EC Number   |
General Information |
Reference |
|---|
   2.4.1.92 | malfunction |
alpha-L-iduronidase knockout mutant, IDUA KO, mice show reduced expression of GD3 and GM2/GD2 synthases and neuraminidase1 in cerebellum, and a decrease in GM2/GD2 synthase and neuraminidase 1 in the hippocampus. The observed ganglioside changes result from a combined effect of glycosaminoglycans on ganglioside biosynthesis and degradation. C57Bl/6 knockout mice deficient for alpha-L-iduronidase (IDUA-KO) represent a murine model for human mucopolysaccharidosis type I, MPS I, an autosomal recessive disease caused by a genetic defect that codifies a lysosomal hydrolase, alpha-L-iduronidase, IDUA, EC. 3.2.1.76 |
-, 736174 |
| 2.4.1.92 | malfunction |
genes of complement components (C1qalpha, C1qbeta, C1qgamma, C4 and C3aR) are up-regulated in the cerebellum of mice with combined knockout of GM2/GD2 synthase and GD3 synthase |
706531 |
| 2.4.1.92 | malfunction |
GM3 synthase/GM2 synthase double knock out cells evidence significantly impaired tumor growth in syngeneic immunocompetent mice |
723309 |
| 2.4.1.92 | malfunction |
in animals lacking either GM2/GD2 or GM3 synthase, tissue cholesterol concentrations and synthesis rates are normal in nearly all organs, and whole-animal sterol pools and turnover also are not different from control animals. Mice lacking both synthases, however, have small elevations in cholesterol concentrations in several organs, and the whole-animal cholesterol pool is marginally elevated. When either the GM2/GD2 or GM3 synthase activity is deleted in mice lacking Niemann-Pick type C function, the clinical phenotype is not changed, but lifespan is shortened. |
704993 |
| 2.4.1.92 | malfunction |
mutations in gene B4GALNT1 are the cause of an unusual neurodegenerative phenotype, most commonly classified as a complex form of hereditary spastic paraplegia, present in families from Kuwait, Italy and the Old Order Amish. Biochemical profiling of glycosphingolipid biosynthesis confirms a lack of GM2 in affected subjects in association with a predictable increase in levels of its precursor, GM3. In the absence of functional GM2 synthase in the patient cells, there will be a lack of downstream glycosphingolipids as substrates for sialyltransferase, ST3GALII, and this may be the cause of the ectopic sialylation of Gb3 |
735875 |
| 2.4.1.92 | metabolism |
the enzyme catalyzes the second step in complex ganglioside biosynthesis |
735875 |
| 2.4.1.92 | metabolism |
the enzyme is part of the biosynthetic pathway of glycosphingolipids, overview |
735601 |
| 2.4.1.92 | metabolism |
the enzyme is responsible for the biosynthesis of GM2 and GD2 gangliosides, biosynthesis and degradation pathways of a- and b-series gangliosides, overview |
-, 736174 |
| 2.4.1.92 | more |
UVB-irradiation of keratinocytes induces melanoma-associated ganglioside GM2/GD2 synthase gene in melanocytes via secretion of tumor necrosis factor alpha and interleukin 6 |
735601 |
| 2.4.1.92 | physiological function |
GM2 synthase is a GalNAc transferase responsible for synthesizing GM2, GA2 and GD2. GM2 ganglioside is a sialylated glycosphingolipid that is synthesized in the Golgi apparatus as part of a complex biosynthetic pathway |
735875 |
