Molecular characterization of Mycobacterium tuberculosis cystathionine gamma synthase--apo- and holoforms.
作者： Baisakhee Saha , Somnath Mukherjee , Amit Kumar Das
DOI: 10.1016/J.IJBIOMAC.2009.02.007
关键词:
摘要: 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 refolding processes cystathionine gamma synthase from Mycobacterium tuberculosis (MtCGS). Unfolding by GdnHCl inactivates enzyme due loss ketoenamine tautomer. Though induces difference secondary structure content, it is unable provide stabilizing effect during overall process. But tertiary stability protein thereby counteracting deleterious denaturant. In silico modelling cofactor docking insights into molecular enzyme.
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