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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2000-1-31
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pubmed:abstractText |
The Escherichia coli peptide antibiotic microcin B17 (MccB17) contains thiazole and oxazole heterocycles derived from a distributive yet directional cyclization of cysteines and serines in the McbA precursor catalyzed by MccB17 synthetase. Whether the formation of upstream rings potentiates downstream heterocyclization has not been previously determined.
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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 |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1074-5521
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
789-99
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10574779-Amino Acid Sequence,
pubmed-meshheading:10574779-Anti-Bacterial Agents,
pubmed-meshheading:10574779-Bacterial Proteins,
pubmed-meshheading:10574779-Bacteriocins,
pubmed-meshheading:10574779-Cysteine,
pubmed-meshheading:10574779-Escherichia coli,
pubmed-meshheading:10574779-Isomerism,
pubmed-meshheading:10574779-Models, Molecular,
pubmed-meshheading:10574779-Molecular Sequence Data,
pubmed-meshheading:10574779-Multienzyme Complexes,
pubmed-meshheading:10574779-Mutagenesis,
pubmed-meshheading:10574779-Peptides,
pubmed-meshheading:10574779-Protein Conformation,
pubmed-meshheading:10574779-Serine
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|
pubmed:year |
1999
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pubmed:articleTitle |
Expressed protein ligation to probe regiospecificity of heterocyclization in the peptide antibiotic microcin B17.
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pubmed:affiliation |
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, 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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