Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-kestose + H2O
D-fructose + ?
1-kestose + H2O
D-fructose + D-glucose + sucrose
-
-
-
?
2 sucrose
1-kestose + glucose
-
fructosyltransferase activity at high sucrose concentrations
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + D-fructose
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + D-fructose + ?
sucrose, also used to measure transfructosylating activity at high substrate concentration, 0.2 M sodium acetate buffer, pH 5.6, 50°C
products are mainly glucose and fructose, but also neokestose, 1-kestose, and nystose are built
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + ?
1-kestose, about 25% activity compared to sucrose, 0.2 M sodium acetate buffer, pH 5.6, 50°C
-
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranosyl-(1,2)-beta-D-fructofuranosyl-(1-2)-beta-D-fructofuranose + H2O
D-glucose + ?
nystose, about 4% activity compared to sucrose, 0.2 M sodium acetate buffer, pH 5.6, 50°C
-
-
?
alpha-D-glucopyranosyl-(1,6)-D-fructofuranose + H2O
alpha-D-glucopyranose + D-fructofuranose
palatinose, about 2% activity compared to sucrose, 0.2 M sodium acetate buffer, pH 5.6, 50°C
-
-
?
alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranose
glucose
-
sucrose in 50 mM sodium acetate buffer, pH 5.5, 30 degrees Celsius
-
-
?
beta-methyl fructoside + H2O
?
-
-
-
-
?
cellobiose + H2O
?
-
-
-
-
?
chicory inulin + H2O
D-fructose + D-glucose
-
-
-
?
fructooligosaccharide + H2O
D-fructose + ?
-
-
-
-
?
fructosylnystose + H2O
D-fructose + ?
-
-
-
-
?
grass juice + H2O
?
-
hydrolysis of polyfructose moieties in agriculturally-sourced grass juice with recombinant truncated cytosolic enzyme results in the release of more than 13 mg/ml more bioavailable fructose than is measured in untreated grass juice. Bioethanol yields from fermentation experiments with Brewer's yeast and grass juice plus enzymeaere more than 25% higher than those achieved using untreated grass juice feedstock
-
-
?
inulin
D-fructose
-
6% of the activity with fructooligosaccharides
-
-
?
inulin + H2O
beta-D-fructose + ?
inulin + H2O
D-fructose + ?
inulin + H2O
D-fructose + D-glucose + fructooligosaccharides
inulin + H2O
fructose + ?
isoamyl alcohol + H2O
?
-
-
-
-
?
levan + H2O
D-fructose + ?
methyl-beta-D-fructofuranoside + H2O
?
-
-
-
-
?
nystose + H2O
D-fructose + ?
nystose + H2O
D-fructose + D-glucose
-
-
-
-
?
nystose + H2O
D-fructose + D-glucose + sucrose
-
-
-
?
raffinose
beta-D-fructose + melibiose
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
raffinose + H2O
beta-D-fructose + alpha-D-melibiose
raffinose + H2O
beta-D-fructose + melibiose
raffinose + H2O
D-fructose + ?
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
raffinose + H2O
fructose + melibiose
Raftiline HP + H2O
D-glucose + D-fructose
low activity
-
-
?
raftiline LS + H2O
D-glucose + D-fructose
-
-
-
?
raftilose + H2O
D-fructose
best substrate for CscA
-
-
?
stachyose + H2O
D-fructose + alpha-D-Gal-(1->6)-alpha-D-Gal-(1->6)-alpha-D-Gal
297% compared to the activity with sucrose
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
sucrose
fructooligosaccharides + glucose
sucrose + H2O
alpha-D-glucose + D-fructose
sucrose + H2O
beta-D-fructose + alpha-D-glucose
sucrose + H2O
beta-D-fructose + D-glucose
sucrose + H2O
D-fructose + D-glucose
sucrose + H2O
D-glucose + D-fructose
sucrose + H2O
fructose + alpha-D-glucose
sucrose + H2O
fructose + D-glucose
-
-
-
?
sucrose + H2O
fructose + glucose
-
-
-
?
sucrose + lactose
lactosucrose
additional information
?
-
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
D-fructose + ?
-
-
-
?
1-kestose + H2O
D-fructose + ?
-
-
-
-
?
1-kestose + H2O
D-fructose + ?
-
-
-
-
?
1-kestose + H2O
D-fructose + ?
-
-
-
-
?
1-kestose + H2O
D-fructose + ?
5.6% compared to the activity with sucrose
-
-
?
1-kestose + H2O
D-fructose + ?
-
-
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + D-fructose
-
sucrose
-
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + D-fructose
sucrose, 0.2 M sodium acetate buffer, pH 4.9, 37°C
-
-
?
alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose + H2O
D-glucose + D-fructose
-
sucrose
-
-
?
inulin + H2O
?
-
worst substrate
-
-
?
inulin + H2O
?
lowest activity
-
-
?
inulin + H2O
beta-D-fructose + ?
-
-
-
-
?
inulin + H2O
beta-D-fructose + ?
-
-
-
-
?
inulin + H2O
beta-D-fructose + ?
-
-
-
?
inulin + H2O
beta-D-fructose + ?
-
-
-
?
inulin + H2O
beta-D-fructose + ?
-
1.8% of the activity with sucrose, isoenzyme AIV I and AIV II
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
?
inulin + H2O
D-fructose + D-glucose + fructooligosaccharides
10.9% compared to the activity with sucrose
-
-
?
inulin + H2O
D-fructose + D-glucose + fructooligosaccharides
-
product ratio of 10.3:1
-
?
inulin + H2O
fructose + ?
-
-
-
?
inulin + H2O
fructose + ?
-
-
-
?
inulin + H2O
fructose + ?
-
-
-
-
?
inulin + H2O
fructose + ?
-
-
-
-
?
inulin + H2O
fructose + ?
-
-
-
-
?
levan + H2O
?
-
-
-
-
?
levan + H2O
D-fructose + ?
low activity
-
-
?
levan + H2O
D-fructose + ?
-
-
-
-
?
melizitose + H2O
?
-
no activity with melizitose
-
-
?
melizitose + H2O
?
-
no activity with melizitose
-
-
?
melizitose + H2O
?
-
8.1% of the activity with sucrose
-
-
?
melizitose + H2O
?
-
8.1% of the activity with sucrose
-
-
?
melizitose + H2O
?
-
4.5% of the activity with sucrose
-
-
?
melizitose + H2O
?
-
acid invertase, 4.6% of the activity with sucrose, alkaline invertase, 3.1% of the activity with sucrose
-
-
?
neokestose + H2O
?
-
-
-
-
?
neokestose + H2O
?
-
-
-
-
?
nystose + H2O
?
-
-
-
-
?
nystose + H2O
?
-
-
-
-
?
nystose + H2O
?
-
-
-
-
?
nystose + H2O
?
-
-
-
-
?
nystose + H2O
D-fructose + ?
-
-
-
?
nystose + H2O
D-fructose + ?
-
-
-
-
?
nystose + H2O
D-fructose + ?
-
-
-
-
?
nystose + H2O
D-fructose + ?
-
-
-
-
?
nystose + H2O
D-fructose + ?
-
-
-
?
raffinose
beta-D-fructose + melibiose
-
96% of the activity with sucrose
-
-
?
raffinose
beta-D-fructose + melibiose
-
96% of the activity with sucrose
-
-
?
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
25% of the activity with sucrose, recombinant isozyme lbbetafruct3
-
-
?
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
37% of the activity with sucrose, recombinant isozyme lbbetafruct2
-
-
?
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
-
isozymes IT I and IT II
-
-
?
raffinose + H2O
alpha-D-galactosyl-1,6-alpha-D-glucose + D-fructose
-
-
-
?
raffinose + H2O
beta-D-fructose + alpha-D-melibiose
109% compared to the activity with sucrose
-
-
?
raffinose + H2O
beta-D-fructose + alpha-D-melibiose
-
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
invertase 2 has higher affinity for sucrose than for raffinose
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
invertase 2 has higher affinity for sucrose than for raffinose
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
acid invertase, 38.9% of the activity with sucrose, alkaline invertase, 40.0% of the activity with sucrose
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
about 20% of the activity with sucrose, isoenzyme AIV I and AIV II
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
beta-D-fructose + melibiose
-
about 30% of the activity with sucrose, isoenzyme AIV I and AIV II
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
lower activity of all mutants than of wild-type
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
ir
raffinose + H2O
D-fructose + melibiose
-
13.5% of the activity with sucrose
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
no activity
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
10% of the activity with sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
no activity with alkaline invertase, hydrolysis with neutral invertase
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
5.0% of the activity with sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
invertase I, at 45% of the activity with sucrose. Invertase II and III, at 30% of the activity with sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
hydrolyzed at 15% of the rate of sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
77% of the activity with sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
77% of the activity with sucrose
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
raffinose + H2O
fructose + melibiose
-
soluble enzyme
-
-
?
raffinose + H2O
fructose + melibiose
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
no activity with alkaline invertase, hydrolysis with neutral invertase
-
-
?
stachyose + H2O
?
13% of the activity with sucrose, recombinant isozyme lbbetafruct2
-
-
?
stachyose + H2O
?
9% of the activity with sucrose, recombinant isozyme lbbetafruct3
-
-
?
stachyose + H2O
?
-
2.6% of the activity with sucrose
-
-
?
stachyose + H2O
?
-
invertase I, at 45% of the activity with sucrose. Invertase II and III, at 30% of the activity with sucrose
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
about 20% of the activity with sucrose, isoenzyme AIV I and AIV II
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
stachyose + H2O
?
