118373-81-2Relevant articles and documents
Balhimycin, a new glycopeptide antibiotic with an unusual hydrated 3-amino-4-oxoaldopyranose sugar moiety
Chatterjee,Vijayakumar,Nadkarni,Patel,Blumbach,Ganguli,Fehlhaber,Kogler,Vertesy
, p. 3480 - 3484 (1994)
Balhimycin (1), C66H73Cl2N9O24, is a new glycopeptide antibiotic of the vancomycin class. It was isolated from the fermentation broth of an Amycolatopsis sp. Hoechst India Limited Y-86,21022. Its structure was elucidated on the basis of spectroscopic and chemical degradation studies. The aglycon is identical to that of vancomycin. The molecule contains two sugars, D-glucose and dehydrovancosamine. The latter unit remains as a hydrate in solution.
SEMI-SYNTHETIC GLYCOPEPTIDES WITH ANTIBACTERIAL ACTIVITY
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Page/Page column 38, (2009/01/20)
Semi- synthetic glycopeptides having antibacterial activity are described, in particular, the semi-synthetic glycopeptides described hereins are made by subjecting the a glycopeptide (Compound A, Compound B, COMPOUND H or Compound C) in acidic medium to hydrolyze the disaccharide moiety of the amino acid-4 of the parent glycopeptide to give the amino acid-4 monosaccharide; temporary protection of the amino grouρ(s); conversion of the monosaccharide to the amino-sugar derivative; acylation of the amino substituent on the amino acid-4 amino-substituted sugar moiety on these scaffolds with certain acyl groups; conversion of the acid moiety on the macrocyclic ring of these scaffolds to certain substituted amides and removal of the tempory aimo protection grouρ(s). Also provided are methods for the synthesis of the compounds, pharmaceutical compositions containing the compounds, and methods of use of the compounds for the treatment and/or prophylaxis of diseases, especially bacterial infections.
A systematic investigation of the synthetic utility of glycopeptide glycosyltransferases
Oberthuer, Markus,Leimkuhler, Catherine,Kruger, Ryan G.,Lu, Wei,Walsh, Christopher T.,Kahne, Daniel
, p. 10747 - 10752 (2007/10/03)
Glycosyltransferases involved in the biosynthesis of bacterial secondary metabolites may be useful for the generation of sugar-modified analogues of bioactive natural products. Some glycosyltransferases have relaxed substrate specificity, and it has been assumed that promiscuity is a feature of the class. As part of a program to explore the synthetic utility of these enzymes, we have analyzed the substrate selectivity of glycosyltransferases that attach similar 2-deoxy-L-sugars to glycopeptide aglycons of the vancomycin-type, using purified enzymes and chemically synthesized TDP β-2-deoxy-L-sugar analogues. We show that while some of these glycopeptide glycosyltransferases are promiscuous, others tolerate only minor modifications in the substrates they will handle. For example, the glycosyltransferases GtfC and GtfD, which transfer 4-epi-L-vancosamine and L-vancosamine to C-2 of the glucose unit of vancomycin pseudoaglycon and chloroorienticin B, respectively, show moderately relaxed donor substrate specificities for the glycosylation of their natural aglycons. In contrast, GtfA, a transferase attaching 4-epi-L-vancosamine to a benzylic position, only utilizes donors that are closely related to its natural TDP sugar substrate. Our data also show that the spectrum of donors utilized by a given enzyme can depend on whether the natural acceptor or an analogue is used, and that GtfD is the most versatile enzyme for the synthesis of vancomycin analogues.
