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Several GM3 derivatives have been synthesized. Among them were lyso-GM3 derivatives and GM3 analogues with modifications in the sialic acid moiety. They were used as glycolipid acceptors in assays for GM2 and GD3 synthase of rat liver Golgi. Analysis of the resulting enzyme activities and of the reaction products revealed different substrate specificities for GM2 and GD3 synthase although the normal glycolipid acceptor for both transferases is ganglioside GM3. Specificity of GD3 synthase is strongly determined by the substrate's negative charge and the acyl residue in amide bond to the amino group of neuraminic acid, while GM2 synthase reacts quite indifferently to these changes in the sialic moiety of the substrate. Both enzymes seem to be sensitive to the spatial extension at the neuraminic acid's carboxylic group.
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
May 1987,
Biological chemistry Hoppe-Seyler,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
May 1989,
FEBS letters,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
August 1989,
FEBS letters,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
February 1976,
FEBS letters,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
November 1998,
Lipids,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
May 1981,
The Journal of cell biology,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
June 1996,
European journal of biochemistry,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
December 1991,
Journal of neurochemistry,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
April 1996,
Glycoconjugate journal,
D Klein, and
G Pohlentz, and
G Schwarzmann, and
K Sandhoff
April 1997,
Neurochemical research,