-
-
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
-
soluble AI activity in mungbean hypocotyl is regulated by multiple distinct mechanisms. Rapid down-regulation of soluble acid invertase and the Vr-AI1 transcript level. The speed of down-regulation is markedly reduced in the presence of sucrose, indole-3-acetic acid and light, respectively
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
-
INVA(AOX1) and INVB(AOX1) are highly active at sucrose concentrations of up to 400 and 300 mM, respectively. The tolerance to sucrose decreases to 300 mM for D-INVA(AOX1)
-
-
?
sucrose
beta-D-fructose + alpha-D-glucose
-
INVA(AOX1) and INVB(AOX1) are highly active at sucrose concentrations of up to 400 and 300 mM, respectively. The tolerance to sucrose decreases to 300 mM for D-INVA(AOX1)
-
-
?
sucrose
fructooligosaccharides + glucose
-
-
-
?
sucrose
fructooligosaccharides + glucose
-
-
converts sucrose to 61.2% fructooligosaccharides with a 50% concentration of sucrose as substrate, fructosyltransferase activity
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
activity measured in whole fly homogenates, substrate concentration of 50 mM in sodium phosphate buffer
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
highest activity at 20 mM
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
invertase 2 also shows transfructosylating activity producing fructooligosaccharides. Invertase 1 does not show transfructosylating activity
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
invertase 2 also shows transfructosylating activity producing fructooligosaccharides. Invertase 1 does not show transfructosylating activity
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
10% of the activity with fructooligosaccharides
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
10% of the activity as compared to raffinose
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
10% of the activity as compared to raffinose
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
the enzyme plays a key role in primary metabolism and plant development
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
invertase InvB has a higher affinity toward sucrose and a higher catalytic efficiency (kcat/Km) of about five times to that of invertase InvA
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
isoenzyme AIV I and AIV II
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
the hydrolysis by invertases occurs predominantly when sucrose concentration is below 5%. The increase in the concentration of sucrose to levels above 10% results in the highest transferase activity, reaching about 12.6 g/l of nystose
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
the hydrolysis by invertases occurs predominantly when sucrose concentration is below 5%. The increase in the concentration of sucrose to levels above 10% results in the highest transferase activity, reaching about 13.3 g/l of nystose
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
ultrasound technology is an interesting alternative to improve the invertase performance, accelerating enzymatic reaction
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
the hydrolysis by invertases occurs predominantly when sucrose concentration is below 5%. The increase in the concentration of sucrose to levels above 10% results in the highest transferase activity, reaching about 13.3 g/l of nystose
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
isoenzyme AIV I and AIV II
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
Sac A alone is unable to allow growth on sucrose. A mutant strain, ZM4S, not able to grow on sucrose lacks the two sucrases SacB and SacC, but SacA is present in the intracellular form
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
50 mM MES-buffer, pH 5.6, 20 min, 28°C
at sucrose concentrations higher than 100 mM distinct but small amount of 1-kestose is found as transglycosylation product
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
best substrate
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
37 degrees Celsius, 0.1 M sodium acetate, pH 5, no hydrolysis of cellobiose, maltose, lactose, inulin
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
Corynebacterium murisepticum
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
beta-D-fructofuranose
?
sucrose + H2O
D-fructose + D-glucose
-
100 mM sucrose, 10 min, 55 degrees Celsius, 50 mM sodium acetate buffer, pH 4.5
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
alkaline invertase is highly specific for sucrose, neutral invertase also hydrolyzes raffinose and stachyose
-
-
?
sucrose + H2O
D-fructose + D-glucose
hydrolytic activity toward sucrose is approximately 10times higher than toward raffinose
-
-
?
sucrose + H2O
D-fructose + D-glucose
hydrolytic activity toward sucrose is approximately 10times higher than toward raffinose
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
100 mM sucrose, 1 mg/ml mitochondria, room temperature (22-25°C), 300 mM mannitol + 10 mM morpholinepropanesulfonic acid buffer, pH 7.4, no enzyme activity with maltose or raffinose
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
involved in root cell development and reproductivity in rice
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
1% sucrose, 50 mM potassium phosphate, pH 7, 37 degrees Celsius, 30 min
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
136063, 136069, 136071, 136072, 136075, 136076, 136083, 136084, 136085, 136086, 136090, 136092, 136107, 136113, 136122, 136123, 136131, 136135, 136140, 729344, 729414, 729769 -
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
beta-D-fructofuranose
?
sucrose + H2O
D-fructose + D-glucose
-
-
beta-D-fructofuranose
?
sucrose + H2O
D-fructose + D-glucose
best substrate
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
ir
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
low activity
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
5 mM sucrose, 50 mM Na-acetate, pH 5.2, and 0.02% Na-azide, 30°C, 60 min
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
preferred substrate, recombinant isozyme lbbetafruct2
-
-
?
sucrose + H2O
D-glucose + D-fructose
preferred substrate, recombinant isozyme lbbetafruct3
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
ir
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
isozymes IT I and IT II
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
preferred substrate
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
high activity on sugar cane bagasse, soybean waste, and wheat bran, saccharification levels are 93.69, 57.67, and 55.24, respectively
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
best substrate
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
sucrose is the only substrate
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
fructose + alpha-D-glucose
-
-
-
-
?
sucrose + H2O
fructose + alpha-D-glucose
-
-
-
-
?
sucrose + lactose
lactosucrose
-
transfructosylation mechanism of an ordered bi-bi type in which sucrose is bound first to the enzyme and lactosucrose is released last
-
-
?
sucrose + lactose
lactosucrose
-
transfructosylation mechanism of an ordered bi-bi type in which sucrose is bound first to the enzyme and lactosucrose is released last
-
-
?
trehalose + H2O
?
-
slow hydrolysis
-
-
?
trehalose + H2O
?
-
8.0% of the activity with sucrose
-
-
?
trehalose + H2O
?
-
8.0% of the activity with sucrose
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
-
the enzyme shows also transfructosylation activity with cellobiose or cellotriose as acceptor and sucrose as donor, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme shows also transfructosylation activity with cellobiose or cellotriose as acceptor and sucrose as donor, mechanism, overview
-
-
?
additional information
?
-
-
specific to the beta-1,2 linkage between glucose and fructose
-
-
?
additional information
?
-
-
specific to the beta-1,2 linkage between glucose and fructose
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
high regiospecificity to transfer the fructosyl moiety for the 1-OH group of terminal fructofuranosides
-
-
?
additional information
?
-
-
in vivo substrate specificity of the wild-type and the derepressed mutant strains, overview
-
-
?
additional information
?
-
does not use inulin and levan as substrates
-
-
?
additional information
?
-
-
does not use inulin and levan as substrates
-
-
?
additional information
?
-
-
no hydrolysis of maltose, cellobiose and lactose
-
-
?
additional information
?
-
-
no hydrolysis of maltose, cellobiose and lactose
-
-
?
additional information
?
-
-
no activity with maltose, starch, and trehalose
-
-
?
additional information
?
-
-
intracellular invertase 2 and invertase 1 do not hydrolyze inulin
-
-
?
additional information
?
-
-
intracellular invertase 2 and invertase 1 do not hydrolyze inulin
-
-
?
additional information
?
-
-
intracellular invertase 2 and invertase 1 do not hydrolyze inulin
-
-
?
additional information
?
-
-
intracellular invertase 2 and invertase 1 do not hydrolyze inulin
-
-
?
additional information
?
-
-
alkaline invertase activity appears when the root begins to develop and simultaneously to synthesize sucrose - activity of enzyme form I is high during sucrose accumulation and the enzyme rapidly decreases when sucrose reaches a constant level, while the level of enzyme II activity is approximately constant
-
-
?
additional information
?
-
-
acid invertase activity is very high in immature roots, but rapidly decreases before sucrose is stored and is hardly detectable in mature roots
-
-
?
additional information
?
-
no activity with melezitose, raffinose is a poor substrate
-
-
?
additional information
?
-
-
no activity with melezitose, raffinose is a poor substrate
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
enzyme is induced in presence of sucrose and suppressed in presence of glucose or maltose
-
-
?
additional information
?
-
Corynebacterium murisepticum
-
not repressed by presence of glucose in the medium
-
-
?
additional information
?
-
-
no hydrolysis of lactose and maltose
-
-
?
additional information
?
-
-
post-translational regulation of isozyme CWI involving inhibitor CIF
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
vacuolar invertases from Cu-tolerant and non-tolerant populations of Elsholtzia haichowensis have similar enzyme properties, and the enzyme protein divergences contribute little to the varied vacuolar invertase activities between the contrasting populations
-
-
?
additional information
?
-
vacuolar invertases from Cu-tolerant and non-tolerant populations of Elsholtzia haichowensis have similar enzyme properties, and the enzyme protein divergences contribute little to the varied vacuolar invertase activities between the contrasting populations
-
-
?
additional information
?
-
-
vacuolar invertases from Cu-tolerant and non-tolerant populations of Elsholtzia haichowensis have similar enzyme properties, and the enzyme protein divergences contribute little to the varied vacuolar invertase activities between the contrasting populations
-
-
?
additional information
?
-
inulin and levan are not hydrolyzed
-
-
?
additional information
?
-
-
inulin and levan are not hydrolyzed
-
-
?
additional information
?
-
inulin and levan are not hydrolyzed
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview, the cell wall-bound isozyme is involved in nucellar projection in the endospermal transfer cell layer
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct2
-
-
?
additional information
?
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct2
-
-
?
additional information
?
-
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct2
-
-
?
additional information
?
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct3
-
-
?
additional information
?
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct3
-
-
?
additional information
?
-
-
activity with cellobiose, maltose, lactose, and inulin, by isozyme lbbetafruct3
-
-
?
additional information
?
-
-
no substrate: stachyose, melizitose
-
-
?
additional information
?
-
no hydrolysis when using 4-nitrophenyl-alpha-D-glucopyranose as substrate
-
-
?
additional information
?
-
-
no hydrolysis when using 4-nitrophenyl-alpha-D-glucopyranose as substrate
-
-
?
additional information
?
-
-
no sucrose:sucrose fructosyltransferase activity
-
-
?
additional information
?
-
-
substrate specificity of isozymes SAI and CWI, no activity with stachyose of isozymes SAI and CWI
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
-
cell-wall invertase isozymes CIN1-9 play an important role in carbon allocation to developing organs, and respond to rapidly to water deficit in antheres and and peduncles and through a reduction in sink strength help to coordinate a delay in anthesis and heading, their expression is affected by water and temperature stress, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
-
function in seed development
-
-
?
additional information
?
-
-
post-translational regulation of isozyme CWI involving inhibitor CIF
-
-
?
additional information
?
-
-
the cell wall-bound isozyme Cin1 shows cytokinin-like function in leaf senescence, overview, the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
both isozymes IT I and IT II show no activity with maltose
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
no substrate: trehalose
-
-
?
additional information
?
-
-
no hydrolysis of lactose, maltose, trehalose, melizitose and melibiose
-
-
?
additional information
?
-
-
no transfructosylation reraction at 1 M sucrose
-
-
?
additional information
?
-
-
at high substrate concentrations, 1 M, transferase activity, transferring the beta-D-fructofuranosyl residue to primary alcohols such as methanol, ethanol and n-propanol, extracellular enzyme
-
-
?
additional information
?
-
-
no activity with maltose, lactose, turanose, leucrose, and palatinose
-
-
?
additional information
?
