Synthesis and structure–activity relationships of o-sulfonamido-arylhydrazides as inhibitors of LL-diaminopimelate aminotransferase (LL-DAP-AT)

Chenguang Fan; John C. Vederas

doi:10.1039/C2OB00040G

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Organic & Biomolecular Chemistry

Issue 30, 2012

The international home of synthetic, physical and biomolecular organic chemistry.

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Synthesis and structure–activity relationships of o-sulfonamido-arylhydrazides as inhibitors of LL-diaminopimelate aminotransferase (LL-DAP-AT)

Chenguang Fan^a and John C. Vederas*^a

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Department of Chemistry, University of Alberta, Edmonton, Canada
E-mail: john.vederas@ualberta.ca

Org. Biomol. Chem., 2012,10, 5815-5819

DOI: 10.1039/C2OB00040G
Received 05 Jan 2012, Accepted 30 Jan 2012
First published online 27 Feb 2012

This article is part of themed collection: Organic & Biomolecular Chemistry 10th Anniversary

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Abstract
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Recently, LL-diaminopimelate aminotransferase (LL-DAP-AT), a pyridoxal-5′-phosphate (PLP)-dependent enzyme, was reported to catalyze a key step in the biosynthesis of L-lysine in plants and Chlamydia. Previous screening of a 29201-compound library against LL-DAP-AT identified an o-sulfonamidoarylhydrazide as a reversible inhibitor with IC₅₀ [similar] 5 μM. Structure–activity relationship (SAR) studies based on this lead compound identified key structural features essential for enzyme inhibition and led to slightly improved inhibitors. Preliminary studies on the mode of inhibition of LL-DAP-AT by this class of compounds are also reported.