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Literature summary extracted from

  • Yaghootfam, A.; Schestag, F.; Dierks, T.; Gieselmann, V.
    Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-phosphotransferase (2003), J. Biol. Chem., 278, 32653-32661.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.6.8 plasmids containing the wild-type and mutant cDNAs are transiently transfected into BHK cells Homo sapiens
3.1.6.8 wild-type and mutant enzymes transiently transfected into BHK cells Homo sapiens
3.1.6.12 wild-type and mutant enzymes transiently transfected into BHK cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.6.8 K302A 34% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K302A 34% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium Homo sapiens
3.1.6.8 K367A 60% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K367A 60% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 106% of the mannose-phosphorylation of the wild-type enzyme Homo sapiens
3.1.6.8 K393A 39% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K393A 39% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 123% of the mannose-phosphorylation of the wild-type enzyme Homo sapiens
3.1.6.8 K393A/K395G 35% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K393A/K395G 35% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium Homo sapiens
3.1.6.8 K393A/K395H 30% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K393A/K395H 30% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium Homo sapiens
3.1.6.8 K433A 102% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K433A 102% of the activity of wild-type enzyme when expressed in BHK cells. Mutation has no effect on distribution of the enzyme activity between cell and medium. 95% of the mannose-phosphorylation of the wild-type enzyme Homo sapiens
3.1.6.8 K457G 7.5% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K457G 7.5% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 60% of total activity compared to 35% of the wild-type enzyme. 31% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158 Homo sapiens
3.1.6.8 K457R 45% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K457R 45% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 60% of total activity compared to 35% of the wild-type enzyme. 33% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158 Homo sapiens
3.1.6.8 K457S 25% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K457S 25% of the activity of wild-type enzyme when expressed in BHK cells. 50% of the mannose-phosphorylation of the wild-type enzyme. Mutation leads to an increase of enzyme activity in the medium to about 65% of total activity compared to 35% of the wild-type enzyme. 50% of the mannose-phosphorylation of the wild-type enzyme. Mutation affects phosphorylation of oligosaccharide Asn350 to a greater extent than that of oligosaccharide Asn158 Homo sapiens
3.1.6.8 K463Q 14% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K463Q 14% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an decrease of enzyme activity in the medium to about 25% of total activity compared to 35% of the wild-type enzyme Homo sapiens
3.1.6.8 K463R 39% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 K463R 39% of the activity of wild-type enzyme when expressed in BHK cells. 31% of the mannose-phosphorylation of the wild-type enzyme. Mutation leads to an decrease of enzyme activity in the medium to about 25% of total activity compared to 35% of the wild-type enzyme Homo sapiens
3.1.6.8 additional information only substitution of Lys457 causes a reduction of phosphorylation to 33% and increases secretion of the mutant enzyme Homo sapiens
3.1.6.8 N158Q/N350Q 43% enzyme activity in comparison to wild-type enzyme Homo sapiens
3.1.6.8 N158Q/N350Q 43% of the activity of wild-type enzyme when expressed in BHK cells. Mutation leads to an increase of enzyme activity in the medium to about 25% of total activity compared to 75% of the wild-type enzyme Homo sapiens
3.1.6.12 K470A mutation leads to an decrease of enzyme activity in the medium to 13% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens
3.1.6.12 K470A/K497A/K507A mutation leads to an decrease of enzyme activity in the medium to 17% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens
3.1.6.12 K470A/K507A mutation leads to an decrease of enzyme activity in the medium to 16% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens
3.1.6.12 K497A mutation leads to an decrease of enzyme activity in the medium to 19% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens
3.1.6.12 K497A/K507A mutation leads to an decrease of enzyme activity in the medium to 18% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens
3.1.6.12 K507A mutation leads to an decrease of enzyme activity in the medium to 23% of total activity compared to 25% of the wild-type enzyme, no effect on phosphorylation Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.6.8 lysosome
-
 Homo sapiens 5764
-
3.1.6.12 lysosome
-
 Homo sapiens 5764
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.6.8 Homo sapiens
-
-
-
3.1.6.12 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.6.8 glycoprotein 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 Homo sapiens
3.1.6.8 phosphoprotein 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 Homo sapiens
3.1.6.12 glycoprotein 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 Homo sapiens
3.1.6.12 phosphoprotein 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 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.6.8 cerebroside 3-sulfate + H2O 3-O-sulfogalactosyl ceramide Homo sapiens cerebroside + sulfate galactosyl ceramide ?

Synonyms

EC Number Synonyms Comment Organism
3.1.6.8 ASA
-
 Homo sapiens
3.1.6.12 ASB
-
 Homo sapiens