-
-
Lys e 2 is able to trigger histamine release from passively sensitized basophils of patients with IgE to carbohydrate determinants
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
function of cell wall-bound invertase activity during pathogen infection, the Lin8-mutant lines 33 and 57 do not increase activity in response to Xanthomonas campestris pv vesicatoria infection, line 50 only slightly, and all mutant lines show symptoms delayed, expression of senescent-associated genes is decreased, mutants have about 50% lower starch content due to 2-fold increased sucrose export, and show a tendency for increased fructose content
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
enzyme does not show transfructosylating activity. No substrate: inulin
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview, the cell wall-bound isozyme is involved in establishing a higher sink strength in young seeds at the site of assimilate unloading into the apoplast
-
-
?
additional information
?
-
-
acid invertases play a key role in sugar metabolism
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
the enzyme is an important in carbohydrate metabolism, it is regulated by abiotic stress, the phytohormone abscisic acid, glucose, and may as well depend on the circadian rhythm in leaves, overview
-
-
?
additional information
?
-
-
the enzyme is an important in carbohydrate metabolism, it is regulated by abiotic stress, the phytohormone abscisic acid, glucose, and may as well depend on the circadian rhythm in leaves, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
inulin + H2O
D-fructose + D-glucose + fructooligosaccharides
-
product ratio of 10.3:1
-
?
raffinose + H2O
D-fructose + melibiose
-
-
-
-
ir
sucrose
beta-D-fructose + alpha-D-glucose
-
soluble AI activity in mungbean hypocotyl is regulated by multiple distinct mechanisms. Rapid down-regulation of soluble acid invertase and the Vr-AI1 transcript level. The speed of down-regulation is markedly reduced in the presence of sucrose, indole-3-acetic acid and light, respectively
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
sucrose + H2O
D-fructose + D-glucose
sucrose + H2O
D-glucose + D-fructose
sucrose + H2O
fructose + D-glucose
-
-
-
?
additional information
?
-
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
the enzyme plays a key role in primary metabolism and plant development
-
-
?
sucrose + H2O
beta-D-fructose + alpha-D-glucose
-
Sac A alone is unable to allow growth on sucrose. A mutant strain, ZM4S, not able to grow on sucrose lacks the two sucrases SacB and SacC, but SacA is present in the intracellular form
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
involved in root cell development and reproductivity in rice
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
ir
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
ir
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
high activity on sugar cane bagasse, soybean waste, and wheat bran, saccharification levels are 93.69, 57.67, and 55.24, respectively
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
-
in vivo substrate specificity of the wild-type and the derepressed mutant strains, overview
-
-
?
additional information
?
-
-
alkaline invertase activity appears when the root begins to develop and simultaneously to synthesize sucrose - activity of enzyme form I is high during sucrose accumulation and the enzyme rapidly decreases when sucrose reaches a constant level, while the level of enzyme II activity is approximately constant
-
-
?
additional information
?
-
-
acid invertase activity is very high in immature roots, but rapidly decreases before sucrose is stored and is hardly detectable in mature roots
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
enzyme is induced in presence of sucrose and suppressed in presence of glucose or maltose
-
-
?
additional information
?
-
Corynebacterium murisepticum
-
not repressed by presence of glucose in the medium
-
-
?
additional information
?
-
-
post-translational regulation of isozyme CWI involving inhibitor CIF
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview, the cell wall-bound isozyme is involved in nucellar projection in the endospermal transfer cell layer
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview, the cell wall-bound isozyme responses to pathogen attack and wounding
-
-
?
additional information
?
-
-
cell-wall invertase isozymes CIN1-9 play an important role in carbon allocation to developing organs, and respond to rapidly to water deficit in antheres and and peduncles and through a reduction in sink strength help to coordinate a delay in anthesis and heading, their expression is affected by water and temperature stress, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
function in seed development
-
-
?
additional information
?
-
-
function in seed development
-
-
?
additional information
?
-
-
post-translational regulation of isozyme CWI involving inhibitor CIF
-
-
?
additional information
?
-
-
the cell wall-bound isozyme Cin1 shows cytokinin-like function in leaf senescence, overview, the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
Lys e 2 is able to trigger histamine release from passively sensitized basophils of patients with IgE to carbohydrate determinants
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
function of cell wall-bound invertase activity during pathogen infection, the Lin8-mutant lines 33 and 57 do not increase activity in response to Xanthomonas campestris pv vesicatoria infection, line 50 only slightly, and all mutant lines show symptoms delayed, expression of senescent-associated genes is decreased, mutants have about 50% lower starch content due to 2-fold increased sucrose export, and show a tendency for increased fructose content
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview, the cell wall-bound isozyme is involved in establishing a higher sink strength in young seeds at the site of assimilate unloading into the apoplast
-
-
?
additional information
?
-
-
acid invertases play a key role in sugar metabolism
-
-
?
additional information
?
-
-
cell wall and vacuole invertases are important metabolic enzymes, but also key players during wound and pathogen defense reactions and in several developmental transitions, post-translational regulation mechanisms, overview
-
-
?
additional information
?
-
the enzyme is an important in carbohydrate metabolism, it is regulated by abiotic stress, the phytohormone abscisic acid, glucose, and may as well depend on the circadian rhythm in leaves, overview
-
-
?
additional information
?
-
-
the enzyme is an important in carbohydrate metabolism, it is regulated by abiotic stress, the phytohormone abscisic acid, glucose, and may as well depend on the circadian rhythm in leaves, overview
-
-
?
additional information
?
-
-
the isozymes have different functions, e.g. the vacuolar isozyme is responsible for control of sugar composition in fruits and storage organs, for osmoregulation and cell enlargement, and response to drought stress, hypoxia, wounding, and gravitropism, the extracellular isozyme is involved in sucrose partitioning, and response to wounding and pathogen infection, several regulation mechanisms, overview
-
-
?
additional information
?
-
the isozymes play important roles in plant development, enzyme regulation, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,5-anhydro-D-mannose
-
competitive
2,5-dideoxy-2,5-imino-D-glucitol
-
-
2,5-dideoxy-2,5-imino-D-mannitol
-
very good inhibitor
2-Amino-2-hydroxymethyl propane-1,3-diol
-
extracellular enzyme
4-chloromercuribenzoate
-
0.5 mM, 62% inhibition of isozyme IT I, 86% inhibition of isozyme IT II
4-hydroxymercuribenzoate
complete inhibition at 1 mM
AgCl
-
47.08% residual activity at 0.5 mM
AgNO3
-
0.1 mM, 37% inhibition; 1 mM, 88% inhibition
Al2(SO4)3
-
18.35% residual activity at 0.5 mM
Al3+
-
20.5% residual activity at 10 mM
alpha-chymotrypsin
-
0.5 mg/ml
-
alpha-methyl glucoside
-
50 mM, 20% inhibition
ammonium heptamolybdate
-
-
ammonium sulfate
-
intracellular enzyme
Arabidopsis thaliana cell wall/vacuolar inhibitor of fructosidase 1
-
cell-wall invertase: 69% activity of control
-
Arabidopsis thaliana cell wall/vacuolar inhibitor of fructosidase 2
-
cell-wall invertase: 67% activity of control
-
ATP
-
inhibition of neutral invertase, no inhibition of alkaline invertase
Beta vulgaris cell wall/vacuolar inhibitor of fructosidase
-
cell-wall invertase: 57% activity of control
-
beta-methyl-fructoside
-
336 mM, 27% inhibition
CaCl2
-
72.27% residual activity at 0.5 mM
Cd-acetate
-
10 mM, 50% inhibition
cell-wall inhibitor of beta-fructosidase
-
-
-
cellobiose
-
40 mM, 22% inhibition
cellwall inhibitor of beta-fructosidase
2.6 A crystal structure of cell-wall invertase 1 in complex with protein inhibitor, cell-wall inhibitor of beta-fructosidase, from tobacco. The structure recognizes a small amino acid motif in the inhibitor that directly targets the invertase active site. The activity of INV1 and its interaction with inhibitor are strictly pH-dependent with a maximum at about pH 4.5. At this pH, isothermal titration calorimetry reveals that the inhibitor tightly binds its target with nanomolar affinity
-
CTP
-
inhibition of neutral invertase, no inhibition of alkaline invertase
endogenous protein inhibitors
-
fructose 1,6-diphosphate
-
-
fructose 6-phosphate
-
slight inhibition
galactose
-
50 mM, 10% inhibition
GTP
-
inhibition of neutral invertase, no inhibition of alkaline invertase
guanidinium hydrochloride
