1093/oxfordjournals.jbchem.a130725.
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.
从鲎（活化石）肌肉中分离出果糖二磷酸醛缩酶[ED 4.1.2.13]，并检测了其一些分子和酶学性质。该酶是一种分子量约为160,000的四聚体。在底物存在下，硼氢化钠还原可抑制酶活性，羧肽酶A[EC 3.4.12.2]消化可使酶失活。果糖二磷酸（FDP）和果糖-1-磷酸（F1P）活性的最适pH分别为6.5 - 8和7.5 - 8.2。两种底物的FDP/F1P活性比值为30，Km值分别为1.7×10⁻⁵M和2.5×10⁻³M。根据所得结果，鲎醛缩酶被归类为1类，A型。与其他来源的酶相比，该酶在各种性质上存在广泛的同源性，不过在氨基酸组成和动力学性质上可发现一些差异。
