Information on EC 2.8.2.25 - flavonol 3-sulfotransferase

New: Word Map on EC 2.8.2.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Flaveria

EC NUMBER
COMMENTARY hide
2.8.2.25
-
RECOMMENDED NAME
GeneOntology No.
flavonol 3-sulfotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + quercetin = adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate group transfer
-
-
-
-
PATHWAY
BRENDA Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
121855-10-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 + kaempferol
adenosine 3',5'-bisphosphate + kaempferol 3-sulfate
show the reaction diagram
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 + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + rhamnetin
adenosine 3',5'-bisphosphate + rhamnetin 3-sulfate
show the reaction diagram
3'-phosphoadenylylsulfate + tamarixetin
adenosine 3',5'-bisphosphate + ?
show the reaction diagram
-
31% of activity compared to rhamnetin
-
-
?
additional information
?
-
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'-phosphoadenylylsulfate + quercetin
adenosine 3',5'-bisphosphate + quercetin 3-sulfate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no divalent cation required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-diphosphoadenosine
-
competitive with respect to 3'-phosphoadenylylsulfate, noncompetitive with respect to quercetin
quercetin 3-sulfate
additional information
-
EDTA, SH-reagents at 1 and 10 mM, e.g. p-chloromercuribenzoate, iodoacetate or iodoacetamide, are not inhibitory
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00018 - 0.0004
3'-phosphoadenylylsulfate
0.0002 - 0.0003
quercetin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
and pH 8.5, two maxima
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 34500, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
L95Y
-
different effects on kinetic konstants
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
additional information