-
2 M, 2% residual activity
invertase inhibitor of Solanum lycopersicum
6.7 nM tomato invertase with 1-2.5 nM inhibitor retains more than 90% invertase activity, 3-4 nM less than 90% activity, 5 nM about 75%, about 6.7 nM about 60% activity, pH 4.9, 37 degrees Celsius, 100 mM sucrose as substrate, proteinaceous functional inhibitor is expressed in leaves, flowers, and green fruit, proteolytically cleaving the invertase
-
iodoacetamide
-
5 mM, about 20% inhibition of isozyme IT I, 44% inhibition of isozyme IT II
K2PtCl3
-
non-competitive
KCl
-
70% residual activity at 0.5 mM
Lectins
-
lectins which bind mannose and glucose, and those which bind oligomers of N-acetylglucosamine
-
maltose
-
80 mM, 40% inhibition
Man-alpha(1-6)-[Xyl-beta(1-2)]-Man-beta(1-4)-GlcNAc-beta(1-4)-[Fuc-alpha(1-3)]-GlcNAc
-
pineapple stem bromelain glycopeptide MUXF, complete inhibition
melezitose
-
40 mM, 10% inhibition
melibiose
-
40 mM, 13% inhibition
MnSO4
-
96.12% residual activity at 0.5 mM
MoO42-
-
about 60% residual activity at 10 mM
NaBr
-
62.7% residual activity at 10 mM
NaCl
-
0.1 M, partial, intracellular enzyme
NaH2PO4
-
67.9% residual activity at 10 mM
NH4F
-
51.3% residual activity at 10 mM
Nicotiana tabacum cell wall inhibitor of fructosidase
-
cell-wall invertase: 28% activity of control; vacuolar invertase: 59% activity of control
-
Nicotiana tabacum vacuolar inhibitor of fructosidase
-
cell-wall invertase: 52% activity of control
-
p-chloromercuribenzoate
-
-
PMSF
-
0.5 mM, 20% inhibition of isozyme IT I, 60% inhibition of isozyme IT II
polyethylene ethanol
-
65.48% residual activity at 0.5% (v/v)
protein C/VIF-RP1-4
-
i.e. vacuole inhibitor protein of beta-fructosidase related proteins, 4 different amino acid sequences
-
pyridoxal 5'-phosphate
-
-
pyridoxal hydrochloride
-
-
pyridoxine hydrochloride
-
-
Sodium dodecyl sulfate
-
10 mM, no residual activity
Sodium sulfate
-
0.1 M, partial, intracellular enzyme
SolyVIF
non-competitive inhibition
-
sorbitol
-
inhibitory action at 30 and 40% solution
trehalose
-
50 mM, 23% inhibition
Tris-HCl
-
Tris-HCl does not affect acid invertase activity up to 14 mM, 10 mM Tris-HCl inhibits alkaline invertase activity by about 50%
turanose
-
20 mM, complete inhibition
Tween 80
-
46.76% residual activity at 0.2% (v/v)
UTP
-
inhibition of neutral invertase, no inhibition of alkaline invertase
vacuolar invertase inhibitor 2
-
-
-
WO42
-
about 25% residual activity at 10 mM
xylitol
-
inhibitory action at 35 and 40% solution
Zn(NO3)2
-
66.2% residual activity at 10 mM
ZnCl2
-
0.1 mM, 84% inhibition; 1 mM, 100% inhibition
2-mercaptoethanol
-
87.8% residual activity at 10 mM
2-mercaptoethanol
-
2 mM, 50.3% loss of activity
Ag+
-
AgNO3
Ag+
-
18% residual activity at 10 mM
Ag+
-
0.02 mM, complete inhibition of invertase I, 44% inhibition of invertase II
Ag+
-
10 mM, no residual activity
Ag+
-
1 mM, 26% inhibition of beta-fructofuranosidase activity, no effect on invertase activity
Ag+
-
1.7 mM AgNO3, complete inhibition
Ag+
-
1 mM, 56% inhibition of isozyme IT I, 81% inhibition of isozyme IT II
Ag+
-
62% inhibition at 0.01 mM, 89% inhibition at 1 mM
Ag+
-
0.1 mM, 95% inhibition of the CM-cellulose adsorbed enzyme, enzyme embedded within a polyacrylamide gel is inhibited 72.7%
Ag+
-
0.004 mM, complete inhibition; AgNO3
aniline
-
10 mM, 45% inhibition of invertase I, no inhibition of invertase II
aniline
-
5 mM, 36% inhibition of isozyme IT I, 17% inhibition of isozyme IT II
aniline
-
extracellular enzyme
Ba2+
-
-
Ca2+
-
73% residual activity at 1 mM
Ca2+
-
2 mM, 36.7% loss of activity
Ca2+
15% inhibition at 1 mM
Ca2+
-
CaCl2; inhibition of alkaline invertase no inhibition of neutral invertase
Ca2+
5 mM, 25% loss of activity
Ca2+
-
5 mM, 35% inhibition of isozyme IT I, 84% inhibition of isozyme IT II
Cd2+
-
-
Cd2+
5 mM, 63% loss of activity
Cd2+
-
1 mM, 66% inhibition
Co2+
-
-
Co2+
-
63.5% residual activity at 10 mM
Co2+
38% inhibition at 1 mM
Co2+
5 mM, 56% loss of activity
Co2+
-
2 mM, 64% residual activity
Cu2+
-
-
Cu2+
-
53% residual activity at 10 mM; 94% residual activity at 1 mM
Cu2+
-
28.5% residual activity at 10 mM
Cu2+
-
10 mM, 52% residual activity
Cu2+
complete inhibition at 1 mM
Cu2+
-
1 mM, 75% inhibition of beta-fructofuranosidase activity, no effect on invertase activity
Cu2+
5 mM, 23% loss of activity
Cu2+
-
1.7 mM, partial inhibition; CuSO4
Cu2+
-
1 mM, 90% inhibition
Cu2+
-
1 mM, 53% inhibition of isozyme IT I, 85% inhibition of isozyme IT II
Cu2+
-
significant inhibition at 0.04 mM
Cu2+
-
2 mM, 5% residual activity
Cu2+
virtually abolishes invertase activity
Cu2+
-
inhibits invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter, native invertase INVB and invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter
CuSO4
-
complete inhibition at 0.5 mM
CuSO4
-
0.1 mM, 46% inhibition; 1 mM, 100% inhibition
CuSO4
-
6.2 mM, 50% inhibition
CuSO4
-
acid invertase is inhibited about 50% by 4.8 mM CuSO4. Alkaline invertase is inhibited by 0.6 mMCuSO4 up to 50%
D-fructose
-
competitive inhibition of the fruit acid invertase
D-fructose
-
product inhibition, 2.5 mM, 62% inhibition of isozyme IT I, 70% inhibition of isozyme IT II
D-fructose
-
competitive inhibition of the tuber and leaf enzyme
D-glucose
-
product inhibition, 2.5 mM, 58% inhibition of isozyme IT I, 72% inhibition of isozyme IT II
D-glucose
-
non-competitive inhibition of the tuber and leaf acid invertase
DTNB
-
-
DTNB
-
0.5 mM, 24% inhibition of isozyme IT I, 11% activation of isozyme IT II
EDTA
-
12.34% residual activity at 0.2% (w/v)
EDTA
-
47.9% residual activity at 10 mM
endogenous protein inhibitors
-
-
-
endogenous protein inhibitors
-
-
endogenous protein inhibitors
-
-
Fe2+
-
11.6% residual activity at 10 mM
Fe2+
55% inhibition at 1 mM
Fe2+
-
1 mM, 9% inhibition of beta-fructofuranosidase activity, 7% inhibition of invertase activity
Fe3+
-
16.5% residual activity at 10 mM
Fe3+
-
2 mM, 0.8% residual activity
FeCl2
-
-
FeSO4
-
25.29% residual activity at 0.5 mM
fructose
-
competitive inhibitor for invertase 2
fructose
-
competitive inhibitor of neutral and alkaline enzyme
fructose
-
40 mM, 52% inhibition; 4 mM, 22% inhibition
fructose
-
competitive inhibition of a classical type
fructose
-
competitive inhibition of a classical type
fructose
-
partial competitive
glucose
-
non-competitive inhibitor of neutral and alkaline invertase
glucose
-
40 mM, 100% inhibition
glucose
-
non-competitive
glucose
-
non-competitive
Hg+
-
complete inhibition at 10 mM
Hg+
-
complete inhibition at 10 mM
Hg2+
-
HgCl2
Hg2+
-
1 mM, complete inhibition
Hg2+
-
0.002 mM, 55% inhibition of invertase I, complete inhibition of invertase II
Hg2+
-
10 mM, no residual activity
Hg2+
-
1 mM, complete inhibition of beta-fructofuranosidase activity, 65% inhibition of invertase activity
Hg2+
-
no inhibition of neutral and alkaline invertase
Hg2+
5 mM, complete loss of activity
Hg2+
-
invertase I is more than 2fold more resistant than invertase IIA and IIB
Hg2+
-
1.7 mM HgCl2, complete inhibition
Hg2+
-
1 mM, 67% inhibition
Hg2+
-
65% inhibition at 0.001 mM
Hg2+
-
1 mM, 93% inhibition of isozyme IT I, 95% inhibition of isozyme IT II
Hg2+
-
44% inhibition at 0.01 mM, 96% inhibition at 1 mM
Hg2+
-
2 mM, no residual activity
Hg2+
-
0.002 mM, complete inhibition; HgCl2
Hg2+
-
inhibits native invertase INVA, invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter, native invertase INVB and native invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter
HgCl2
-
0.1 mM, 48% inhibition; 1 mM, 89% inhibition
HgCl2
-
does not affect acid invertase activity, 0.05 mM HgCl2 inhibits alkaline invertase activity by about 50%
I2
-
0.004 mM, complete inhibition of invertase II, 9% inhibition of invertase I
I2
-
extracellular enzyme
I2
-
0.004 mM, complete inhibition
INVINH1
-
endogenous tomato invertase inhibitor. Ectopic overexpression of INVINH1 in Arabidopsis thaliana specifically reduces cell wall invertase activity. By contrast, silencing its expression in tomato significantly increases the activity of cell wall invertase without altering activities of cytoplasmic and vacuolar invertases. Elevation of cell wall invertase activity in RNA interference transgenic tomato leads to a prolonged leaf life span involving in a blockage of abscisic acid-induced senescence and an increase in seed weight and fruit hexose level
-
INVINH1
cell wall invertase inhibitor gene name; cell wall invertase inhibitor gene name
-
K+
-
-
K+
-
67.1% residual activity at 10 mM
K+
-
2 mM, 79% residual activity
lactose
-
-
lactose
-
40 mM, 17% inhibition
Mg2+
-
-
Mg2+
-
79% residual activity at 10 mM
Mg2+
-
2 mM, 31.1% loss of activity
Mg2+
-
MgCl2, inhibition of alkaline invertase no inhibition of neutral invertase
Mg2+
5 mM, 23% loss of activity
Mg2+
-
1 mM, 11% inhibition of isozyme IT I, 14% inhibition of isozyme IT II
Mg2+
-
about 90% residual activity at 10 mM
Mn2+
-
1 mM, 1% inhibition of fructofuranosidase activity
Mn2+
-
MnCl2, inhibition of alkaline invertase no inhibition of neutral invertase
Na+
-
-
Na+
-
73% residual activity at 10 mM
Na+
negatively effected by 0.8 M Na+
NEM
-
10 mM, complete inhibition
NH4Cl
-
25% residual activity at 10 mM
NH4Cl
-
36.6% residual activity at 10 mM
Ni2+
-
-
Ni2+
5 mM, 52% loss of activity
Ni2+
-
inhibits native invertase INVB and invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter
Pb2+
5 mM, 48% loss of activity
PCMB
-
6 mM, complete inhibition
PCMB
-
10 mM, 90% inhibition
PCMB
-
0.002 mM, 21% inhibition of invertase I, 79% inhibition of invertase II
PCMB
-
