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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2000-5-31
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pubmed:abstractText |
Aminoacyl (Phe, Gly) derivatives of nucleoside aliphatic analogues bearing a hydroxyalkyl chain have been prepared by the condensation of the alcohols with N-benzyloxycarbonyl-amino acid in the presence of DCC followed by hydrogenolysis in methanol. These compounds inhibit peptidyl transferase activity and binding of acceptor substrate to E. coli ribosomes. The inhibitory activity is not much affected by the nature of either the aminoacyl or the heterocyclic base residue. In the transfer reaction, no peptide bond formation occurs with the above compounds as acceptors.
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pubmed:commentsCorrections |
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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 |
Oct
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1221-31
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:10793684-Alkylation,
pubmed-meshheading:10793684-Binding Sites,
pubmed-meshheading:10793684-Enzyme Inhibitors,
pubmed-meshheading:10793684-Escherichia coli,
pubmed-meshheading:10793684-Esters,
pubmed-meshheading:10793684-Glycine,
pubmed-meshheading:10793684-Heterocyclic Compounds,
pubmed-meshheading:10793684-Molecular Conformation,
pubmed-meshheading:10793684-Molecular Structure,
pubmed-meshheading:10793684-Nucleosides,
pubmed-meshheading:10793684-Peptidyl Transferases,
pubmed-meshheading:10793684-Phenylalanine,
pubmed-meshheading:10793684-Protein Binding,
pubmed-meshheading:10793684-Ribosomes,
pubmed-meshheading:10793684-Structure-Activity Relationship
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pubmed:year |
1974
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pubmed:articleTitle |
The inhibition of peptidyl transferase activity by aminoacyl derivatives of some nucleoside aliphatic analogues.
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pubmed:publicationType |
Journal Article,
Comparative Study
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