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Information on EC 3.1.6.12 - N-acetylgalactosamine-4-sulfatase and Organism(s) Rattus norvegicus and UniProt Accession P50430
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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: Rattus norvegicus
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosamine 4-sulfatase
-
-
-
-
arylsulfatase B
ASB
chondroitinase
-
-
-
-
chondroitinsulfatase
-
-
-
-
G4S
-
-
-
-
N-acetylgalactosamine 4-sulfate sulfohydrolase
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-
-
-
N-acetylgalactosamine-4-sulfatase
-
-
-
-
sulfatase, acetylgalactosamine 4-
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-
-
-
arylsulfatase B
-
-
-
-
ASB
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
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-
-
-
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 + H2O
chondroitin + sulfate
-
-
-
-
?
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
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)2 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)2 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)3 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine)3 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)4 + H2O
N-acetylgalactosamine-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)4 + sulfate
-
only the 4-sulfated endgroup is attacked by the enzyme
-
-
?
N-acetylgalactosamine 4-sulfate-beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate + H2O
N-acetylgalactosamine-beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate + sulfate
-
-
-
-
?
N-acetylglucosamine 4-sulfate + H2O
N-acetylglucosamine + sulfate
-
-
-
-
?
additional information
?
-
-
ARSB removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate and dermatan sulfate
-
-
?
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
-
-
?
additional information
?
-
-
ARSB removes 4-sulfate groups from the nonreducing end of chondroitin-4-sulfate and dermatan sulfate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
astrocyte treatment with ethanol inhibits the activity of arylsulfatase B, and triggers the degradation of chondroitin-4-sulfate, increases total sulfated glycosaminoglycans, chondroitin-4-sulfate and neurocan core-protein content and inhibits neurite outgrowth in neurons cocultured with ethanol-treated astrocytes in vitro. Ethanol also inhibits arylsulfatase B activity and increases sulfated glycosaminoglycans and neurocan levels in the developing hippocampus after in vivo ethanol exposure
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)2
-
-
0.049
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)3
-
-
0.064
N-acetylgalactosamine 4-sulfate-(beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate)4
-
-
0.027
N-acetylgalactosamine 4-sulfate-beta-glucuronosyl-(1-3)-N-acetylgalactosamine 4-sulfate
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in post-natal ventral rat prostate, a distinct and reciprocal localization of arylsulfatase B and N-acetylgalactosamine-6-sulfatase is seen, with arylsulfatase B predominant in the stroma and N-acetylgalactosamine-6-sulfatase predominant in the epithelium. Control arylsulfatase B activity increases significantly between days 5 and 30, but following estrogen exposure, activity is reduced and the observed increase on day 30 is inhibited
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
silencing or overexpression of ASB in normal rat kidney epithelial cells in tissue culture modifies the content of total sulfated glycosaminoglycans, C4S, kininogen, and bradykinin in spent media and cell lysates. Treatment of the cultured cells with chondroitinase ABC also increases the secretion of bradykinin into the spent media and reduces the C4S-associated kininogen. When ASB is overexpressed, the cellular kininogen that associates with C4S declines, suggesting a vital role for chondroitin-4-sulfation in regulating the kininogen-C4S interaction
physiological function
physiological function
astrocyte treatment with ethanol inhibits the activity of arylsulfatase B, and triggers the degradation of chondroitin-4-sulfate, increases total sulfated glycosaminoglycans, chondroitin-4-sulfate and neurocan core-protein content and inhibits neurite outgrowth in neurons cocultured with ethanol-treated astrocytes in vitro. Ethanol also inhibits arylsulfatase B activity and increases sulfated glycosaminoglycans and neurocan levels in the developing hippocampus after in vivo ethanol exposure. Arylsulfatase B silencing increases the levels of sulfated glycosaminoglycans, chondroitin-4-sulfate, and neurocan in astrocytes and inhibits neurite outgrowth in cocultured neurons
