A Moenomycin-type Structural Analogue of Lipid II some possible mechanisms of the mode of action of transglycosylase inhibitors can be discarded

Autor:	Dietrich Müller, Lothar Hennig, Astrid Markus, Matthias Findesien, Jean van Heijenoort, Ralf Kosmol, Peter Welzel
Rok vydání:	1997
Předmět:	chemistry.chemical_classification Sugar phosphates Enzyme chemistry Lipid II Biochemistry Moenomycin A Stereochemistry Peptidoglycan biosynthesis Mode of action
Zdroj:	Journal für Praktische Chemie/Chemiker-Zeitung. 339:340-358
ISSN:	1521-3897 0941-1216
DOI:	10.1002/prac.19973390162
Popis:	The transglycosylation step in the peptidoglycan biosynthesis belongs to the general class of glycosyltransferase-catalyzed reactions. The structural analogue 2 of moenomycin A has been synthesized and has been found to be antibiotically inactive. The assumption that moenomycin-type transglycosylase inhibitors such as 1 bind at the donor site of the enzyme and that their mode of action is the result of the high stability of the sugar phosphate bond seems to be ruled out by the present results.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ccd50e05858df81b120599467eae6e66 https://doi.org/10.1002/prac.19973390162 Zobrazit plný text záznamu Plný text