Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase MurG.
Chembiochem
; 4(7): 603-9, 2003 Jul 07.
Article
em En
| MEDLINE
| ID: mdl-12851929
ABSTRACT
A continuous fluorescence coupled enzyme assay was developed to study the acceptor specificity of the glycosyltransferase MurG toward different lipid I analogues with various substituents replacing the undecaprenyl moiety. It was found that most lipid I analogues are accepted as substrates and, amongst these, the saturated C14 analogue exhibits the best activity. This substrate was used to evaluate the inhibition activity of such antibiotics as moenomycin, vancomycin, and two chlorobiphenyl vancomycin derivatives. A vancomycin derivative with a chlorobiphenyl moiety on the aglycon section was identified as a potent inhibitor of MurG.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Proteínas da Membrana Bacteriana Externa
/
N-Acetilglucosaminiltransferases
/
Inibidores Enzimáticos
/
Monossacarídeos
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article