Hill H A, Lobb R R, Sharp S L, Stokes A M, Harris J I, Jack R S
Biochem J. 1976 Mar 1;153(3):551-60. doi: 10.1042/bj1530551.
A comparison of the product-inhibition patterns during cleavage of D-fructose 1,6-diphosphate by aldolases from yeast, rabbit muscle and Bacillus stearothermophilus shows an ordered reaction sequence for all three enzymes, with dihydroxyacetone phosphate the last-leaving product. Addition of Zn2+, Co2+, Fe2+, Mn2+ or Cd2+ ions to the inactive apo-(Bacillus stearothermophilus aldolase) restores activity to different extents, whereas Ni2+, Mg2+ or Cu2+ ions have no effect. The cleavage activity of this aldolase is not enhanced by added K+ ion. The effects of metal replacement on thermal stability, Km and Vmax. are given and the possible role of the metal is discussed in the light of these results.
对酵母、兔肌肉和嗜热脂肪芽孢杆菌的醛缩酶在裂解1,6-二磷酸-D-果糖过程中的产物抑制模式进行比较,结果表明这三种酶的反应顺序均为有序反应,磷酸二羟丙酮是最后离开的产物。向无活性的脱辅基(嗜热脂肪芽孢杆菌醛缩酶)中添加Zn2+、Co2+、Fe2+、Mn2+或Cd2+离子可不同程度地恢复其活性,而Ni2+、Mg2+或Cu2+离子则无此作用。添加K+离子不会增强该醛缩酶的裂解活性。给出了金属置换对热稳定性、Km和Vmax的影响,并根据这些结果讨论了金属可能发挥的作用。