3.1.6.4: N-acetylgalactosamine-6-sulfatase
This is an abbreviated version!
For detailed information about N-acetylgalactosamine-6-sulfatase, go to the full flat file.
Word Map on EC 3.1.6.4
-
3.1.6.4
-
mucopolysaccharidosis
-
lysosomal
-
morquio
-
keratan
-
glycosaminoglycans
-
dysplasia
-
chondroitin-6-sulfate
-
sulfatases
-
arylsulfatase
-
elosulfase
-
n-acetylgalactosamine-4-sulfatase
-
medicine
-
kyphoscoliosis
-
odontoid
-
sumf1
-
synthesis
-
sanfilippo
-
pectus
-
platyspondyly
-
carinatum
-
valgum
- 3.1.6.4
- mucopolysaccharidosis
- lysosomal
- morquio
- keratan
- glycosaminoglycans
- dysplasia
- chondroitin-6-sulfate
-
sulfatases
- arylsulfatase
-
elosulfase
- n-acetylgalactosamine-4-sulfatase
- medicine
-
kyphoscoliosis
-
odontoid
- sumf1
- synthesis
-
sanfilippo
-
pectus
-
platyspondyly
-
carinatum
-
valgum
Reaction
Synonyms
6-sulfatase, acetylgalactosamine 6-sulfatase, AtsA2, chondroitin sulfatase, chondroitinase, chondroitinsulfatase, galactose-6-sulfatase, galactose-6-sulfate sulfatase, GalNAc6S sulfatase, GALNS, N-acetylgalactosamine 6-sulfatase, N-acetylgalactosamine 6-sulphate sulphatase, N-acetylgalactosamine-6-sulfatase, N-acetylgalactosamine-6-sulfate sulfatase, sulfatase, acetylgalactosamine 6-, sulfatase, chondroitin
ECTree
Advanced search results
Application
Application on EC 3.1.6.4 - N-acetylgalactosamine-6-sulfatase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
medicine
synthesis
-
diagnosis of Morquio disease since extracts of Morquio fibroblasts are devoid of the enzyme
medicine
-
Morquio A is an autosomal recessive disease caused by the deficiency of N-acetylgalactosamine-6-sulfate sulfatase, leading to the lysosomal accumulation of keratan-sulfate and chondroitin-6-sulfate
medicine
application of a combined assay for defects in iduronate-2-sulfatase (ID2S) leading to mucopolysaccharidosis II, and N-acetylgalactosamine-6-sulfatase (GALN) and N-acetylgalactosamine-4-sulfatase (ARSB) defects related to mucopolysaccharidosis IVA and MPS VI, respectively. The average enzyme activities of ID2S, GALN, and ARSB in random neonates are 19.6, 1.7, and 13.4 micromol/h/l, respectively. The average enzyme activities of ID2S, GALN, and ARSB in disease-affected individuals are 0.5, 0.3, and 0.3 micromol/h/l, respectively
medicine
GALNS activity (nmol/17 h/mg protein) is 0-7.4 in samples from mucopolysaccharidosis type IVA patients, as 19.85-93.7 in their parents and as 38.4-164 in the healthy controls. Statistically significant differences are observed between the three groups in terms of enzyme activity. There are no significant differences in enzyme activity by age. The female subjects in both the patient and parents groups show lower enzyme activity compared to the male subjects
medicine
in human prostate cancer tissues, the N-acetylgalactosamine-4-sulfatase ARSB activity is reduced and the galactosamine-N-acetyl-6-sulfatase GALNS activity is increased, compared to normal prostate tissue
production and characterization of an active recombinant N-acetylgalactosamine-6-sulfate sulfatase in Escherichia coli BL21. When native signal peptide is present, higher enzyme activity levels are observed in both soluble and inclusion bodies fractions, and signal peptide removal has a significant impact on enzyme activation. Enzyme activity in the culture media is only detected when signal peptide is presented and the culture is carried out under semi-continuous mode
synthesis
increase of recombinant GALNS activity produced in Escherichia coli is obtained with a promoter regulated under sigmas. Additional improvements are observed when osmotic shock is applied. Overexpression of chaperones has no effect on recombinant GALNS activity. High concentrations of sucrose in conjunction with the physiological-regulated promoter proUmod significantly increase the GALNS production and activity
synthesis
removal of the native signal peptide and coexpression with human formylglycine-generating enzyme SUMF1 in Pichia pastoris allow an improvement of 4.5fold in the specific GALNS activity. Recombinant GALNS shows a high stability at 4°C, while the activity is markedly reduced at 37 and 45°C. Recombinant GALNS is taken-up by HEK-293 cells and human skin fibroblasts in a dose-dependent manner, without any additional protein or host modification