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Literature summary for 3.1.6.1 extracted from

  • Virgens, M.Y.; Pol-Fachin, L.; Verli, H.; Saraiva-Pereira, M.L.
    Effects of glycosylation and pH conditions in the dynamics of human arylsulfatase A (2014), J. Biomol. Struct. Dyn., 32, 567-579.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N350S mutant exhibits a consistent degree of unfolding, which may be related to its in vitro reduced stability Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
Homo sapiens 5764
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P15289
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein lowering pH and increasing glycosylation reduces the flexibility of the enzyme. At acidic pH, the glycosylated enzyme presents a higher secondary conformational stability when compared to its nonglycosylated counterpart Homo sapiens

Synonyms

Synonyms Comment Organism
ARSA
-
Homo sapiens

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
lowering pH and increasing glycosylation reduces the flexibility of the enzyme. At acidic pH, the glycosylated enzyme presents a higher secondary conformational stability when compared to its nonglycosylated counterpart Homo sapiens