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Updated: Jun 23, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Molecular characterization of Mycobacterium tuberculosis cystathionine gamma synthase--apo- and holoforms
Baisakhee Saha1, Somnath Mukherjee, Amit Kumar Das
1Department of Biotechnology, Indian Institute of Technology, Kharagpur, West Bengal 721302, India.
Abstract:
Multiple probes like absorbance, circular dichroism, fluorescence and biochemical changes have been exploited to understand the role of PLP (pyridoxal 5' phosphate) in guanidine hydrochloride (GdnHCl) mediated unfolding and refolding processes of cystathionine gamma synthase from Mycobacterium tuberculosis (MtCGS). Unfolding by GdnHCl inactivates the enzyme due to loss of ketoenamine tautomer. Though PLP induces difference in secondary structure content, it is unable to provide stabilizing effect during the overall secondary structure unfolding process. But it induces tertiary structure stability of the protein thereby counteracting the deleterious effect of denaturant. In silico modelling and cofactor docking provide insights into molecular structure of the enzyme.
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