Information on EC 2.8.2.25 - flavonol 3-sulfotransferase

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The expected taxonomic range for this enzyme is: Flaveria

EC NUMBER
COMMENTARY
2.8.2.25
-
RECOMMENDED NAME
GeneOntology No.
flavonol 3-sulfotransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
also acts on some other flavonol aglycones
-
-
-
3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
overview on mechanism, substrates and binding sites
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Flavone and flavonol biosynthesis
-
quercetin sulfate biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:quercetin 3-sulfotransferase
Also acts on some other flavonol aglycones.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
sulfotransferase, flavonol 3-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
121855-10-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylylsulfate + eupatin
adenosine 3',5'-bisphosphate + eupatin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + isorhamnetin
adenosine 3',5'-bisphosphate + isorhamnetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + isorhamnetin
adenosine 3',5'-bisphosphate + isorhamnetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + isorhamnetin
adenosine 3',5'-bisphosphate + isorhamnetin 3-sulfate
show the reaction diagram
-
94% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + isorhamnetin
adenosine 3',5'-bisphosphate + isorhamnetin 3-sulfate
show the reaction diagram
-
94% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + isorhamnetin
adenosine 3',5'-bisphosphate + isorhamnetin 3-sulfate
show the reaction diagram
-
10% of activity compared to quercetin
-
?
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + kaempferol 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + kaempferol 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + kaempferol 3-sulfate
show the reaction diagram
-
48% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + kaempferol
adenosine 3',5'-bisphosphate + kaempferol 3-sulfate
show the reaction diagram
-
48% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + ombuin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
37% of activity compared to rhamnetin
-
-
?
3'-phosphoadenylylsulfate + patuletin
adenosine 3',5'-bisphosphate + patuletin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + patuletin
adenosine 3',5'-bisphosphate + patuletin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + patuletin
adenosine 3',5'-bisphosphate + patuletin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + patuletin
adenosine 3',5'-bisphosphate + patuletin 3-sulfate
show the reaction diagram
-
52% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
best substrate
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
58% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
58% of activity compared to rhamnetin
-
?
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
-
best substrate
-
?
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
-
best substrate
-
?
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
-
75% of activity compared to quercetin
-
?
3'-phosphoadenylylsulfate + tamarixetin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
31% of activity compared to rhamnetin
-
-
?
additional information
?
-
-
overview on substrates
-
-
-
additional information
?
-
-
quercetagetin, gossypetin, myricetin or galangin are no substrates
-
-
-
additional information
?
-
-
involved in biosynthesis of polysulfated flavonols
-
-
-
additional information
?
-
-
involved in biosynthesis of polysulfated flavonols
-
-
-
additional information
?
-
-
first step in biosynthesis of flavonol polysulfates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
3'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
-
-
-
?
additional information
?
-
-
involved in biosynthesis of polysulfated flavonols
-
-
-
additional information
?
-
-
involved in biosynthesis of polysulfated flavonols
-
-
-
additional information
?
-
-
first step in biosynthesis of flavonol polysulfates
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
no divalent cation required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
quercetin 3-sulfate
-
noncompetitive with respect to quercetin or 3'-phosphoadenylylsulfate
quercetin 3-sulfate
-
in cultures, up to 50% decrease in enzymic activity
3',5'-diphosphoadenosine
-
competitive with respect to 3'-phosphoadenylylsulfate, noncompetitive with respect to quercetin
additional information
-
EDTA, SH-reagents at 1 and 10 mM, e.g. p-chloromercuribenzoate, iodoacetate or iodoacetamide, are not inhibitory
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00018
-
3'-phosphoadenylylsulfate
-
cosubstrate quercetin, pH 6.0
0.0002
-
3'-phosphoadenylylsulfate
-
cosubstrate rhamnetin
0.0002
-
3'-phosphoadenylylsulfate
-
cosubstrate quercetin, pH 7.5, 30C
0.0004
-
3'-phosphoadenylylsulfate
-
cosubstrate quercetin, recombinant enzyme
0.0002
-
quercetin
-
pH 6.0
0.0002
-
quercetin
-
30C, pH 7.5
0.0003
-
quercetin
-
recombinant enzyme
0.0002
-
Rhamnetin
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
and pH 8.5, two maxima
6.5
-
-
and pH 8.5, two maxima
6.5
-
-
and pH 8.5, two maxima
6.5
-
-
and pH 8.5, two maxima
8.5
-
-
and pH 6.5, two maxima
8.5
-
-
and pH 6, two maxima
8.5
-
-
and pH 6.5, two maxima
8.5
-
-
and pH 6.5, two maxima
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 34500, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H118A
-
strong reduction of catalytic activity
H118E
-
strong reduction of catalytic activity
K59A
-
300fold decrease in specific activity, K59 is not required for cosubstrate binding
K59R
-
K59 interacts with 5-portion of the nucleotide, involved in proper orientation of the phosphosulfate group
K59R
-
15-fold decrease in specific activity, K59 is not required for cosubstrate binding
R140K
-
no effect on protein stability, strong reduction of specific activity
R140S
-
no effect on protein stability, strong reduction of specific activity
R141K
-
R141 interacts with 5-portion of the nucleotide
R276A/T73A
-
marked decrease in specific activity, involved in binding of cosubstrate
R276E
-
marked decrease in specific activity, involved in binding of cosubstrate
L95Y
-
different effects on kinetic konstants
additional information
-
kinetic data of several mutant enzymes, unconservative mutations in K134, Y137 or Y150 lead to protein instability in solution
additional information
-
construction of chimeric enzymes with EC2.8.2.27, to find domains defining substrate and position specificity