Acceptor Specificity and Inhibition of the Bacterial Cell-Wall Glycosyltransferase MurG
| Autor: | Thomas K. Ritter, Haitian Liu, Reiko Sadamoto, Chi-Huey Wong, Min Wu, Pamela Sears |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Stereochemistry
N-Acetylglucosaminyltransferases Biochemistry Bacterial cell structure Substrate Specificity Enzyme catalysis Inhibitory Concentration 50 Cell Wall Vancomycin Glycosyltransferase Escherichia coli medicine Moiety Enzyme Inhibitors Molecular Biology biology Chemistry Monosaccharides Organic Chemistry Substrate (chemistry) Lipid Metabolism Lipids Acceptor Enzyme assay Bambermycins biology.protein Molecular Medicine Oligopeptides Bacterial Outer Membrane Proteins medicine.drug |
| Zdroj: | ChemBioChem. 4:603-609 |
| ISSN: | 1439-4227 |
| DOI: | 10.1002/cbic.200300557 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text