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3.1.6.2: steryl-sulfatase

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

Word Map on EC 3.1.6.2

Reaction

3beta-hydroxyandrost-5-en-17-one 3-sulfate
+
H2O
=
3beta-hydroxyandrost-5-en-17-one
 +
sulfate

Synonyms

3-beta-hydroxysteroid sulfate sulfatase, arylsufatase, arylsulfatase C, ASC, AtsA, cholesterol sulfate sulfohydrolase, CHS-ase, dehydroepiandrosterone sulfatase, dehydroepiandrosterone sulfate sulfatase, DHEAS, E1-STS, ES, estrone sulfatase, More, neurosteroid sulfatase, NSS, oestrone sulfatase, phenolic steroid sulfatase, pregnenolone sulfatase, steroid 3-sulfatase, steroid sulfatase, steroid sulfate sulfohydrolase, steroid sulphatase, sterol sulfatase, sterolsulfate sulfohydrolase, Steryl-sulfate sulfohydrolase, STS, sulfatase, sterol

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.6 Sulfuric-ester hydrolases
                3.1.6.2 steryl-sulfatase

Engineering

Engineering on EC 3.1.6.2 - steryl-sulfatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C446Y
-
patient with X-linked ichthyosis
DELTA1-21
lacks 21 N-terminal amino acids, that encode the signal peptide, reduced STS activity
DELTA185-583
lacks 399 C-terminal amino acids, reduced STS activity
H136F
point mutation in histidine 136, reduced STS activitiy
H136W
point mutation in histidine 136, reduced STS activity
H136Y
point mutation in histidine 136, reduced STS activity
H444R
-
patient with X-linked ichthyosis
N259Q
point mutation in asparagine 259 glycosylation site, reduced STS activity
N333Q
point mutation in other potential glycosylation site asparagine 333, no reduced STS activity
N459Q
point mutation in other potential glycosylation site asparagine 459, no reduced STS activity
N47Q
point mutation in asparagine 47 glycosylation site, reduced STS activity
N47Q/N259Q
double mutation in asparagine 47 and 259 glycosylation sites, reduced STS activity
N54Q
point mutation in in asparagine 54 non-glycosylation site , no reduced STS activity
P212G
point mutation in proline 212, no reduced STS activity
Q560P
-
no effect of mutation on enzyme synthesis and degradation, dominant negative effect on enzyme activity when coexisting with wild-type enzyme
R419S
-
patient with X-linked ichthyosis
S341L
-
patient with X-linked ichthyosis
W372P
-
patient with X-linked ichthyosis
W372R
-
patient with X-linked ichthyosis
I156L/K158E/L325F
140fold increase in catalyticefficiency, 3.5 degrees increase in melting temperature at pH 9.0
I156V/L157V/K158I/K330V
140fold increase in catalyticefficiency
K330V
catalytic efficiency similar to wild-type
R155P
2.5fold increase in catalyticefficiency
R155P/I156V/L325F/K330V
30fold increase in catalyticefficiency, 3.5 degrees increase in melting temperature at pH 9.0
R155P/K330V
5fold increase in catalyticefficiency
R155P/L157V/K158I/K330V
150fold increase in catalyticefficiency
R155T
2fold increase in catalyticefficiency
R155TK330V
2fold increase in catalyticefficiency
K330V
-
catalytic efficiency similar to wild-type
-
R155P
-
2.5fold increase in catalyticefficiency
-
R155P/K330V
-
5fold increase in catalyticefficiency
-
R155T
-
2fold increase in catalyticefficiency
-
R155TK330V
-
2fold increase in catalyticefficiency
-
additional information