1 mM, 80% inhibition of beta-fructofuranosidase activity, 65% inhibition of invertase activity
PCMB
-
0.1 mM, significant inhibition
PCMB
-
0.1 mM, 94% inhibition of the CM-cellulose adsorbed enzyme, enzyme embedded within a polyacrylamide gel is inhibited 16.7%
protein C/VIF-RP
-
i.e. vacuole inhibitor protein of beta-fructosidase related proteins, amino acid sequence comparison
-
protein C/VIF-RP
-
i.e. vacuole inhibitor protein of beta-fructosidase related proteins, amino acid sequence comparison
-
protein CIF
-
i.e. cell wall inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase, DNA and amino acid sequence determination and analysis, dendrogram, properties, overview
-
protein CIF
-
i.e. cell wall inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase
-
protein CIF
-
i.e. cell wall inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase, high expression in cell culture
-
protein CIF
-
i.e. cell wall inhibitor protein of beta-fructosidase, endogenous, nonglycosylated, specific inhibitor of the invertase, DNA and amino acid sequence determination and analysis, strong expression in flowers, in ovary, stamen, and petals, co-expression with the enzyme in leaves and cell suspension culture, properties, expression regulation in response to abscisic acid and polyethylene glycol, overview
-
protein CIF
-
i.e. cell wall inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase, high expression in cell culture
-
protein VIF
-
i.e. vacuole inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase, DNA and amino acid sequence determination and analysis, dendrogram, properties, overview
-
protein VIF
-
i.e. vacuole inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase
-
protein VIF
-
i.e. vacuole inhibitor protein of beta-fructosidase, endogenous, specific inhibitor of the invertase, DNA and amino acid sequence determination and analysis, strong expression in roots, properties, overview
-
pyridoxal
-
1 mM, 65% inhibition of invertase I, 25% inhibition of invertase II
pyridoxal
-
invertase I is more than 2fold more resistant than invertase IIA and IIB
pyridoxal
-
1 mM, 15% inhibition
pyridoxamine
-
10 mM, 28% inhibition of invertase I, 65% inhibition of invertase II
pyridoxamine
-
10 mM, 85% inhibition
pyridoxine
-
2.5 mM, 70% inhibition of invertase I, 20% inhibition of invertase II
pyridoxine
-
5 mM, 48% inhibition of isozyme IT I, 75% inhibition of isozyme IT II
pyridoxine
-
2.5 mM, 24% inhibition
SDS
-
2 mM, 89.5% loss of activity
SDS
complete inhibition at 1 mM
sucrose
increase of the sucrose concentration from 2.5 mM to 1 M results in decreased hydrolysis activity
sucrose
-
substrate inhibition above 100 mM
sucrose
-
substrate inhibition, 400 mM: 10% inhibition of isozyme IT I, 20% inhibition of isozyme IT II, 1 M: 10% inhibition of isozyme IT I, 62% inhibition of isozyme IT II
sucrose
-
the intact enzyme is inhibited at sucrose concentrations in excess of 0.1 M
sucrose
substrate inhibition, but retains 50% activity up to 1 M sucrose
sucrose
-
invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter and invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter are highly active at sucrose concentrations of up to 400 and 300 mM, respectively
Tris
-
-
Tris
-
10 mM, 87% inhibition; 1 mM, 74% inhibition
Urea
-
4 M
Urea
-
2 M, 29% residual activity
Zn2+
-
inhibitory
Zn2+
-
19% residual activity at 10 mM
Zn2+
56% inhibition at 1 mM
Zn2+
-
1 mM, 26% inhibition of beta-fructofuranosidase activity, 13% inhibition of invertase activity
Zn2+
5 mM, 38% loss of activity
Zn2+
-
1 mM, no inhibition of isozyme IT I, 86% inhibition of isozyme IT II
Zn2+
-
2 mM, 0.8% residual activity
Zn2+
-
about 80% residual activity at 10 mM
Zn2+
-
inhibits native invertase INVB and invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter
ZnSO4
-
65.6% residual activity at 0.5 mM
additional information
-
not inhibited by metal ions
-
additional information
-
no inhibition of the fruit acid invertase by D-glucose
-
additional information
-
vacuolar invertase: no inhibition of Arabidopsis thaliana cell wall/vacuolar fructosidase 1
-
additional information
-
decrease of enzyme activity during fruit development; decrease of enzyme activity in leaves during fruit development
-
additional information
-
Pb2+ and Hg2+ do not inhibit the enzyme activity at a concentration of 1 mM
-
additional information
-
MgCl2 and CaCl2 (1 mM) are typical alkaline invertase inhibitors, they do not inhibit the neutral invertase
-
additional information
-
the enzyme can be significantly inactivated by high pressure processing with pressure (50-600 MPa) at 45°C and 50°C, and be activated by high pressure processing (50-400 MPa) at 40°C. The secondary structure of the enzyme is not sensitive to high pressure processing, and its tertiary structure is modified by high pressure processing. High pressure processing at 400 MPa/50°C for 2.5 min induces dissociation of the enzyme, and high pressure processing at 600 MPa/50°C for 30 min results aggregation and fibril formation of the enzyme
-
additional information
-
sucrose specifically suppresses the expression of acid invertase Cin5
-
additional information
-
not inhibitory: HgCl2
-
additional information
-
not inhibited by fructose
-
additional information
-
repression of the wild-type and mutant enzymes by D-glucose
-
additional information
-
high substrate concentrations and also high levels of the cleavage products glucose and fructose do not severly inhibit sucrose inversion
-
additional information
-
product inhibition does not appear to be involved in the physiological regulation of the enzyme
-
additional information
Mg2+ does not affect the activity
-
additional information
-
Mg2+ does not affect the activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.2
fructosylnystose
-
pH 5.7, 37°C
1.7
neokestose
-
pH 5.7, 37°C
additional information
additional information
-
1.3
1-kestose
-
in 0.2M sodium acetate buffer (pH 5.6), at 50°C
1.7
1-kestose
-
pH 5.7, 37°C
4.5
1-kestose
pH 5.5, 42°C, alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranosyl-(1,2)-beta-D-fructofuranose
49
1-kestose
-
pH 5.0, 37°C
700
1-kestose
-
in 50 mM sodium acetate buffer (pH 5.0), at 30°C
22.5
cellobiose
-
in 100 mM sodium acetate buffer, pH 5.0, at 50°C
123.6
cellobiose
-
in the presence of Mn2+, in 100 mM sodium acetate buffer, pH 5.0, at 50°C
0.9
inulin
37°C, pH 7.5
2.66
inulin
-
in sodium acetate buffer, 100 mM, pH 4.5, at 60°C
7
inulin
-
mutant N254A, pH 5.0
9
inulin
-
mutant Y462A, pH 5.0
12
inulin
-
wild-type, pH 5.0
14
inulin
-
mutant Q435A, pH 5.0
15.6
inulin
-
pH 5.0, 37°C
24
inulin
-
mutant Q176E, pH 5.0
25.9
inulin
-
pH 5.7, 37°C
44
inulin
-
mutant S281I, pH 5.0
47
inulin
-
mutant Q228V, pH 5.0
60
inulin
-
mutant N142Y, pH 5.0
575
inulin
-
mutant Q176S, pH 5.0
1.6
nystose
-
in 0.2M sodium acetate buffer (pH 5.6), at 50°C
3.8
nystose
-
mutant Q435A, pH 5.0
3.9
nystose
-
pH 5.7, 37°C
8
nystose
-
mutant N142Y, pH 5.0
8
nystose
-
mutant N254A, pH 5.0
8
nystose
-
mutant Y462A, pH 5.0
8.1
nystose
-
mutant Q176E, pH 5.0
9
nystose
-
mutant Q228V, pH 5.0
11
nystose
-
mutant Q176S, pH 5.0
15
nystose
-
pH 5.0, 37°C
15
nystose
-
mutant S281I, pH 5.0
1.3
raffinose
-
in 0.2M sodium acetate buffer (pH 5.6), at 50°C
1.6
raffinose
-
invertase I
2.9
raffinose
-
invertase I
4.5
raffinose
-
pH 5.0, 40°C
7.37
raffinose
-
in sodium acetate buffer, 100 mM, pH 4.5, at 60°C
7.6
raffinose
-
enzyme form F-1
10.6
raffinose
-
beta-FFase L, pH 5.1
10.8
raffinose
-
invertase II
13
raffinose
-
invertase III
16.4
raffinose
-
55°C, pH 4.6, invertase 2
16.7
raffinose
-
enzyme form F-2
17
raffinose
-
invertase II
19.6
raffinose
-
soluble enzyme
20.4
raffinose
-
beta-FFase E, pH 5.1
20.7
raffinose
-
pH 7.5, alkaline invertase
21.7
raffinose
-
beta-FFase L, pH 3.6
32.19
raffinose
pH 5.0, 37°C
55.98
raffinose
-
40°C, pH 4.5
125
raffinose
-
beta-FFase E, pH 3.6
141
raffinose
37°C, pH 7.5
150
raffinose
-
extracellular and intracellular enzyme
150
raffinose
-
exteracellular enzyme
392
raffinose
-
pH 5.0, 37°C
14
stachyose
-
invertase I
25
stachyose
-
invertase II
168
stachyose
37°C, pH 7.5
434.42
stachyose
-
40°C, pH 4.5
0.00829
sucrose
-
37°C, pH not specified in the publication
0.01582
sucrose
-
37°C, pH not specified in the publication
0.06528
sucrose
-
37°C, pH not specified in the publication
0.104
sucrose
-
pH and temperature not specified in the publication
0.1193
sucrose
-
37°C, pH not specified in the publication
0.282
sucrose
30°C, pH 5.0
0.32
sucrose
-
neutral invertase
0.37
sucrose
-
pH and temperature not specified in the publication
0.56
sucrose
-
saline-released acid invertase
0.65
sucrose
-
native enzyme
0.65
sucrose
-
invertase 1
0.98
sucrose
-
invertase 2
1
sucrose
-
invertase IIA
1.08
sucrose
-
at pH 5.5 and 55°C
1.37
sucrose
pH 7.5, 37°C, wild-type enzyme
1.4
sucrose
-
enzyme embedded within a polyacrylamide gel
1.43
sucrose
-
deglycosylated enzyme
1.54
sucrose
-
pH 4.7, 30°C, F-form, extracellular
1.7
sucrose
-
invertase IIB
1.7
sucrose
-
cell-wall bound enzyme
1.8
sucrose
-
acid invertase, pH 6.5, 37°C
2
sucrose
-
pH 4.7, 30°C, S-form, extracellular
2
sucrose
in 50 mM acetate buffer (pH 5.0) at 37°C
2
sucrose
-
pH and temperature not specified in the publication
2
sucrose
pH and temperature not specified in the publication
2.1
sucrose
-
invertase P-2
2.17
sucrose
-
beta-FFasse-E, pH 5.1
2.4
sucrose
-
invertase I
2.4
sucrose
-
pH 7.0, 37°C
2.4
sucrose
-
pH 6.8, 37°C
2.4
sucrose
-
wild-type, pH 5.0
2.46
sucrose
pH 7.0, 50°C
2.5
sucrose
-
extracellular enzyme, pH 4.5, 60°C
2.68
sucrose
30°C, pH 5.0
2.77
sucrose
