Molecular and Structural Biology Division, Central Drug Research Institute, Lucknow 226001, India.
Int J Biol Macromol. 2011 Dec 1;49(5):917-22. doi: 10.1016/j.ijbiomac.2011.08.008. Epub 2011 Aug 12.
Metabolic plasticity of Mycobacterium renders high degree of adaptive advantages in the persistence through the upregulation of glyoxylate shunt. The malate synthase (MS), an important enzyme of the shunt belongs to the G isoform and expressed predominantly as monomer. Here we did a comparative unfolding studies of two homologous MS from Mycobacterium tuberculosis (MtbMS) and Escherichia coli (ecMS) using various biophysical techniques. Despite having high sequence identities, they show different structural, stability and functional properties. The study suggests that the differences in the stability and unfolding of the two enzymes are by virtue of differential electrostatic modulation unique to their respective molecular assembly.
分枝杆菌的代谢可塑性通过糖异生支路的上调赋予了高度的适应性优势，从而得以持续存在。苹果酸合酶（MS）是支路中的一种重要酶，属于 G 同工型，主要以单体形式表达。在这里，我们使用各种生物物理技术对来自结核分枝杆菌（MtbMS）和大肠杆菌（ecMS）的两种同源 MS 进行了比较展开研究。尽管它们具有很高的序列同一性，但它们表现出不同的结构、稳定性和功能特性。研究表明，两种酶的稳定性和展开的差异是由于它们各自的分子组装所具有的独特的差异静电调制。
