Information on EC 2.4.1.239 - flavonol-3-O-glucoside glucosyltransferase:
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The lowest common taxonomy group for this enzyme is: Pisum sativum

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EC NUMBERCOMMENTARY
2.4.1.239-

RECOMMENDED NAMEGeneOntology No.
flavonol-3-O-glucoside glucosyltransferaseGO:0033838

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
UDP-glucose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside
show the reaction diagram		----
UDP-glucose + a flavonol 3-O-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside
show the reaction diagram		one of three specific glucosyltransferases in pea, Pisum sativum, that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside, see also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240, flavonol-3-O-glycoside glucosyltransferase, TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowlyPisum sativum-657425

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
transfer of glycosyl groupPisum sativum--657425

PATHWAYKEGG LinkMetaCyc Link
kaempferol triglucoside biosynthesis-PWY-5348

SYSTEMATIC NAMEIUBMB Comments
UDP-glucose:flavonol-3-O-beta-D-glucoside 2''-O-beta-D-glucosyltransferaseOne of three specific glucosyltransferases in pea (Pisum sativum) that successively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91, flavonol 3-O-glucosyltransferase and EC 2.4.1.240, flavonol-3-O-glycoside glucosyltransferase). TDP-glucose can replace UDP-glucose as the glucose donor but the reaction proceeds more slowly.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
UDP-glucose:glucosyltransferasePisum sativum--654323

CAS REGISTRY NUMBERCOMMENTARY
50812-18-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Pisum sativumvar. Alaska654323, 657425--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
TDP-glucose + a flavonol 3-O-beta-D-glucosideTDP + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-3fold lower rate than with UDP-glucose as glucosyl donor654323--?
UDP-glucose + a flavonol 3-O-beta-D-glucosideUDP + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-highly specific enzyme, specific for flavonol-3-O-monoglucosides, 3fold higher rate than with TDP-glucose as glucosyl donor654323--?
UDP-glucose + kaempferol 3-O-beta-D-glucosideUDP + kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-best substrate654323--?
UDP-glucose + kaempferol 3-O-beta-D-glucosideUDP + kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-glucosylates kaempferol monoglucoside and quercetin monoglucoside equally657425--?
UDP-glucose + myricetin 3-O-beta-D-glucosideUDP + myricetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-50% of the activity with kaempferol 3-O-beta-D-glucoside654323--?
UDP-glucose + pelargonidin 3-O-beta-D-glucosideUDP + pelargonidin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-2% of the activity with kaempferol 3-O-beta-D-glucoside654323--?
UDP-glucose + quercetin 3-O-beta-D-glucosideUDP + quercetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-62% of the activity with kaempferol 3-O-beta-D-glucoside654323--?
UDP-glucose + quercetin 3-O-beta-D-glucosideUDP + quercetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram		Pisum sativum-glucosylates kaempferol monoglucoside and quercetin monoglucoside equally657425--?
additional information?-Pisum sativum-involved in the biosynthesis of flavonol triglucosides657425---
additional information?-Pisum sativum-one of three glucosyl transferases involved in the biosynthesis of flavonol-3-triglucosides654323---
additional information?-Pisum sativum-glucosylation of kaempferol and quercetin in the 3-position to form the 3-O-triglucoside, reaction proceeds from the aglycone via the mono- and diglucoside intermediates, this reaction sequence is probably associated with three distinct enzyme activities657425---
additional information?-Pisum sativum-no glucosylation of pelargonidin, naringenin, naringin and p-coumaric acid by the three flavonol:glucosyltransferases, not: ADP-glucose, GDP-glucose, kaempferol, kaempferol diglucoside, quercetin-3-rutinoside, quercetin-3-rhamnoside654323---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
additional information?-Pisum sativum-involved in the biosynthesis of flavonol triglucosides657425--
additional information?-Pisum sativum-one of three glucosyl transferases involved in the biosynthesis of flavonol-3-triglucosides654323--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
additional informationPisum sativum-no cofactor requirement654323-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
additional informationPisum sativum-not activated by divalent cations, 0.1-10 mM654323

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
UDPPisum sativum-product inhibition, 1.75 mM, 50% inhibition654323 2D-image
additional informationPisum sativum-not inhibited by divalent cations, 0.1-10 mM, EDTA, EGTA, no substrate inhibition654323-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.004-kaempferol 3-O-beta-D-glucosidePisum sativum-pH 7.3, 30°C654323 2D-image
0.64-UDP-glucosePisum sativum-pH 7.3, 30°C654323 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional information-Pisum sativum--654323

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.3-Pisum sativum-assay at657425
89Pisum sativum-0.2 M glycine-NaOH buffer, lower activity in 0.2 M Tris-HCl buffer654323

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Pisum sativum-assay at654323, 657425

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
leafPisum sativum-young leaf tissues have much higher levels of glucosyltransferase activity than the petioles and internodes657425Manually annotated by BRENDA team
seedlingPisum sativum-light-grown, one week old654323Manually annotated by BRENDA team
seedlingPisum sativum-young, light-grown, much higher levels of glucosyltransferase activity in young leaf tissues than in petioles and internodes657425Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-15°C or room temperature, partially purified enzyme, 36 h, 80% loss of activityPisum sativum-654323
4°C, 2 weeks, stablePisum sativum-654323

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
331fold, separation of three distinct flavonol:glucosyltransferasesPisum sativum-654323

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
654323Jourdan, P.S.; Mansell, R.L.Isolation and partial characterization of three glucosyl transferases involved in the biosynthesis of flavonol triglucosides in Pisum sativum LArch. Biochem. Biophys.213434-4431982Pisum sativum PubMed
657425Shute, J.L.; Jourdan, P.S.; Mansell, R.L.UDP-glucose:glucosyltransferase activity involved in the biosynthesis of flavonol triglucosides in Pisum sativum L. seedlingsZ. Naturforsch. C34738-7411979Pisum sativum PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.239)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)