3.1.6.8: cerebroside-sulfatase
This is an abbreviated version!
For detailed information about cerebroside-sulfatase, go to the full flat file.
Word Map on EC 3.1.6.8
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3.1.6.8
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metachromatic
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leukodystrophy
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sulfatide
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medicine
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lysosomal
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asa
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demyelinate
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sural
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pseudodeficiency
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nitrocatechol
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sulfatases
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molecular biology
- 3.1.6.8
-
metachromatic
- leukodystrophy
- sulfatide
- medicine
- lysosomal
- asa
-
demyelinate
-
sural
-
pseudodeficiency
- nitrocatechol
-
sulfatases
- molecular biology
Reaction
Synonyms
ARS, ARSA, arylsulfatase A, arylsulfatase E, arylsulfatase-A, AS-A, ASA, cerebroside sulfatase, cerebroside sulfate sulfatase, Cerebroside-sulfatase, sulfatase, cerebroside
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.1.6.8 - cerebroside-sulfatase
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glycoprotein
phosphoprotein
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compared to the degree of mannose-phosphorylation of the wild-type enzyme, the mutant enzyme K457R has 33%, mutant enzyme K457S has 50%, mutant enzyme K457G has 31%, mutant enzyme K433A has 95%, mutant enzyme K367A has 106% and mutant enzyme K393A has 123% of mannose-phosphorylation respectively
glycoprotein
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the wild-type enzyme has three N-glycosylation sites. Only oligosaccharides at the first, Asn158, and the third, Asn350, glycosylation site are phosphorylated, whereas the second, Asn184 is not
glycoprotein
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three N-glycosylation sites and three N-linked oligosaccharide side chains at asparagine residues 158, 184, and 350, the recombinantly expressed enzyme shows a high variability of the high-mannose-type N-glycans, which prevail at all glycosylation sites, depending on the culture conditions and the cell line expressing the enzyme, overview. The composition of the glycans is largely determined by substantial trimming in the medium, the susceptibility for trimming is different for the glycans at the three N-glycosylation sites, which of the glycans is most susceptible to trimming also depends on production conditions. Structure and ligand binding analysis, overview