30°C, pH 5.0
2.8
sucrose
-
acid invertase
2.94
sucrose
-
pH and temperature not specified in the publication
3 - 3.5
sucrose
-
native invertase, pre-incubation at 80°C for 20 min, 55°C, pH 4.5
3.3
sucrose
-
pH and temperature not specified in the publication
3.33
sucrose
-
pH 4.5, 30°C, isoenzyme AIV I
3.45
sucrose
-
beta-FFase E, pH 4.5
3.5
sucrose
-
soluble enzyme
3.5
sucrose
-
pH 5.0, 40°C
3.57
sucrose
-
in MES buffer, pH 5.0, at 40°C
3.7
sucrose
-
beta-FFase L, pH 5.1
3.7
sucrose
-
pH 5.0, 37°C, isozyme IT II
3.8 - 4.4
sucrose
-
acid invertases
4
sucrose
pH 5.5, 42°C, alpha-D-glucopyranosyl-(1,2)-beta-D-fructofuranose
4
sucrose
-
pH and temperature not specified in the publication
4.4
sucrose
-
invertase II
4.4
sucrose
-
invertase P-1
4.41
sucrose
-
pH 6.5, 37°C, hyperbolic saturation kinetics
4.58
sucrose
-
pH 4.5, 30°C, isoenzyme AIV II
4.76
sucrose
-
beta-FFase L, pH 4.5
4.8
sucrose
-
pH and temperature not specified in the publication
4.89
sucrose
-
pH and temperature not specified in the publication
4.9
sucrose
-
in 0.2M sodium acetate buffer (pH 5.6), at 50°C
4.97
sucrose
pH 5.0, recombinant isozyme lbbetafruct3
5
sucrose
-
enzyme forms INV1 and INV3
5
sucrose
-
mutant Q176S, pH 5.0
5.8
sucrose
pH 5.6, 28°C, wild-type
5.89
sucrose
-
beta-FFase L, pH 3.6
6.2
sucrose
-
enzyme form F-1
6.2
sucrose
-
55°C, pH 4.6, invertase 2
6.4
sucrose
-
invertase II
6.4
sucrose
-
wild-type, pH 5.0
6.6
sucrose
-
invertase III
6.6
sucrose
-
pH 6.0, 37°C
6.7
sucrose
-
invertase II
6.9
sucrose
-
enzyme adsorbed on CM-cellulose
7
sucrose
-
mutant Q176E, pH 5.0
7
sucrose
-
mutant Y462A, pH 5.0
7.2
sucrose
-
invertase entrapped into calcium alginate beads
7.43
sucrose
-
immobilized enzyme, pH 6.0, 45°C
7.69
sucrose
-
beta-FFase E, pH 3.6
8
sucrose
-
mutant N254A, pH 5.0
8.1
sucrose
-
invertase I
8.8
sucrose
pH 5.6, 28°C, W440Y
8.9
sucrose
pH 7.7, 30°C, invertase InvB, wild-type enzyme
9
sucrose
-
mutant Q435A, pH 5.0
9.1
sucrose
-
free enzyme, pH 5.0, 30°C
9.8
sucrose
-
55°C, pH 4.6, invertase 1
9.85
sucrose
pH 7.5, 37°C, mutant enzyme E234A
10
sucrose
-
pH and temperature not specified in the publication
10.05
sucrose
-
25% xylitol, 55°C, pH 4.5
10.1
sucrose
pH 5.0, recombinant isozyme lbbetafruct2
10.69
sucrose
pH 5.0, 37°C
10.75
sucrose
-
30% glycerol, 55°C, pH 4.5
10.9
sucrose
-
pH 7.0, 37°C, isozyme IT I
11
sucrose
-
40°C, pH 5.5
11
sucrose
-
40°C, pH 5.5
11
sucrose
-
40°C, pH 5.5
11
sucrose
-
mutant Q228V, pH 5.0
11
sucrose
-
pH and temperature not specified in the publication
11
sucrose
-
pH and temperature not specified in the publication
11.5
sucrose
-
15% sorbitol, 55°C, pH 4.5
11.9
sucrose
-
enzyme form F-2
11.9
sucrose
-
in the presence of Mn2+, in 100 mM sodium acetate buffer, pH 5.0, at 50°C
12
sucrose
-
enzyme form INV2
12.3
sucrose
-
extracellular invertase I
12.5
sucrose
-
native invertase, 55°C, pH 4.5
13
sucrose
-
mutant S281I, pH 5.0
13.14
sucrose
pH 7.5, 37°C, mutant enzyme D63A
13.4
sucrose
-
in sodium acetate buffer, 100 mM, pH 4.5, at 60°C
13.4
sucrose
-
pH and temperature not specified in the publication
14
sucrose
-
85°C, pH 6.0
14
sucrose
-
pH and temperature not specified in the publication
14
sucrose
at pH 4.5 and 50°C
14.3
sucrose
-
pH 6.8, neutral invertase
15.1
sucrose
-
pH 8.0, alkaline invertase
16.66
sucrose
-
40% xylitol, pre-incubation at 80°C for 20 min, 55°C, pH 4.5
17.8
sucrose
at pH 4.5 and 45°C
17.85
sucrose
-
40% glycerol, pre-incubation at 80°C for 20 min, 55°C, pH 4.5
18.1
sucrose
pH 7.7, 30°C, invertase InvB, mutant enzyme R430N
18.6
sucrose
-
pH and temperature not specified in the publication
18.7
sucrose
-
pH 7.5, neutral invertase
19
sucrose
-
mutant N24S, pH 4.8, 50°C
19.23
sucrose
-
40% glycerol, 55°C, pH 9
20
sucrose
-
neutral and alkaline invertase
20.8
sucrose
pH 7.9, 30°C, invertase InvA, wild-type enzyme
21
sucrose
pH and temperature not specified in the publication
21.27
sucrose
-
40% sorbitol, pre-incubation at 80°C for 20 min, 55°C, pH 4.5
21.73
sucrose
-
40% xylitol, 55°C, pH 9
22.7
sucrose
-
in 100 mM sodium acetate buffer, pH 5.0, at 50°C
24.5
sucrose
-
free enzyme, pH 4.5, 57°C
25
sucrose
-
extracellular enzyme
25
sucrose
-
pH and temperature not specified in the publication
25 - 26
sucrose
-
extracellular enzyme
25.55
sucrose
-
40°C, pH 4.5
25.6
sucrose
-
isoforms EINV1, EIV2, EINV3, EINV4, pH 4.5, 25°C
26
sucrose
-
extracellular enzyme
27.1
sucrose
in 100 mM Na-acetate, pH 4.6, and 100 mM sucrose, at 35°C
27.1
sucrose
pH 7.9, 30°C, invertase InvA, mutant enzyme R429N
29
sucrose
-
mutant N142Y, pH 5.0
29.41
sucrose
-
native invertase, 55°C, pH 9
30.7
sucrose
pH and temperature not specified in the publication
35.67
sucrose
-
pH and temperature not specified in the publication
37.6
sucrose
-
immobilized enzyme, pH 4.5, 57°C
38
sucrose
-
pH 5.7, 37°C
38
sucrose
-
wild-type, pH 4.8, 50°C
38.6
sucrose
-
alkaline invertase, pH 6.5, 37°C
41
sucrose
-
pH 5.0, 35°C, invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter
41.2
sucrose
-
free enzyme
42
sucrose
-
pH 7.0, 30°C
46.5
sucrose
-
enzyme immobilized on polyurethane rigid adhesive foam, pH 5.0, 50°C
50
sucrose
-
pH 5.5, 40°C, deglycosylated invertase INVB
50
sucrose
-
pH 5.5, 40°C, invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter
51
sucrose
-
pH 5.5, 30°C, free chimeric fusion enzyme INVA-CBD
53.68
sucrose
-
pH 5.0, 37°C, wild-type enzyme
57
sucrose
Corynebacterium murisepticum
-
-
60
sucrose
-
pH and temperature not specified in the publication
61.2
sucrose
-
free enzyme, pH 5.0, 50°C
70.4
sucrose
-
covalently bound enzyme, pH 5.0, 30°C
78
sucrose
-
immobilized enzyme, 290 mM sucrose, room temperature, 50 mM sodium acetate buffer, pH 5
78.6
sucrose
pH 5.0, 60°C
83
sucrose
-
pH 5.0, 35°C, deglycosylated invertase INVA
86
sucrose
-
pH and temperature not specified in the publication
89.3
sucrose
pH 7.9, 30°C, invertase InvA, mutant enzyme R429A
93
sucrose
-
40°C, pH 5.0, without ultrasound
94
sucrose
-
40°C, pH 5.0, with ultrasound
98
sucrose
-
free enzyme, 290 mM sucrose, room temperature, 50 mM sodium acetate buffer, pH 5.5
98
sucrose
-
pH 5.5, 40°C, native invertase INVB
110
sucrose
-
pH 5.5, 30°C, free INVA
110
sucrose
-
pH 5.0, 35°C, native invertase INVA
130
sucrose
-
adsorbed enzyme, pH 5.0, 30°C
140.7
sucrose
-
pH 5.0, 37°C, mutant enzyme C317A
142.6
sucrose
-
pH 5.0, 37°C, mutant enzyme E316Q
153
sucrose
-
pH 5.5, 30°C, cellulose immobilized chimeric fusion enzyme INVA-CBD
160
sucrose
-
pH 5.0, 37°C
160.6
sucrose
-
pH 5.0, 50°C, 55 mg/ml
169.8
sucrose
-
pH 5.0, 37°C, mutant enzyme W159F
189
sucrose
-
pH 5.5, 30°C, Nylon-6 immobilized INVA
213.6
sucrose
-
pH 5.0, 37°C, mutant enzyme W159L
227
sucrose
-
pH 4.5, 35°C
227
sucrose
-
pH and temperature not specified in the publication
230
sucrose
-
in 50 mM sodium acetate buffer (pH 5.0), at 30°C
230
sucrose
-
pH and temperature not specified in the publication
290
sucrose
-
pH and temperature not specified in the publication
370
sucrose
-
pH 6.0, 37°C
370
sucrose
-
pH and temperature not specified in the publication
398
sucrose
-
pH 5.0, 37°C
470
sucrose
-
pH and temperature not specified in the publication
1300
sucrose
-
mutant N21S, pH 4.8, 50°C
5000
sucrose
-
mutant W19Y/N21S, pH 4.8, 50°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of soluble and micelle entrapped enzyme
-
additional information
additional information
-
enzyme in cells immobilized in gelatin hydrogels are analyzed concerning kinetics, thermostability, and reusability, overview
-
additional information
additional information
-
kinetics, isozymes SAI and CWI, isozyme Sai has a lower KM for sucrose and a higher KM for raffinose compared to isozyme CWI
-
additional information
sucrose
-
0.23 mg/ml, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003
-
value about, leaf, 20 days after anthesis
0.00125
-
value about, leaf, 4 days after anthesis
0.003
-
value about, leaf, 12 days after anthesis
0.0067
-
value about, leaf, 8 days after anthesis
0.0083
-
value about, leaf, 2 days before anthesis, day of anthesis and 4 days after anthesis
0.0116
-
matrix, 10 min, room temperature, control
0.014
-
untreated mitochondria, 37°C
0.0231
-
mitochondria, alamethicin treated to enable unrestricted transport, 37°C
0.0269
-
matrix, 10 min, 37°C
0.03
-
value about, mesocarp tissue, 20 days after anthesis
0.067
-
value about, mesocarp tissue, 16 days after anthesis
0.083
-
value about, mesocarp tissue, 8 and 12 days after anthesis
0.1
-
value about, mesocarp tissue, 2 days before anthesis
0.13
-
value about, mesocarp tissue, 2 days before anthesis and day of anthesis
0.15
-
value about, mesocarp tissue, 4 days after anthesis
0.2083
-
value about, mesocarp tissue, 16 days after anthesis
0.225
-
value about, mesocarp tissue, 12 days after anthesis
0.768
-
pH 5.0, 37°C, mutant enzyme W159L with substrate sucrose, 33.2% activity with substrate raffinose compared to wild-type
0.82
-
pH 6.5, 37°C, alkaline invertase
11.5
-
intracellular enzyme, crude protein cell extract
12.3
-
after purification, in 100 mM sodium citrate buffer (pH 4.5)
1200
1-kestose as substrate
1480
-
isoform EINV4, 25°C, pH 4.5
158.2
-
purified native enzyme
16.3
-
pH 5.0, 37°C, mutant enzyme C317A with substrate sucrose, 20.7% activity with substrate raffinose compared to wild-type
16.6
-
pH 6.5, 37°C, acid invertase
1695
purified recombinant His-tagged isozyme betafruct3
186
-
immobilized enzyme, pH 6.0, 45°C
20.6
-
cellulose immobilized chimeric fusion enzyme INVA-CBD
218
-
free enzyme, pH 6.0, 45°C
2180
-
after 51.4fold purification, at 30°C
2410
-
isoform EINV2, 25°C, pH 4.5
