Abstract
The search for potential inhibitors that target so far unexplored bacterial enzyme mono-N-succinyl-L,Ldiaminopimelic acid desuccinylase (DapE) has stimulated a development of methodology for quick and efficient preparation of mono-N-acylated 2,6-diaminopimelic acid (DAP) derivatives bearing the different carboxyl groups or lipophilic moieties on their amino group.
Keywords: Bacterial enzyme, N-succinyl-L, L-diaminopimelic acid (SDAP), synthesis of SDAP analogues, selective protection
Protein & Peptide Letters
Title: Synthesis of N-Succinyl-L,L-Diaminopimelic Acid Mimetics Via Selective Protection
Volume: 17 Issue: 3
Author(s): V. Vanek, J. Picha, M. Budesinsky, M. Sanda, J. Jiracek, R. C. Holz and J. Hlavacek
Affiliation:
Keywords: Bacterial enzyme, N-succinyl-L, L-diaminopimelic acid (SDAP), synthesis of SDAP analogues, selective protection
Abstract: The search for potential inhibitors that target so far unexplored bacterial enzyme mono-N-succinyl-L,Ldiaminopimelic acid desuccinylase (DapE) has stimulated a development of methodology for quick and efficient preparation of mono-N-acylated 2,6-diaminopimelic acid (DAP) derivatives bearing the different carboxyl groups or lipophilic moieties on their amino group.
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Cite this article as:
Vanek V., Picha J., Budesinsky M., Sanda M., Jiracek J., Holz C. R. and Hlavacek J., Synthesis of N-Succinyl-L,L-Diaminopimelic Acid Mimetics Via Selective Protection, Protein & Peptide Letters 2010; 17 (3) . https://dx.doi.org/10.2174/092986610790780387
DOI https://dx.doi.org/10.2174/092986610790780387 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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