Information on EC 2.4.1.82 - galactinol-sucrose galactosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.82
-
RECOMMENDED NAME
GeneOntology No.
galactinol-sucrose galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose = myo-inositol + raffinose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lychnose and isolychnose biosynthesis
-
-
stachyose biosynthesis
-
-
stellariose and mediose biosynthesis
-
-
Galactose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-galactosyl-(1->3)-1D-myo-inositol:sucrose 6-alpha-D-galactosyltransferase
4-Nitrophenyl alpha-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-alpha-galactosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
62213-45-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; plants are cold-treated
-
-
Manually annotated by BRENDA team
gene RFS4, isozyme RS4
UniProt
Manually annotated by BRENDA team
cultivar Guonong No. 25
UniProt
Manually annotated by BRENDA team
L. cv. Bravo
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
v. California Dark Red
-
-
Manually annotated by BRENDA team
gene RFS
SwissProt
Manually annotated by BRENDA team
; plants are cold-treated
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-alpha-D-galactosyl-myo-inositol + D-ononitol
myo-inositol + alpha-D-galactosyl-D-ononitol
show the reaction diagram
D-ononitol is 1-D-4-O-methyl-myo-inositol
-
r
1-alpha-D-galactosyl-myo-inositol + D-pinitol
myo-inositol + galactopinitol A
show the reaction diagram
D-pinitol is 1-D-3-O-methyl-chiro-inositol
i.e. O-alpha-D-galactopyranosyl-(1,2)-4-O-methyl-D-chiro-inositol
r
1-alpha-D-galactosyl-myo-inositol + H2O
myo-inositol + D-galactose
show the reaction diagram
1-alpha-D-galactosyl-myo-inositol + sucrose
myo-inositol + raffinose
show the reaction diagram
4-nitrophenol-alpha-D-galactopyranoside + sucrose
4-nitrophenol + raffinose
show the reaction diagram
alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose
myo-inositol + raffinose
show the reaction diagram
alpha-D-galactosyl-D-ononitol + sucrose
D-ononitol + raffinose
show the reaction diagram
-
-
?
galactinol + sucrose
myo-inositol + raffinose
show the reaction diagram
-
-
-
ir
galactinol + sucrose
raffinose + ?
show the reaction diagram
-
-
-
?
myo-inositol + raffinose
1-alpha-D-galactosyl-1D-myo-inositol + sucrose
show the reaction diagram
raffinose + sucrose
sucrose + raffinose
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
1-alpha-D-galactosyl-myo-inositol + sucrose
myo-inositol + raffinose
show the reaction diagram
-
first step in biosynthesis of raffinose sugars
-
-
-
alpha-D-galactosyl-(1->3)-1D-myo-inositol + sucrose
myo-inositol + raffinose
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxygalactonojirimycin
strong, competitive towards galactinol
Ag+
-
1 mM, strong
Al3+
-
1 mM, strong
Hg2+
-
1 mM, strong
iodoacetamide
-
49% inhibition at 1 mM
Mn2+
-
-
myo-inositol
competitive against sucrose
N-ethylmaleimide
-
90% inhibition at 1 mM
Ni2+
destabilization, 30.2% activity at 1 mM
Zn2+
-
1 mM, strong
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heat shock transcription factor A2
in HsfA2 overexpressing plants transcription levels of RS2 increases 5fold
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.17
alpha-D-galactosyl-(1->3)-1D-myo-inositol
pH 7.0, 25C, recombinant His-tagged enzyme
1 - 7.9
galactinol
10
raffinose
-
+ sucrose, exchange reaction
1 - 22.9
Sucrose
additional information
additional information
Michaelis-Menten kinetics
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.189
1-deoxygalactonojirimycin
-
10.1 - 22.3
myo-inositol
3.7
Sucrose
hydrolysis reaction of galactinol, noncompetitive against galactinol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00005
recombinant in Sf21 insect cells
0.0012
-
crude seed extract
0.00138
-
protoplast
0.00258
-
protoplast
0.00396
-
protoplast
0.497
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 7.8
-
about half-maximal activity at pH 5.7 and pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 50
-
about half-maximal activity at 28C and 50C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
gel filtration
88700
amino acid sequence determination
100000
-
glycerol density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
10 min, 80% loss of activity, galactinol and raffinose protect, not sucrose
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithioerythritol stabilizes during purification
-
Mg2+, bovine serum albumin, Triton, Tween 20, and DTT stabilize the enzyme, the latter is used in the enzyme assay
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, in crude extract, t1/2: 3 days
-
frozen, purified enzyme, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
no success in purifying the recombinant His-tagged enzyme from Sf21 insect cells; partial
partial
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Yunyan 85
functional expression as His-tagged protein in Spodoptera frugiperda Sf21 cells via baculovirus infection
gene RFS, cloned from genomic DNA from seddling leaves, DNA and amino acid sequence determination and analysis, semi-quantitative PCR enzyme expression analysis
gene RFS4, cloning from seeds and functional recombinant expression of His-tagged enzyme in Escherichia coli
gene RFS5, functional recombinant expression in Escherichia coli strain BL21 codon plus
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression can be induced by low temperature (highest expression after 2 h at 6C) and 0.15 mM (fruit) and 0.2 mM (leaf) abscisic acid
gene expression of Os07g0209100 encoding raffinose synthase is upregulated by overexpression of the transcription factor 11 (WRKY11) induced by heat pretreatment
the enzyme is induced in leaves by abiotic stresses
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S150F
line 165, mutation induced by mutagen ethyl-methanesulfonate, seed phenotype does not differ from wild-type
T107I
line 397, mutation induced by mutagen ethyl-methanesulfonate, seed sucrose is increased by 28%, raffinose is reduced to 37% and stachyose is reduced to approximately 24% compared to wild-type
additional information