245.6
-
after 3.11fold purification, at pH 5.0 and 40 ?C
2470
-
isoform EINV3, 25°C, pH 4.5
25.6
-
free chimeric fusion enzyme INVA-CBD
26
-
purified isozyme IT II
28.8
-
purified isozyme IT I
3.3
-
enzyme expressed in Hansenula polymorpha
3.4
-
enzyme expressed in Pichia pastoris
3.9
-
crude extract, with sucrose as substrate, in 100 mM sodium acetate buffer, pH 5.0, at 50°C
30.73
-
pH 5.0, 37°C, mutant enzyme W159F with substrate sucrose, 41% activity with substrate raffinose compared to wild-type
3128
-
intracellular enzyme
3160
-
isoform EINV1, 25°C, pH 4.5
4.43
-
pH 5.0, 37°C, mutant enzyme E316Q with substrate sucrose, 15.5% activity with substrate raffinose compared to wild-type
4.7
-
extracellular enzyme, crude protein cell extract
42.4
-
crude extract, at 30°C
42.5
-
after 7.1fold purification, at pH 4.5, 60°C
456
-
Nylon-6 immobilized INVA
47.92
-
crude extract, at pH 5.0 and 40 ?C
4700
-
intracellular enzyme
4800
-
extracellular enzyme
5200
sucrose as substrate
553
purified recombinant isozyme lbbetafruct2
555
-
after 139.4fold purification, with sucrose as substrate, in 100 mM sodium acetate buffer, pH 5.0, at 50°C
6
-
crude extract, at pH 4.5, 60°C
6.58
-
pH 5.0, 37°C, wild-type enzyme with substrate sucrose
601
-
extracellular enzyme, pH 4.5, 60°C
70
purified recombinant isozyme lbbetafruct3
884.3
purified recombinant His-tagged isozyme betafruct2
90
palatinose as substrate
0.00083
-
value about, leaf, 12 and 16 days after anthesis
0.00083
-
value about, leaf, 20 days after anthesis
0.00167
-
value about, leaf, 16 days after anthesis
0.00167
-
value about, leaf, 2 days before anthesis and day of anthesis
0.00167
-
value about, leaf, 8 days after anthesis
0.02
-
-
0.02
-
soluble cell extract, in 100 mM sodium citrate buffer (pH 4.5)
0.1167
-
value about, mesocarp tissue, 4 days after anthesis
0.1167
-
value about, mesocarp tissue, day of anthesis
0.1917
-
value about, mesocarp tissue, 20 days after anthesis
0.1917
-
value about, mesocarp tissue, 8 days after anthesis
2560
-
F-form
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
maximum activity at 15% sorbitol (1.23-fold increase), increased activity from 5-20% solutions, 100 mM sucrose, 10 min, 55°C, 50 mM sodium acetate buffer, pH 4.5
additional information
-
maximum activity at 25% xylitol (1.57-fold increase), increased activity from 10-30% solutions, 100 mM sucrose, 10 min, 55°C, 50 mM sodium acetate buffer, pH 4.5
additional information
-
maximum activity at 30% glycerol (1.39-fold increase), increased activity from 10-40% solutions, 100 mM sucrose, 10 min, 55°C, 50 mM sodium acetate buffer, pH 4.5
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
mutant with 11.4% reduced neutral invertase activity compared to wild-type, with higher sucrose and lower glucose (-10% in leaves, -22% in roots) and fructose (-12% in leaves, -21% in roots) contents in 14-day-old mutant plants than in wild-type, part of the mutant phenotype is due to glucose deficit, mutant morphology phenotype is not fully expressed in 3% glucose medium
additional information
no activity with substrates: maltose (alpha-D-glucopyranosyl-(1,4)-D-glucopyranose), lactose (beta-D-galactopyranosyl-(1,4)-D-glucopyranose), leucrose (alpha-D-glucopyranosyl-(1,5)-D-fructofuranose)
additional information
-
no activity with substrates: maltose (alpha-D-glucopyranosyl-(1,4)-D-glucopyranose), lactose (beta-D-galactopyranosyl-(1,4)-D-glucopyranose), leucrose (alpha-D-glucopyranosyl-(1,5)-D-fructofuranose)
additional information
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown, reduced activity after feeding with sucrose observed
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
repressed and derepressed activities of wild-type and mutant enzymes in dry cell material, overview
additional information
-
-
additional information
-
Lin8-RNAi line 33 activity: 3.4 micromol/squaremeter/min, vacuolar invertase: 3.6 micromol/squaremeter/min
additional information
-
Lin8-RNAi line 50 activity: 3.6 micromol/squaremeter/min, vacuolar invertase: 5.6 micromol/squaremeter/min
additional information
-
Lin8-RNAi line 57 activity: 1.5 micromol/squaremeter/min, vacuolar invertase: 4.0 micromol/squaremeter/min
additional information
-
wild-type activity: 40.5 micromol/squaremeter/min, vacuolar invertase: 4.2 micromol/squaremeter/min
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
VIN activity in elongating fibers is approximately 4-6fold higher than that in leaves, stems, and roots. It is undetectable in fiberless cotton seed epidermis but becomes evident in initiating fibers and remains high during their fast elongation and drops when elongation slows. A genotype with faster fiber elongation has significantly higher fiber VIN activity and hexose levels than a slow-elongating genotype
brenda
-
-
brenda
-
invertase I is primarily localized in anthers, invertase II and II are present at 5% of invertase I activity. Much higher levels of invertase II and III are found in the nonanther organs of the flower
brenda
-
-
brenda
compared to invertase InvA, invertase InvB possesses a much higher catalytic activity. The higher activity may be responsible for the vital role of InvB in heterocyst development and nitrogen fixation
brenda
-
-
brenda
-
brenda
the enzyme is highly and specifically expressed in the midgut and silk gland
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
cell-wall invertase isozymes CIN1-3, 5, and 8, high expression level of CIN2, plant hormones abscisic acid and gibberellic acid induce cell wall isozyme CIN2 in peduncles antagonizing both peduncle elongation and maintenance of CIN2 transcript levels
brenda
-
brenda
-
-
brenda
expressed at high levels at both the transcriptional and translational levels. The enzyme might function as a digestive enzyme to hydrolyze sugar in the silk gland lumen
brenda
-
cell wall-bound isozyme Inv-CW has an essential function in carbohydrate supply
brenda
-
strong expression of isoform CWIN1
brenda
-
-
brenda
-
whole fly homogenates
brenda
-
brenda
expressed to a higher extent in promastigotes than in amastigotes
brenda
-
expressed to a higher extent in promastigotes than in amastigotes
brenda
expressed to a higher extent in promastigotes than in amastigotes
brenda
-
invertase I is primarily localized in anthers, invertase II and III are present in much smaller amounts
brenda
-
-
brenda
-
-
brenda
-
-
brenda
in the coat barely visible expression of OsCIN3, in the embryo very strong expression of OsCIN3, in the endosperm weak expression of OsCIN3
brenda
in the coat strong expression of OsCIN1, in the embryo barely visible expression of OsCIN1, in the endosperm no expression of OsCIN1
brenda
in the coat weak expression of OsCIN2, in the embryo strong expression of OsCIN2, in the endosperm strong expression of OsCIN2
brenda
-
-
brenda
-
invertase F-form and invertase S-form
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
of single cells from leaf explant
brenda
-
-
brenda
-
co-expression of isozyme CWI with inhibitor CIF
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
high invertase activity in the apical segment of the coleoptile, the level of activity decreases sharply with distance from the apex
brenda
-
a soluble and a cell wall-bound enzyme
brenda
-
-
brenda
-
-
brenda
-
isoenzyme P-2
brenda
-
microconidia
brenda
-
isoenzyme P-2
-
brenda
-
microconidia
-
brenda
-
-
brenda
of seed. Separate growth of cotyledon types, Cot and Cot E based on a unique differential regeneration response, in vitro on Gamborg's B5 basal nutrient medium, 2% sucrose, and supplemented with N6-benzyladenine. Temporal differences in acid invertase enzyme activity are observed in differentiating explants. In general all N6-benzyladenine levels and both in the presence and/or absence of sucrose, acid invertase levels are lower in Cot than Cot E explants. A higher frequency of regeneration of Cot E explants is positively correlated with higher invertase activity. Invertase gene expression is highest in Cot explants at 12 and 15 days following culture
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
of old cell cultures, isoenzyme P-2
brenda
-
of old cell cultures, isoenzyme P-2
-
brenda
-
-
brenda
-
the ability of the maturing embryo to maintain mitotic activity is mediated by metabolic signals of the enzyme from the seed coat
brenda
-
-
brenda
-
localization of the cell wall-bound isozyme in the transfer cell layer
brenda
-
-
brenda
-
-
brenda
-
low expression level of isozyme CWI, but high expression in androecium and gynoecium development
brenda
-
-
brenda
-
PaxgINV3 tightly regulated, probably floral-specific cell-wall invertase
brenda
-
brenda
highest expression
brenda
-
co-expression of isozyme CWI with endogenous proteinous inhibitor VIF in flowers
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
green and ripening
brenda
high expression in mature fruit
brenda
-
green and ripening
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
the vacuolar isozyme Inv-V is important in kernel development, overview
brenda
-
brenda
-
-
brenda
-
mature green
brenda
-
low activity
brenda
-
barley detectable
brenda
-
young and mature
brenda
-
mature
brenda
-
-
brenda
VIN activity in elongating fibers is approximately 4-6fold higher than that in leaves, stems, and roots
brenda
-
three soluble invertases
brenda
-
brenda
young and mature, expression of isozyme lbbetafruct3 is restricted to shoots and leaves
brenda
high expression
brenda
-
-
brenda
-
-
brenda
-
brenda
-
