Specificity of human glucosylceramide β‐glucosidase towards synthetic glucosylsphingolipids inserted into liposomes
Specificity of human glucosylceramide β‐glucosidase towards synthetic glucosylsphingolipids inserted into liposomes
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人葡萄糖神经酰胺 β-葡萄糖苷酶对插入脂质体的合成葡萄糖鞘脂的特异性
DOI：
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
K. Sandhoff
中科院分区：
文献类型：
--
作者：
F. Sarmientos;G. Schwarzmann;K. Sandhoff
The behaviour of highly purified glucosylceramide β-glucosidase (glucosylceramidase, EC 3.2.1.45) from human placenta [Furbish, F. S., Blair, H. E., Shiloach, J., Pentchev, P. G. & Brady, R. B. (1977) Proc. Natl Acad. Sci. USA 74, 3560–3563] was investigated in the absence of detergents with structurally modified glucosyl-ceramides inserted into unilamellar liposomes. The reaction between the water-soluble enzyme and the liposomal substrates was significantly dependent on the structure of the lipophilic aglycon moiety of glycolipids: glucosyl-N-acetyl-sphingosines (d-erythro and l-threo) were better substrates than the corresponding glucosylceramides. The l-threo derivatives were poorer substrates with higher apparent Km values than the corresponding d-erythro derivatives. For glucosyl-3-keto-ceramide and glucosyl-dihydro-ceramide (d-erythro), higher Km values were found than for glucosylceramide. Sphingosine, glucosylsphingosine and glucosyl-N-acetyl-sphingosine were the most effective inhibitors of the hydrolysis of glucosylceramide. d-erythro-Ceramide and d-galactosyl-N-acetyl-d-erythro-sphingosine inhibited the hydrolyis of amphiphilic glucosylceramide but not that of water-soluble 4-methyl-umbelliferyl-β-glucoside, suggesting a hydrophobic binding site of the enzyme for the aglycon moiety of its membrane-bound substrate.
Dilution experiments suggested that at least a fraction of the enzyme associates with the liposomes and degrades the lipid substrate even in the absence of activator proteins.
Acidic phospholipids incorporated into liposomes caused a powerful stimulation (30–40-fold) of the glucosylceramide β-glucosidase, whereas acidic sphingolipids (sulphatide, gangliosides GM1 and GD1a) incorporated into liposomes stimulated this enzyme only moderately (3–10-fold).
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DOI：
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