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3.1.6.1: arylsulfatase (type I)

This is an abbreviated version!
For detailed information about arylsulfatase (type I), go to the full flat file.

Word Map on EC 3.1.6.1

Reaction

an aryl sulfate
+
H2O
=
a phenol
+
sulfate

Synonyms

4-methylumbelliferyl sulfatase, ARS, ARS-A, ARS-B, ARSA, ARSB, ARSE, ARSK, ary 423, Aryl-sulfate sulphohydrolase, arylsufatase B, arylsulfatase, arylsulfatase A, arylsulfatase B, arylsulfatase E, arylsulfatase Es-2, arylsulfatase G, arylsulfatase gene, arylsulfatase III, arylsulfatase J, arylsulfatase K, arylsulfatase type VI, arylsulfate sulfohydrolase II, arylsulfohydrolase, arylsulphatase, arylsulphatase A, AS-A, ASG, AstA, AtsA, estrogen sulfatase, KIAA1001, nitrocatechol sulfatase, p-nitrophenyl sulfatase, P70, PAS, phenolsulfatase, phenylsulfatase, sulfatase, sulfatase, aryl-

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.6 Sulfuric-ester hydrolases
                3.1.6.1 arylsulfatase (type I)

Engineering

Engineering on EC 3.1.6.1 - arylsulfatase (type I)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C80A
about 20% of wild-type activity at neutral pH, about 5% of wild-type activity at pH optimum
G137A
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
I40S
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
N350S
mutant exhibits a consistent degree of unfolding, which may be related to its in vitro reduced stability
P578S
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
T409M
-
the mutation is associated with X-linked recessive chondrodysplasia punctata
W124G
-
naturally occurring missense mutation causing ARSA deficiency, isolated from two Tunisian patients with late infantile metachromatic leukodystrophy, MLD
N215Q
residue Asn215 functions as glycosylation site
N356Q
residue Asn356 functions as glycosylation site
N497Q
mutation of glycosylation site N497 abrogates transport to lysosomes, due to impaired mannose 6-phosphate modification
H260L
mutant displays increased thermostability and increased half-life at 55°C
K253H/H260L
7.7fold increase in half-life compared to wild-type
K253N
mutant shows enhanced thermal stability
P314T
mutant shows enhanced thermal stability
C51A
-
mutant with strongly reduced activity
C51S
-
mutant with strongly reduced activity
M72Q
-
2fold increase in activity compared with starting mutant G138S
additional information