Information on EC 2.8.2.32 - scymnol sulfotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.8.2.32
-
RECOMMENDED NAME
GeneOntology No.
scymnol sulfotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + 5beta-scymnol = adenosine 3',5'-bisphosphate + 5beta-scymnol sulfate
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenosine 5'-phosphosulfate:5beta-scymnol sulfotransferase
The enzyme from the shark Heterodontus portusjacksoni is able to sulfate the C27 bile salts 5beta-scymnol (the natural bile salt) and 5alpha-cyprinol (the carp bile salt). Enzyme activity is activated by Mg2+ but inhibited by the product 5beta-scymnol sulfate.
CAS REGISTRY NUMBER
COMMENTARY hide
220591-70-4
-
9032-76-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Trygonoptera sp.
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenosine 5'-phosphosulfate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5-beta-cholestane-27-yl
adenosine 3',5'-diphosphate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-yl sulfate
show the reaction diagram
-
trivial name 5beta-scymnol
trivial name 5beta-scymnol sulfate
-
?
3'-phosphoadenosine 5'-phosphosulfate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-ol
adenosine 3',5'-diphosphate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-sulfate
show the reaction diagram
3'-phosphoadenosine 5'-phosphosulfate + 5alpha-cyprinol
adenosine 3',5'-diphosphate + 5alpha-cyprinol sulfate
show the reaction diagram
3'-phosphoadenosine 5'-phosphosulfate + 5beta-scymnol
adenosine 3',5'-diphosphate + 5beta-scymnol sulfate
show the reaction diagram
3'-phosphoadenosine 5'-phosphosulfate + testosterone
adenosine 3',5'-diphosphate + testosterone sulfate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenosine 5'-phosphosulfate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-ol
adenosine 3',5'-diphosphate + (24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-sulfate
show the reaction diagram
3'-phosphoadenosine 5'-phosphosulfate + 5beta-scymnol
adenosine 3',5'-diphosphate + 5beta-scymnol sulfate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 3',5'-diphosphate
adenosine-3',5'-diphosphate
EDTA
-
50 mM, 89% inhibition
iodoacetate
-
0.1 mM, 99% inhibition
iodoacetic acid
p-chloromercuribenzoate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018
(24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5-beta-cholestane-27-ol
Trygonoptera sp.
-
-
0.003 - 0.013
(24R)-3alpha,7alpha,12alpha,24,26-pentahydroxy-5beta-cholestane-27-ol
0.0044
3'-phosphoadenosine 5'-phosphosulfate
-
room temperature, pH 6.5
0.004
3'-phosphoadenosine-5'-phosphosulfate
-
pH 6.5
0.014
5beta-scymnol
-
pH 6.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037 - 0.00084
adenosine 3',5'-diphosphate
0.00054
adenosine 3'-5'-diphosphate
-
-
0.00098 - 0.019
adenosine-3',5'-diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000026
Trygonoptera sp.
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
Trygonoptera sp.
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 37
Trygonoptera sp.
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing, probably two isoenzymes
5.85
-
isoelectric focusing, probably two isoenzymes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
gel filtration; native PAGE, probably two isoenzymes
45000
-
native PAGE, probably two isoenzymes
66000
-
gel filtration
69000
Trygonoptera sp.
-
gel filtration
80000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 40000, SDS-PAGE, probably two isoenzymes; 1 * 45000, SDS-PAGE, probably two isoenzymes
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freeze-thawing reduces activity, enzyme has very low stability at 4C especially during concentration procedures
-
inactivated by repeated thawing and freezing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, at least 12 months, no loss of activity
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-80C, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydroxyapatite, DEAE-Sephacel, Sephadex G-100, partially purified
-
hydroxylapatite, DEAE-Sephacel
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hydroxylapatite, Sephadex G-100
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hydroxylapatite, Sephadex G-100, partially purified
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Sephadex G-100, hydroxylapatite
Trygonoptera sp.
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