PMID:21864568
| Citation |
Kumar, R and Bhakuni, V (2011) Comparative analysis of malate synthase G from Mycobacterium tuberculosis and E. coli: role of ionic interaction in modulation of structural and functional properties. Int. J. Biol. Macromol. 49:917-22 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1016/j.ijbiomac.2011.08.008 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cloning, Molecular; Enzyme Stability/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Glyoxylates/metabolism; Ions/chemistry; Ions/metabolism; Isoenzymes/chemistry; Isoenzymes/genetics; Isoenzymes/metabolism; Malate Synthase/chemistry; Malate Synthase/genetics; Malate Synthase/metabolism; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis/enzymology; Mycobacterium tuberculosis/genetics; Plasmids; Protein Structure, Quaternary; Protein Unfolding/drug effects; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Species Specificity; Transformation, Bacterial; Urea/adverse effects |
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