physiological function
in post-natal ventral rat prostate, a distinct and reciprocal localization of arylsulfatase B and N-acetylgalactosamine-6-sulfatase is seen, with arylsulfatase B predominant in the stroma and N-acetylgalactosamine-6-sulfatase predominant in the epithelium. Control arylsulfatase B activity increases significantly between days 5 and 30, but following estrogen exposure, activity is reduced and the observed increase on day 30 is inhibited
physiological function
-
arylsulfatase B regulates interaction of chondroitin-4-sulfate and kininogen in renal epithelial cells. ASB activity may provide a link between salt responsiveness and the bradykinin-associated mechanism of blood pressure regulation
physiological function
-
ASB, owing to its effect on chondroitin-4-sulfation, impacts on the kininogen-bradykinin axis and, thereby, may influence blood pressure
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_RAT
528
0
58959
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ASB silencing or overexpression, silencing leads to reduced ASB activity, which than leads to increased chondroitin-4-sulfation, increased binding of kininogen, and reduced bradykinin release
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
in the renal tissue of Dahl salt-sensitive rats exposed to high salt diet, arylsulfatase B activity is significantly less than in Dahl salt-sensitive rats exposed to low salt diet, and chondroitin-4-sulfate and total sulfated glycosaminoglycan content are significantly greater. A marked increase in chondroitin-4-sulfate disaccharidesis observed in the renal tissue of the rats exposed to high salt diet. Unsulfated, hyaluronan-derived disaccharides are increased in the rats on the low salt diet. In the rats on high salt diet, with lower arylsulfatase B activity and higher chondroitin-4-sulfate levels, cell-bound, high-molecular weight kininogen is greater and urinary bradykinin is lower. Arylsulfatase B activity in renal tissue and normal rat kidney cells declines when exogenous chloride concentration is increased in vitro
nutrition
in the renal tissue of Dahl salt-sensitive rats exposed to high salt diet, arylsulfatase B activity is significantly less than in Dahl salt-sensitive rats exposed to low salt diet, and chondroitin-4-sulfate and total sulfated glycosaminoglycan content are significantly greater. A marked increase in chondroitin-4-sulfate disaccharidesis observed in the renal tissue of the rats exposed to high salt diet. Unsulfated, hyaluronan-derived disaccharides are increased in the rats on the low salt diet. In the rats on high salt diet, with lower arylsulfatase B activity and higher chondroitin-4-sulfate levels, cell-bound, high-molecular weight kininogen is greater and urinary bradykinin is lower. Arylsulfatase B activity in renal tissue and normal rat kidney cells declines when exogenous chloride concentration is increased in vitro
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liau, Y.H.; Galicki, N.I.; Horowitz, M.I.
Heterogeneity of rat rib chondroitin sulfate and susceptibility to rat gastric chondrosulfatase
Glycoconjugate research, Metabolic disorders and degradation, (Gregery, J. P. ; Jeanlaz, R. W. , ed. )
2
907-908
1979
Rattus norvegicus
-
Liau, Y.H.; Galicki, N.I.; Horowitz, M.I.
Heterogeneity of rat rib chondroitin sulfate and susceptibility to rat gastric chondrosulfatase
Biochim. Biophys. Acta
539
315-323
1978
Rattus norvegicus
Wojczyk, B.S.; Hoja, D.A.; Litynska, A.M.
Purification of lysosomal arylsulfatase B from rat liver and its reactivity with lectins in affinity immunoelectrophoresis
Int. J. Biochem.
24
1561-1571
1992
Rattus norvegicus
Habuchi, H.; Tsuji, M.; Nakanishi, Y.; Suzuki, S.
Separation and properties of five glycosaminoglycan sulfatases from rat skin
J. Biol. Chem.
254
7570-7578
1979
Rattus norvegicus
Bhattacharyya, S.; Kotlo, K.; Danziger, R.; Tobacman, J.K.
Arylsulfatase B regulates interaction of chondroitin-4-sulfate and kininogen in renal epithelial cells
Biochim. Biophys. Acta
1802
472-477
2010
Homo sapiens, Rattus norvegicus
Zhang, X.; Bhattacharyya, S.; Kusumo, H.; Goodlett, C.R.; Tobacman, J.K.; Guizzetti, M.
Arylsulfatase B modulates neurite outgrowth via astrocyte chondroitin-4-sulfate: dysregulation by ethanol
Glia
62
259-271
2014
Rattus norvegicus (P50430)
Kotlo, K.; Bhattacharyya, S.; Yang, B.; Feferman, L.; Tejaskumar, S.; Linhardt, R.; Danziger, R.; Tobacman, J.K.
Impact of salt exposure on N-acetylgalactosamine-4-sulfatase (arylsulfatase B) activity, glycosaminoglycans, kininogen, and bradykinin
Glycoconj. J.
30
667-676
2013
Rattus norvegicus (P50430)
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