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Comparative analysis of malate synthase G from Mycobacterium tuberculosis and E. coli: Role of ionic interaction in modulation of structural and functional properties
2011 (English)In: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 49, no 5, 917-922 p.Article in journal (Refereed) Published
Abstract [en]

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 coil (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.

Place, publisher, year, edition, pages
2011. Vol. 49, no 5, 917-922 p.
Keyword [en]
Domain, Structural cooperativity, Stability, Enzymatic activity, Ionic interactions
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-163642DOI: 10.1016/j.ijbiomac.2011.08.008ISI: 000296937200008OAI: oai:DiVA.org:uu-163642DiVA: diva2:466677
Available from: 2011-12-16 Created: 2011-12-13 Last updated: 2017-12-08Bibliographically approved

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Kumar, Ranjeet

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