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Information on EC 3.1.6.18 - glucuronate-2-sulfatase
for references in articles please use BRENDA:EC3.1.6.18
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.6 Sulfuric-ester hydrolases
3.1.6.18 glucuronate-2-sulfatase
IUBMB Comments
Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13 iduronate-2-sulfatase)
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
glucuronate-2-sulfatase, glucurono-2-sulfatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GAS
-
-
-
-
glucuronate 2-sulfatase
-
-
-
-
glucurono-2-sulfatase
-
-
-
-
sulfatase, glucuronate 2-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-O-sulfo-D-glucuronate + H2O = sulfate + D-glucuronate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of sulfuric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase
Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13 iduronate-2-sulfatase)
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CAS REGISTRY NUMBER
COMMENTARY
98597-45-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-sulfoglucuronate-N-acetylglucosamine + H2O
D-glucuronic acid N-acetylglucosamine + sulfate
Substrates: -
Products: -
Products: -
?
2-sulfoglucuronate-N-sulfoglucosamine + H2O
D-glucuronic acid N-sulfoglucosamine + sulfate
Substrates: -
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
D-glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-talitol 6-sulfate + SO42-
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: i.e. GSMS
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: enzyme removes ester sulfate from 2-position
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: i.e. O-beta-glucuronic acid 2-sulfate-1,4-O-(2,5)-anhydromannitol 6-sulfate
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: i.e. GSMS
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: i.e. heparan sulfate
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: disaccharide substrate derived from heparin
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-mannitol 6-sulfate + SO42-
-
Substrates: enzyme removes ester sulfate from 2-position
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-talitol 6-sulfate + SO42-
-
Substrates: i.e. GSTS
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-talitol 6-sulfate + SO42-
-
Substrates: i.e. O-beta-glucuronic acid 2-sulfate-1,4-O-(2,5)-anhydrotalitol 6-sulfate
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-talitol 6-sulfate + SO42-
-
Substrates: i.e. chondroitin sulfate
Products: -
Products: -
?
D-glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate + H2O
D-glucuronic acid 2,5-anhydro-D-talitol 6-sulfate + SO42-
-
Substrates: i.e. GSTS
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of iduronate 2-sulfate residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of iduronate 2-sulfate residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of iduronate 2-sulfate residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: no hydrolysis of iduronate 2-sulfate residues
Products: -
Products: -
?
additional information
?
-
Substrates: arylsulfatase K acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
NaCl
-
stimulation, over pH-range 4.2-4.8, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate, inhibits at pH 3
Zn2+
Cu2+
-
pH-dependent: over pH-range 3-4.2, inhibits at higher pH, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
above pH 4.2, activation over pH-range 3-4.2, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
Glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate
-
i.e. GSMS, substrate inhibition, above 0.004 mM
Glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate
-
i.e. GSTS, substrate inhibition, above 0.004 mM
NaCl
-
at pH 3, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate; stimulates between pH 4.2-4.8
NaH2PO4
-
glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
SO42-
-
glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate; product inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
over pH-range 2.7-5.7, maximal activation at 1 mg/ml and pH 3.3, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.7
-
20 mM sodium formate buffer, glucuronic acid 2-sulfate-2,5-anhydro-D-talitol 6-sulfate as substrate
3.3
-
60 mM sodium formate or 60 mM glycine/HCl buffer, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
additional information
-
the pH/activity profile depends on buffer composition and ionic strength, particularly at lower pH-values
3
-
glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 4.9
-
about 90% of maximal activity at pH 3 and about half-maximal activity at pH 4.9
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
-
above, major enzyme form in liver, more than 90% of liver activity, chromatofocusing
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell-lines from normal and Hunter's disease, i.e. idurono 2-sulfatase deficient individuals
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). ARSK_BOVIN
540
0
61361
Swiss-Prot
Secretory Pathway (Reliability: 1)
ARSK_CANLF
535
0
61018
Swiss-Prot
Secretory Pathway (Reliability: 3)
ARSK_CHICK
535
0
61401
Swiss-Prot
Secretory Pathway (Reliability: 3)
ARSK_DANRE
523
0
59499
Swiss-Prot
Secretory Pathway (Reliability: 2)
ARSK_HUMAN
536
1
61450
Swiss-Prot
Secretory Pathway (Reliability: 2)
ARSK_MOUSE
553
0
62801
Swiss-Prot
Secretory Pathway (Reliability: 3)
ARSK_RAT
563
0
64273
Swiss-Prot
Secretory Pathway (Reliability: 1)
ARSK_XENLA
536
0
60658
Swiss-Prot
Secretory Pathway (Reliability: 2)
C0RLG1_BRUMB
Brucella melitensis biotype 2 (strain ATCC 23457)
354
0
38500
TrEMBL
-
HEXSF_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
481
0
53650
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C80A
active site mutant lacking formylglycine, is not active with substrate 2-sulfoglucuronate-N-acetylglucosamine
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in 50 mM sodium acetate buffer, pH 5.6, 0.5 M NaCl, partially purified enzyme preparation, 10% loss of activity within 1 month, purified enzyme, t1/2: 48 h, 0.1 mg/ml bovine serum albumin stabilizes
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shaklee, P.N.; Glaser, J.H.; Conrad, H.E.
A sulfatase specific for glucuronic acid 2-sulfate residues in glycosaminoglycans
J. Biol. Chem.
260
9146-9149
1985
Gallus gallus, Homo sapiens
brenda
Freeman, C.; Hopwood, J.J.
Human liver glucuronate 2-sulphatase. Purification, characterization and catalytic properties
Biochem. J.
259
209-216
1989
Homo sapiens
brenda
Freeman, C.; Hopwood, J.J.
Glucuronate-2-sulphatase activity in cultured human skin fibroblast homogenates
Biochem. J.
279
399-405
1991
Homo sapiens
brenda
Dhamale, O.P.; Lawrence, R.; Wiegmann, E.M.; Shah, B.A.; Al-Mafraji, K.; Lamanna, W.C.; Luebke, T.; Dierks, T.; Boons, G.J.; Esko, J.D.
Arylsulfatase K is the lysosomal 2-sulfoglucuronate sulfatase
ACS Chem. Biol.
12
367-373
2017
Homo sapiens (Q6UWY0)
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.6.18)
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