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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
2007-12-6
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pubmed:abstractText |
Synthesis and evaluation of a chemical library of inhibitors of the mycothiol biosynthesis enzyme GlcNAc-Ins deacetylase (MshB) and the mycothiol-dependent detoxification enzyme mycothiol- S-conjugate amidase (MCA) from Mycobacterium tuberculosis are reported. The library was biased to include structural features of a group of natural products previously shown to competitively inhibit MCA. Molecular docking studies that reproducibly placed the inhibitors in the active site of the enzyme MshB reveal the mode of binding and are consistent with observed biological activity.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Furans,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol,
http://linkedlifedata.com/resource/pubmed/chemical/Isoxazoles,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyl-1-D-inosityl-2-amino-2-deox...,
http://linkedlifedata.com/resource/pubmed/chemical/Oxazines,
http://linkedlifedata.com/resource/pubmed/chemical/Oxazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrans,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides,
http://linkedlifedata.com/resource/pubmed/chemical/Thioglycosides,
http://linkedlifedata.com/resource/pubmed/chemical/mycothiol,
http://linkedlifedata.com/resource/pubmed/chemical/mycothiol S-conjugate amidase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-2623
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6326-36
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pubmed:meshHeading |
pubmed-meshheading:18020307-Amidohydrolases,
pubmed-meshheading:18020307-Bacterial Proteins,
pubmed-meshheading:18020307-Binding Sites,
pubmed-meshheading:18020307-Cysteine,
pubmed-meshheading:18020307-Furans,
pubmed-meshheading:18020307-Glycopeptides,
pubmed-meshheading:18020307-Inositol,
pubmed-meshheading:18020307-Isoxazoles,
pubmed-meshheading:18020307-Models, Molecular,
pubmed-meshheading:18020307-Mycobacterium tuberculosis,
pubmed-meshheading:18020307-Oxazines,
pubmed-meshheading:18020307-Oxazoles,
pubmed-meshheading:18020307-Protein Binding,
pubmed-meshheading:18020307-Pyrans,
pubmed-meshheading:18020307-Stereoisomerism,
pubmed-meshheading:18020307-Sulfonamides,
pubmed-meshheading:18020307-Thioglycosides
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pubmed:year |
2007
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pubmed:articleTitle |
Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol-associated enzymes: the first inhibitors of GlcNAc-Ins deacetylase.
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pubmed:affiliation |
Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Intramural
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