Information on EC 2.8.2.27 - quercetin-3-sulfate 4'-sulfotransferase

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 chlorifolia

EC NUMBER
COMMENTARY hide
2.8.2.27
-
RECOMMENDED NAME
GeneOntology No.
quercetin-3-sulfate 4'-sulfotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + quercetin 3-sulfate = adenosine 3',5'-bisphosphate + quercetin 3,4'-bissulfate
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-sulfate 4'-sulfotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
121855-12-7
-
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 + isorhamnetin 3-sulfate
isorhamnetin 3,4'-disulfate + adenosine 3',5'-bisphosphate
show the reaction diagram
3'-phosphoadenylylsulfate + kaempferol 3-sulfate
kaempferol 3,4'-disulfate + adenosine 3',5'-bisphosphate
show the reaction diagram
3'-phosphoadenylylsulfate + patuletin 3-sulfate
patuletin 3,4'-disulfate + adenosine 3',5'-bisphosphate
show the reaction diagram
-
12% of activity compared to quercetin 3-sulfate
-
?
3'-phosphoadenylylsulfate + quercetin 3-sulfate
quercetin 3,4'-disulfate + adenosine 3',5'-bisphosphate
show the reaction diagram
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 3-sulfate
quercetin 3,4'-disulfate + adenosine 3',5'-bisphosphate
show the reaction diagram
additional information
?
-
-
involved in biosynthesis of polysulfated flavonoids
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phosphate buffer
-
complete inhibition
-
additional information
-
EDTA up to 10 mM, SH-group reagents, e.g. p-chloromercuribenzoate, iodoacetate, iodoacetamide, all at 1 and 10 mM, are not inhibitory
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00038
3'-phosphoadenylylsulfate
0.00036
quercetin 3-sulfate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, bovine serum albumin up to 1 mg/ml, half-life of 3 days
-
4C, half-life of 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of chimeric enzymes with EC2.8.2.25 in order to define domains responsible for substrate binding and position