Issue 30, 2012

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

Abstract

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 29 201-compound library against LL-DAP-AT identified an o-sulfonamidoarylhydrazide as a reversible inhibitor with IC50 ∼ 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.

Graphical abstract: Synthesis and structure–activity relationships of o-sulfonamido-arylhydrazides as inhibitors of ll-diaminopimelate aminotransferase (ll-DAP-AT)

Supplementary files

Article information

Article type
Communication
Submitted
05 1 2012
Accepted
30 1 2012
First published
27 2 2012

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

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

C. Fan and J. C. Vederas, Org. Biomol. Chem., 2012, 10, 5815 DOI: 10.1039/C2OB00040G

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