Abstract: General methods for monitoring the activity of MurG, a GlcNAc transferase involved in bacterial cell wall biosynthesis, is disclosed. More particularly, the synthesis of simplified substrate analogs of Lipid I (the natural substrate for MurG), which function as acceptors for UDP-GlcNAc in an enzymatic reaction catalyzed by MurG, is described. Assays using the substrate analogs of the invention are further disclosed, which are useful for identifying a variety of other substrates, including inhibitors of MurG activity, for facilitating mechanistic and/or structural studies of the enzyme and for other uses. High throughput assays are also described.

Abstract: A glycopeptide of the formula A1-A2-A3-A4-A5-A6-A7, in which each dash represents a covalent bond; wherein A1 comprises a modified or unmodified &agr;-amino acid residue, alkyl, aryl, aralkyl, alkanoyl, aroyl, aralkanoyl, heterocyclic, heterocyclic-carbonyl, heterocyclic-alkyl, heterocyclic-alkyl-carbonyl, alkylsulfonyl, arylsulfonyl, guanidinyl, carbamoyl, or xanthyl; wherein each of A2 to A7 comprises a modified or unmodified &agr;-amino acid residue, whereby (i) A1 is linked to an amino group on A2, (ii) each of A2, A4 and A6 bears an aromatic side chain, which aromatic side chains are cross-linked together by two or more covalent bonds, and (iii) A7 bears a terminal carboxyl, ester, amide, or N-substituted amide group;

Abstract: A glycopeptide of the formula A1—A2—A3—A4—A5—A6—A7, in which each dash represents a covalent bond; wherein A1 comprises a modified or unmodified &agr;-amino acid residue, alkyl, aryl, aralkyl, alkanoyl, aroyl, aralkanoyl, heterocyclic, heterocyclic-carbonyl, heterocyclic-alkyl, heterocyclic-alkyl-carbonyl, alkylsulfonyl, arylsulfonyl, guanidinyl, carbamoyl, or xanthyl; wherein each of A2 to A7 comprises a modified or unmodified &agr;-amino acid residue, whereby (i) A1 is linked to an amino group on A2, (ii) each of A2, A4 and A6 bears an aromatic side chain, which aromatic side chains are cross-linked together by two or more covalent bonds, and (iii) A7 bears a terminal carboxyl, ester, amide, or N-substituted amide group; and wherein one or more of A1 to A7 is linked via a glycosidic bond to one or more glycosidic groups each having one or more sugar residues, at least one of the sugar residues bearing one or more substituents of the formula YXR, N+(R1)═CR2R3, N

Abstract: General methods for monitoring the activity of MurG, a GlcNAc transferase involved in bacterial cell wall biosynthesis, is disclosed. More particularly, the synthesis of simplified substrate analogs of Lipid I (the natural substrate for MurG), which function as acceptors for UDP-GlcNAc in an enzymatic reaction catalyzed by MurG, is described. Assays using the substrate analogs of the invention are further disclosed, which are useful for identifying a variety of other substrates, including inhibitors of MurG activity, for facilitating mechanistic and/or structural studies of the enzyme and for other uses. High throughput assays are also described.

Abstract: General methods for monitoring the activity of MurG, a GlcNAc transferase involved in bacterial cell wall biosynthesis, is disclosed. More particularly, the synthesis of simplified substrate analogs of Lipid I (the natural substrate for MurG), which function as acceptors for UDP-GlcNAc in an enzymatic reaction catalyzed by MurG, is described. Assays using the substrate analogs of the invention are further disclosed, which are useful for identifing a variety of other substrates, including inhibitors of MurG activity, for facilitating mechanistic and/or structural studies of the enzyme and for other uses. High throughput assays are also described.

Abstract: General methods for monitoring the activity of MurG, a GlcNAc transferase involved in bacterial cell wall biosynthesis, is disclosed. More particularly, the synthesis of simplified substrate analogs of Lipid I (the natural substrate for MurG), which function as acceptors for UDP-GlcNAc in an enzymatic reaction catalyzed by MurG, is described. Assays using the substrate analogs of the invention are further disclosed, which are useful for identifying a variety of other substrates, including inhibitors of MurG activity, for facilitating mechanistic and/or structural studies of the enzyme and for other uses. High throughput assays are also described.

Abstract: A method for forming a glycosidic linkage by: (a) contacting a glycoside bearing an anomeric sulfoxide group with a compound bearing a free hydroxyl group in the presence of an organic acid anhydride and a scavenger of sulfenyl esters; and (b) allowing a glycosylation reaction to proceed under conditions effective to produce the glycosidic linkage. In a preferred embodiment of the invention, the glycoside bearing an anomeric sulfoxide group is added to a mixture of the other reactants. In another preferred embodiment of the invention, a Lewis acid is also present in the reaction mixture. This invention is further directed to a method for forming a glycosidic linkage by: (a) forming a solution comprising: a compound bearing a free hydroxyl group, and an organic acid anhydride; (b) adding to the solution a glycoside bearing an anomeric sulfoxide group; and (c) allowing a glycosylation reaction to proceed under conditions effective to produce the glycosidic linkage.