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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2003-4-28
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pubmed:abstractText |
A select series of N(2)-substituted D,L-cycloserine derivatives were prepared a ndevaluated 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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-8820
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
160-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12715876-Alanine Racemase,
pubmed-meshheading:12715876-Antibiotics, Antitubercular,
pubmed-meshheading:12715876-Chromatography, Thin Layer,
pubmed-meshheading:12715876-Cycloserine,
pubmed-meshheading:12715876-Enzyme Inhibitors,
pubmed-meshheading:12715876-Escherichia coli,
pubmed-meshheading:12715876-Mass Spectrometry,
pubmed-meshheading:12715876-Microbial Sensitivity Tests,
pubmed-meshheading:12715876-Mycobacterium tuberculosis,
pubmed-meshheading:12715876-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12715876-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:12715876-Staphylococcus aureus,
pubmed-meshheading:12715876-Structure-Activity Relationship
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pubmed:year |
2003
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pubmed:articleTitle |
N(2)-substituted D,L-cycloserine derivatives: synthesis and evaluation as alanine racemase inhibitors.
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pubmed:affiliation |
Division of Medicinal Chemistry and Natural Products, School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7360, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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