Sandbox Reserved 1068: Difference between revisions
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MbtI Inhibition studies aid in the future design of anti-tubercular agents and broad-spectrum antibiotics. Mimics of the enzyme-bound intermediate of MbtI, isochorismate, prove to be significantly more potent inhibitors than the substrate, chorismate mimics <ref name= "manos-turvey"/>. Specifically, <scene name='69/694235/3rv6_with_vae1/1'>2-hydroxybenzoate-based inhibitors</scene> that contain extended hydrophobic enol ether side chains at C3 in place of the enol-pyruvate side chain found in chorismate and isochorismate. | MbtI Inhibition studies aid in the future design of anti-tubercular agents and broad-spectrum antibiotics. Mimics of the enzyme-bound intermediate of MbtI, isochorismate, prove to be significantly more potent inhibitors than the substrate, chorismate mimics <ref name= "manos-turvey"/>. Specifically, <scene name='69/694235/3rv6_with_vae1/1'>2-hydroxybenzoate-based inhibitors</scene> that contain extended hydrophobic enol ether side chains at C3 in place of the enol-pyruvate side chain found in chorismate and isochorismate. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
{{reflist}} | {{reflist}} | ||
