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Information on EC 3.1.6.12 - N-acetylgalactosamine-4-sulfatase and Organism(s) Mus musculus and UniProt Accession P50429
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3.1.6.12 N-acetylgalactosamine-4-sulfataseIUBMB Comments
Acts also on N-acetylglucosamine 4-sulfate.
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Word Map
- 3.1.6.12
- mucopolysaccharidosis
- lysosomal
-
maroteaux-lamy
- glycosaminoglycans
- arylsulfatase
- dermatan
- feline
-
rhasb
- medicine
-
galsulfase
-
sulfatases
-
stair
-
enzyme-replacement
-
mps-vi
- dysostosis
- diagnostics
- nutrition
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
n-acetylgalactosamine-4-sulfatase, 4-sulfatase, 4-sulphatase, n-acetylgalactosamine 4-sulfatase, n-acetylgalactosamine-4-sulphatase, chondrosulfatase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosamine 4-sulfatase
-
-
-
-
arylsulfatase B
ASB
chondroitinase
-
-
-
-
chondroitinsulfatase
-
-
-
-
G4S
-
-
-
-
N-acetylgalactosamine 4-sulfate sulfohydrolase
-
-
-
-
N-acetylgalactosamine-4-sulfatase
-
-
-
-
sulfatase, acetylgalactosamine 4-
-
-
-
-
arylsulfatase B
-
-
-
-
ASB
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase
Acts also on N-acetylglucosamine 4-sulfate.
CAS REGISTRY NUMBER
COMMENTARY
55354-43-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chondroitin 4-sulfate-heptasaccharide + H2O
chondroitin 4-sulfate-heptasaccharide + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate + H2O
N-acetyl-D-galactosamine + sulfate
-
-
-
-
?
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
p-nitrocatechol sulfate + H2O
p-nitrocatechol + sulfate
-
enzymes catalyze in addition to reaction of EC 3.1.6.12 also arylsulfatase reaction , see also EC 3.1.6.1
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-D-galactosamine 4-sulfate units + H2O
N-acetyl-D-galactosamine units + sulfate
-
acts also on N-acetylglucosamine 4-sulfate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
p-nitrocatechol sulfate
-
pH 7.4, 37°C, enzyme from animals infected with Schistosoma mansoni
3.9
p-nitrocatechol sulfate
-
pH 7.4, 37°C, enzyme from animals without infection
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
enzyme from animals without infection, maximal activity is about 60% of the activity of the enzyme from animals infected with Schistosoma mansoni
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 8
-
pH 4.8: about 80% of maximal activity, pH 8.0: about 60% of maximal activity, enzyme from animals infected with Schistosoma mansoni
5 - 7
-
pH 5.0: about 20% of maximal activity, pH 7.0: about 55% of maximal activity enzyme from animals without infection
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ARSB is extensively expressed and distributed in the entire spinal cord. Expression in anterior horn of gray matter is significantly higher than that in the posterior horn of gray matter and significantly higher than that in the central canal. ARSB is mainly distributed in the microglia and neuron cells in the wild-type mice
-
of animals infected with Schistosoma mansoni. The infection causes a significant increase in activity of arylsulfatase B
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
a decline in ARSB activity increases transmembrane glycoprotein NMB expression. Protein tyrosine phosphatase SHP2 activity declines due to increased binding with chondroitin 4-sulfate when ARSB is reduced. When SHP2 activity is inhibited, phosphorylations of p38 mitogen-associated phosphokinase and of microphthalmia-associated transcription factor increase, leading to transmembrane glycoprotein NMB promoter activation. In contrast, constitutively active SHP2 and overexpression of ARSB inhibit NMB expression
physiological function
abnormal expression and distribution of ARSB are closely associated with the neuron death in the superoxide dismutase mutant G93A transgenic mice. ARSB participates in the pathogenesis of amyotrophic lateral sclerosis (ALS), the relative deficiency of ARSB expression and redistribution in the anterior horn of gray matter and the posterior horn of gray matter of spinal cord in ALS-like superoxide dismutase G93A transgenic mice is closely associated with the neuron death
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ARSB_MOUSE
534
0
59647
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9
-
maximal thermal stability at pH 5.9, rapid decline above pH 6 and below pH 5
135541
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 70
-
pH 6.0, the enzyme from animals infected with Schistosoma mansoni shows more stability than that of the control, the stability at 50°C is identical to the enzyme from control
60
65
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daniel, W.L.; Ruoff, B.M.; Thompson, D.B.
Purification and properties of arylsulfatase B from high- and low-activity mouse strains
Biochem. Genet.
23
771-786
1985
Mus musculus
Daniel, W.L.; Caplan, M.S.
Comparative biochemistry of murine arylsulfatase B
Biochem. Genet.
18
625-642
1980
Mus musculus
Balbaa, M.; El-Kersh, M.; Mansour, H.; Yacout, G.; Isamil, M.; malky, A.; Bassiouny, K.; Abdel-Monem, N.; Kandeel, K.
Activity of some hepatic enzymes in Schistosomiasis and concomitant alterations of arylsulfatase B
J. Biochem. Mol. Biol.
37
223-228
2004
Mus musculus
Balbaa, M.; Bassiouny, K.
In vitro effect of schistosomicidal drugs on hepatic arylsulfatase B from the schistosoma-infected mouse
J. Enzyme Inhib. Med. Chem.
21
81-85
2006
Mus musculus
Zhang, J.; Liang, H.; Zhu, L.; Gan, W.; Tang, C.; Li, J.; Xu, R.
Expression and distribution of arylsulfatase B are closely associated with neuron death in SOD1 G93A transgenic mice
Mol. Neurobiol.
55
1323-1337
2018
Mus musculus (P50429)
Bhattacharyya, S.; Feferman, L.; Tobacman, J.
Inhibition of phosphatase activity follows decline in sulfatase activity and leads to transcriptional effects through sustained phosphorylation of transcription factor MITF
PLoS ONE
11
e0153463
2016
Homo sapiens (P15848), Mus musculus (P50429)
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