Sandbox Reserved 1068: Difference between revisions

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==Inhibition Studies==

MbtI Inhibition studies aid in the future design of [http://psychology.wikia.com/wiki/Antitubercular_drugs anti-tubercular agents] and [http://en.wikipedia.org/wiki/Broad-spectrum_antibiotic broad-spectrum antibiotics] with a novel mode of action. Mimics of the enzyme-bound intermediate of MbtI, <scene name='69/694235/3sr6_inhibitor/3'>isochorismate</scene>, prove to be significantly more potent inhibitors than mimics of the substrate, chorismate <ref name= "1a"/><ref name="2a"/><ref name="5a"/>. The isochorismate mimic based on a 2,3-dihydroxybenzoate scaffold showed low-micromolar inhibition constants against MbtI that were an order of magnitude more potents than the natural substrates<ref name="2a"/>. The most potent inhibitors contained hydrophobic enol ether side chains at C3 instead of the enol-pyruvyl side chains seen in chorismate and isochorismate. <ref name="1a">PMID:20512795</ref> Increased potency of <scene name='69/694235/3rv6_with_vae1/3'>inhibitors with a substituted enolpyruvyl group> as seen in [[3RV6]] has been attributed to a change in the binding mode through localized flexibility of the peptide backbone<ref name="2a"/><ref name="5a"/>.

MbtI Inhibition studies aid in the future design of [http://psychology.wikia.com/wiki/Antitubercular_drugs anti-tubercular agents] and [http://en.wikipedia.org/wiki/Broad-spectrum_antibiotic broad-spectrum antibiotics] with a novel mode of action. Mimics of the enzyme-bound intermediate of MbtI, <scene name='69/694235/3sr6_inhibitor/3'>isochorismate</scene>, prove to be significantly more potent inhibitors than mimics of the substrate, chorismate <ref name= "1a"/><ref name="2a"/><ref name="5a"/>. The isochorismate mimic based on a 2,3-dihydroxybenzoate scaffold showed low-micromolar inhibition constants against MbtI that were an order of magnitude more potents than the natural substrates<ref name="2a"/>. The most potent inhibitors contained hydrophobic enol ether side chains at C3 instead of the enol-pyruvyl side chains seen in chorismate and isochorismate. <ref name="1a">PMID:20512795</ref> Increased potency of <scene name='69/694235/3rv6_with_vae1/3'>inhibitors with a substituted enolpyruvyl group</scene> as seen in [[3RV6]] has been attributed to a change in the binding mode through localized flexibility of the peptide backbone<ref name="2a"/><ref name="5a"/>.

== References ==

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@@ Line 70: / Line 70: @@
 ==Inhibition Studies==
-MbtI Inhibition studies aid in the future design of [http://psychology.wikia.com/wiki/Antitubercular_drugs anti-tubercular agents] and [http://en.wikipedia.org/wiki/Broad-spectrum_antibiotic broad-spectrum antibiotics] with a novel mode of action.  Mimics of the enzyme-bound intermediate of MbtI, <scene name='69/694235/3sr6_inhibitor/3'>isochorismate</scene>, prove to be significantly more potent inhibitors than mimics of the substrate, chorismate <ref name= "1a"/><ref name="2a"/><ref name="5a"/>. The isochorismate mimic based on a 2,3-dihydroxybenzoate scaffold showed low-micromolar inhibition constants against MbtI that were an order of magnitude more potents than the natural substrates<ref name="2a"/>. The most potent inhibitors contained hydrophobic enol ether side chains at C3 instead of the enol-pyruvyl side chains seen in chorismate and isochorismate. <ref name="1a">PMID:20512795</ref> Increased potency of <scene name='69/694235/3rv6_with_vae1/3'>inhibitors with a substituted enolpyruvyl group> as seen in [[3RV6]] has been attributed to a change in the binding mode through localized flexibility of the peptide backbone<ref name="2a"/><ref name="5a"/>.
+MbtI Inhibition studies aid in the future design of [http://psychology.wikia.com/wiki/Antitubercular_drugs anti-tubercular agents] and [http://en.wikipedia.org/wiki/Broad-spectrum_antibiotic broad-spectrum antibiotics] with a novel mode of action.  Mimics of the enzyme-bound intermediate of MbtI, <scene name='69/694235/3sr6_inhibitor/3'>isochorismate</scene>, prove to be significantly more potent inhibitors than mimics of the substrate, chorismate <ref name= "1a"/><ref name="2a"/><ref name="5a"/>. The isochorismate mimic based on a 2,3-dihydroxybenzoate scaffold showed low-micromolar inhibition constants against MbtI that were an order of magnitude more potents than the natural substrates<ref name="2a"/>. The most potent inhibitors contained hydrophobic enol ether side chains at C3 instead of the enol-pyruvyl side chains seen in chorismate and isochorismate. <ref name="1a">PMID:20512795</ref> Increased potency of <scene name='69/694235/3rv6_with_vae1/3'>inhibitors with a substituted enolpyruvyl group</scene> as seen in [[3RV6]] has been attributed to a change in the binding mode through localized flexibility of the peptide backbone<ref name="2a"/><ref name="5a"/>.
 == References ==