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嗜热脂肪芽孢杆菌醛缩酶中的金属置换研究以及I类和II类醛缩酶作用机制的比较。

Metal-replacement studies in Bacillus stearothermophilus aldolase and a comparison of the mechanisms of class I and class II aldolases.

作者信息

Hill H A, Lobb R R, Sharp S L, Stokes A M, Harris J I, Jack R S

出版信息

Biochem J. 1976 Mar 1;153(3):551-60. doi: 10.1042/bj1530551.

DOI:10.1042/bj1530551
PMID:942370
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1172621/
Abstract

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.

摘要

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。

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