N(2)-substituted D,L-cycloserine derivatives: Synthesis and evaluation as alanine racemase inhibitors

Myoung Goo Kim; Ulrich Strych; Kurt Krause; Michael Benedik; Harold Kohn

doi:10.7164/antibiotics.56.160

N(2)-substituted D,L-cycloserine derivatives: Synthesis and evaluation as alanine racemase inhibitors

Myoung Goo Kim
, Ulrich Strych
, Kurt Krause
, Michael Benedik
, Harold Kohn^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

A select series of N(2)-substituted D,L-Cycloserine derivatives were prepared and evaluated for inhibitory activity against purified alanine racemases (alr gene product) from Escherichia coli, Staphylococcus aureus, and Mycobacterium tuberculosis, as well as in a growth inhibition assay. N(2)-Modification led to loss of enzymatic inhibitory activity in most cases consistent with a recent proposal for cycloserine function.

Original language	English
Pages (from-to)	160-168
Number of pages	9
Journal	Journal of Antibiotics
Volume	56
Issue number	2
DOIs	https://doi.org/10.7164/antibiotics.56.160
Publication status	Published - 1 Feb 2003
Externally published	Yes

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abstract = "A select series of N(2)-substituted D,L-Cycloserine derivatives were prepared and evaluated for inhibitory activity against purified alanine racemases (alr gene product) from Escherichia coli, Staphylococcus aureus, and Mycobacterium tuberculosis, as well as in a growth inhibition assay. N(2)-Modification led to loss of enzymatic inhibitory activity in most cases consistent with a recent proposal for cycloserine function.",

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AU - Strych, Ulrich

AU - Krause, Kurt

AU - Benedik, Michael

AU - Kohn, Harold

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AB - A select series of N(2)-substituted D,L-Cycloserine derivatives were prepared and evaluated for inhibitory activity against purified alanine racemases (alr gene product) from Escherichia coli, Staphylococcus aureus, and Mycobacterium tuberculosis, as well as in a growth inhibition assay. N(2)-Modification led to loss of enzymatic inhibitory activity in most cases consistent with a recent proposal for cycloserine function.

UR - https://www.scopus.com/pages/publications/0345700229

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DO - 10.7164/antibiotics.56.160

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N(2)-substituted D,L-cycloserine derivatives: Synthesis and evaluation as alanine racemase inhibitors

Abstract

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