Modulating Enzyme's Conformational Space: Impact of Substrate Binding, Mode Alteration, and Active Site Mutation in DapC, an Aminotransferase Enzyme of Lysine Biosynthetic Pathway.

Abstract excerpt

The microbial aminotransferase enzyme DapC is vital for lysine biosynthesis in various Gram-positive bacteria, including Mycobacterium tuberculosis. Characterization of the enzyme's conformational dynamics and identifying the key residues for ligand binding are crucial for the development of effective antimicrobials. This study employs atomistic simulations to explore and categorize the dynamics of DapC in...

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