3.1.6.12: N-acetylgalactosamine-4-sulfatase
This is an abbreviated version!
For detailed information about N-acetylgalactosamine-4-sulfatase, go to the full flat file.
Word Map on EC 3.1.6.12
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3.1.6.12
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mucopolysaccharidosis
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lysosomal
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maroteaux-lamy
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glycosaminoglycans
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arylsulfatase
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dermatan
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feline
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rhasb
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medicine
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galsulfase
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sulfatases
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stair
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enzyme-replacement
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mps-vi
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dysostosis
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diagnostics
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nutrition
- 3.1.6.12
- mucopolysaccharidosis
- lysosomal
-
maroteaux-lamy
- glycosaminoglycans
- arylsulfatase
- dermatan
- feline
-
rhasb
- medicine
-
galsulfase
-
sulfatases
-
stair
-
enzyme-replacement
-
mps-vi
- dysostosis
- diagnostics
- nutrition
Reaction
Synonyms
4-sulfatase, 4-sulphatase, acetylgalactosamine 4-sulfatase, ARSB, arylsulfatase B, ASB, chondroitinase, chondroitinsulfatase, chondrosulfatase, G4S, gastric chondrosulfohydrolase, N-acetylgalactosamine 4-sulfatase, N-acetylgalactosamine 4-sulfate sulfohydrolase, N-acetylgalactosamine-4-sulfatase, N-acetylgalactosamine-4-sulphatase, sulfatase, acetylgalactosamine 4-
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Posttranslational Modification
Posttranslational Modification on EC 3.1.6.12 - N-acetylgalactosamine-4-sulfatase
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glycoprotein
phosphoprotein
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compared to 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
proteolytic modification
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33% of the intracellular Y210C mutant enzyme remains as a precursor form, for at least 8 h post labeling and is not processed to the mature lysosomal form. A significant amount of the mutant enzyme escapes the endoplasmic reticulum and is either secreted from the expression cells or undergoes delayed intracellular traffic. 67% of the intracellular Y210C mutant enzyme is processed to the mature form by a proteolytic processing step known to occur in lysosomes
additional information
conversion of an active-site cysteine into a formylglycine
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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