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3.1.6.8: cerebroside-sulfatase

This is an abbreviated version!
For detailed information about cerebroside-sulfatase, go to the full flat file.

Word Map on EC 3.1.6.8

Reaction

a cerebroside 3-sulfate
+
H2O
=
a cerebroside
+
sulfate

Synonyms

ARS, arylsulfatase A, sulfatase, cerebroside, cerebroside sulfatase, cerebroside sulfate sulfatase, arylsulfatase E, ASA, Cerebroside-sulfatase, ARSA, AS-A, arylsulfatase-A

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.6 Sulfuric-ester hydrolases
                3.1.6.8 cerebroside-sulfatase

Engineering

Engineering on EC 3.1.6.8 - cerebroside-sulfatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E253K
mutation contributes to enzyme activity reduction
H231Q
mutation identified in three patients belonging to a consanguineous family with late-infantile metachromatic leukodystrophy disorder MLD. The mutation leads to changes in the pre-mRNA secondary structure and in the ArsA protein structure
C300F
-
the sequence alteration is found in a patient with metachromatic leukodystrophy, the mutant strongly interferes with the octamerization process of enzyme but not with its dimerization capacity
P425T
-
the sequence alteration is found in a patient with metachromatic leukodystrophy, the mutant displays a modest reduction of oligomerization process but not with its dimerization capacity
C69A
The inactive mutant in complex with p-nitrocatechol sulfate mimics a reaction intermediate during sulfate ester hydrolysis by the active enzyme, without the covalent bond to the key side-chain C-alpha-formylglycine
P426L
mutation contributes to enzyme activity reduction
N350S
A96G
mutation contributes to enzyme activity reduction
P426L/N350S/96A>G
mutations contribute to sum of the enzyme activity reduction ascribed to each mutation
R496H
R288H
R288H/R496H/N350S
-
about 38% reduction of enzyme activity in comparison to wild-type enzyme, no additive effect of the various amino acid substitutions is found in vitro
E382Q
C500F
K302A
K367A
K393A
K393A/K395G
K393A/K395H
K433A
K457S
K457G
K457R
K463R
K463Q
N158Q/N350Q
T391S
mutation contributes to enzyme activity reduction
E253K/T391S
mutations contribute to sum of the enzyme activity reduction ascribed to each mutation
E307K
naturally occuring ARSA polymorphism, causes a mild peripheral neuropathy phenotype
G293C
mutant shows 0.5% of wild type ARSA activity
C493F
mutant shows 0.7% of wild type ARSA activity
L52P
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
H138D
naturally occuring ARSA polymorphism, causes a mild peripheral neuropathy phenotype
C168stop
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
A212P
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
T304M
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
S406G
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
D407fs
naturally occuring ARSA polymorphism, causes a severe peripheral neuropathy phenotype
P377L
-
inactive misfolded mutant P377L-pdASA
D335V
-
inactive misfolded mutant D335V-ASA
T275M
-
inactive misfolded mutant T275M-ASA
P136L
-
inactive misfolded mutant P136LASA
G86D
-
inactive misfolded mutant G86D-ASA
T201C
-
inactive misfolded mutant T201C-ASA
D255H
-
inactive misfolded mutant D255H-ASA
C69A
site-directed mutagenesis, the mnutant shows abolished enzyme activity and only residual binding to thr sulfoglycolipid substrate
C69A/K123A/K302A
site-directed mutagenesis, the mutant shows abolished substrate binding and activity
additional information