co-expression of isozyme CWIwith endogenous proteinous inhibitor CIF, green and senescent leaves
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
co-expression of isozyme CWI with endogenous proteinous inhibitor VIF in green leaves
brenda
expression of isoform LIN6 in sink tissues, such as pollen grains and vascular tissues of leaves and stems
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
-
isoenzyme P-1
brenda
-
isoenzyme P-1
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
cell wall-bound isozyme Inv-CW has an essential function in carbohydrate supply
brenda
expression of isoform LIN6 in sink tissues, such as pollen grains and vascular tissues of leaves and stems
brenda
expressed to a higher extent in promastigotes than in amastigotes. Induction increases over time and the strongest mRNA induction is observed at day 7, suggesting that invertase expression is highly expressed by promastigotes at stationary phase
brenda
-
expressed to a higher extent in promastigotes than in amastigotes. Induction increases over time and the strongest mRNA induction is observed at day 7, suggesting that invertase expression is highly expressed by promastigotes at stationary phase
brenda
expressed to a higher extent in promastigotes than in amastigotes. Induction increases over time and the strongest mRNA induction is observed at day 7, suggesting that invertase expression is highly expressed by promastigotes at stationary phase
brenda
in the anther strong expression of OsCIN2, in the ovary strong expression of OsCIN2, in the caryopsis day 4 strong expression of OsCIN2 (strong in vascular parenchyma of chalazal vein, weak in cross-cells, nucellar tissue, endosperm, and lateral vein, and not in pericarp), in the caryopsis day 7 strong expression of OsCIN2 (strong in vascular parenchyma of chalazal vein xylem and aleurone layer, weak in vascular parenchyma of chalazal vein phloem, cross-cells, nucellar projection, inner endosperm, very weakly in pericarp and nucellar epidermis), in the caryopsis day 15 very middle strong expression of OsCIN2, in the caryopsis day 25 almost no expression of OsCIN2
brenda
in the anther very strong expression of OsCIN3, in the ovary strong expression of OsCIN3, in the caryopsis day 4 strong expression of OsCIN3 (strong in vascular parenchyma of chalazal vein phloem, cross-cells, nucellar epidermis, endosperm, and lateral vein, weak in vascular parenchyma of chalazal vein xylem, nucellar projection, nucellus, and pericarp), in the caryopsis day 7 strong expression of OsCIN3 (strong in vascular parenchyma of chalazal phloem and aleurone layer, weak in vascular parenchyma of chalazal vein, cross-cells, nucellar projection, epidermis, and endosperm), in the caryopsis day 15 very weak expression of OsCIN3, in the caryopsis day 25 almost no expression of OsCIN3
brenda
in the anther weak expression of OsCIN1, in the ovary strong expression of OsCIN1, in the caryopsis day 4 strong expression of OsCIN1, in the caryopsis day 7 strong expression of OsCIN1, in the caryopsis day 15 very weak expression of OsCIN1, and in the caryopsis day 25 almost no expression of OsCIN1
brenda
-
brenda
-
low activity
brenda
-
-
brenda
-
aged slices of mature roots
brenda
-
-
brenda
-
brenda
VIN activity in elongating fibers is approximately 4-6fold higher than that in leaves, stems, and roots
brenda
-
-
brenda
-
-
-
brenda
-
high expression level of isozyme CWI
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
in the root tips, the activity of the vacuolar and cell wall-bound invertases increases markedly under water stress resulting in the accumulation of hexoses (glucose and fructose) that contributes significantly to osmotic adjustment. A transient rise in hydrogen peroxide (H2O2) precedes the enhancement of invertases upon exposure to osmotic stress. H2O2 probably generated by a NADPH oxidase is required as a signalling molecule for the up-regulation of the vacuolar invertase activity in the root tips under osmotic stress, thereby enhancing the capacity for osmotic adjustment
brenda
-
brenda
-
-
brenda
-
-
brenda
VIN activity is undetectable in fiberless cotton seed epidermis but becomes evident in initiating fibers
brenda
-
seed coat invertase expression may be required for adequate sugar supply and balanced sugar and auxin signaling to support filial tissue development
brenda
-
-
brenda
expression in germinating seed and seedling
brenda
-
expression of isozyme Inv-CW in the thin-walled parenchyma of the seed coat, the site of assimilate unloading into the apoplast
brenda
-
cell wall invertase INCW2 localizes exclusively to the basal endosperm transfer cells of developing seeds
brenda
-
highest activity at the apex of the coleoptile, much lower in the primary leaf, mesocotyl and root
brenda
-
-
brenda
-
-
brenda
OsCIN3 is more constitutively expressed in all sink and source tissues
brenda
strong expression of OsCIN1 (sink and source tissues)
brenda
strong expression of OsCIN2 (sink tissues)
brenda
-
-
brenda
expression in germinating seed and seedling
brenda
-
-
brenda
-
-
brenda
expression of isozyme lbbetafruct3 is restricted to shoots and leaves
brenda
-
brenda
-
shoot of etiolated seedling
brenda
-
-
brenda
-
brenda
VIN activity in elongating fibers is approximately 4-6fold higher than that in leaves, stems, and roots
brenda
-
-
brenda
-
brenda
expression of isoform LIN6 in sink tissues, such as pollen grains and vascular tissues of leaves and stems
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
in the shoot strong expression of OsCIN1, in the root strong expression of OsCIN1, in the sink leaf blade strong expression of OsCIN1, in the source leaf blade weak expression of OsCIN1, in the leaf sheath weak expression of OsCIN1, in the internode weak expression of OsCIN1
brenda
in the shoot strong expression of OsCIN3, in the root strong expression of OsCIN3, in the sink leaf blade very strong expression of OsCIN3, in the source leaf blade strong expression of OsCIN3, in the leaf sheath strong expression of OsCIN3, in the internode strong expression of OsCIN3
brenda
in the shoot weak expression of OsCIN2, in the root weak expression of OsCIN2, in the sink leaf blade strong expression of OsCIN2, in the source leaf blade no expression of OsCIN2, in the leaf sheath no expression of OsCIN2, in the internode strong expression of OsCIN2
brenda
-
PaxgINV1 exclusively involved in dormancy processes, PaxgINV2 rather in phloem uploading and providing actively growing tissue such as xylem
brenda
additional information
-
culture conditions of wild-type and mutant strains: preferred as carbohydrate and nitrogen sources are wheat bran and corn steep liquor, pH 5.5-6.5, optimal conditions, overview, fermentation kinetics of wild-type and mutant strains with different substrates in submerged fermentations, overview
brenda
additional information
isozyme lbbetafruct2 is expressed in most tissues, except for mature leaves and sprouting storage roots, exspecially in sink organs
brenda
additional information
isozyme lbbetafruct2 is expressed in most tissues, except for mature leaves and sprouting storage roots, exspecially in sink organs
brenda
additional information
-
isozyme lbbetafruct2 is expressed in most tissues, except for mature leaves and sprouting storage roots, exspecially in sink organs
brenda
additional information
-
dark-grown Nicotiana tabacum cells transformed with Agrobacterium tumefaciens
brenda
additional information
-
tissue-specific expression of isozymes at flowering and during drought or heat stress, overview
brenda
additional information
-
tomato lines with strongly reduced source leaf cell wall-bound invertase activity by RNAi inhibition, 10-15% source leaf activity, while sink leaves and petioles still have 40-60% of wild-type activity, no alterations in other organs and tissue: Lin8-RNAi line 33, line 50, line 57, gene-silencing
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
102000
-
2 * 102000, S-form, SDS-PAGE
104000
-
x * 58788, MALDI-TOF of deglycosylated isoforms EINV1-EINV4. x * 104000, MALDI-TOF of isoforms EINV1, EINV3, EINV4. x * 101000, MALDI-TOF of isoform EINV2
1070000
-
non-denaturing PAGE
11000
-
7 * 11000, gel filtration in presence of SDS
110000
-
1 * 110000, F-invertase, SDS-PAGE
112500
-
pH 8.3, dimeric enzyme form, gel filtration
126000
-
4 * 126000, alkaline invertase, SDS-PAGE
140000
-
non-denaturing PAGE
155000
-
invertase IIb, gel filtration
170000
-
enzyme expressed in Pichia pastoris, gel filtration
180000
-
x * 180000, SDS-PAGE
185000
-
S-invertase, non-denaturing PAGE
190000
-
enzyme expressed in Hansenula polymorpha, gel filtration
200000
smear band in activity-stained gel, probably the about 270 kDa glycosylated functional active homodimer
216000
-
deglycosylated enzyme, gel filtration
22000
-
x * 22000 and x * 45000, acid invertase, x * 30000, alkaline invertase, SDS-PAGE
224000
-
25°C, isoenzyme P-1, gel filtration
225000 - 250000
-
non-denaturing PAGE
266000
-
4°C, isoenzyme P-2, gel filtration
26900
-
1 * 46700 + 1 * 26900, SDS-PAGE
295000
-
4°C, isonenzyme P-1, gel filtration
30000
-
x * 22000 and x * 45000, acid invertase, x * 30000, alkaline invertase, SDS-PAGE
30900
x * 30900, calculated from amino acid sequence
31300
x * 31300, electrospray ionization mass spectrometry
346000
-
native enzyme, gel filtration
380000
-
acid invertase, gel filtration
40000
-
x * 66000 + x * 43000 + x * 40000, SDS-PAGE
409000
-
pH 4.9, tetrameric enzyme form, gel filtration
41000
-
2 * 41000, SDS-PAGE
43000
-
x * 66000 + x * 43000 + x * 40000, SDS-PAGE
44298
-
1 * 47000, SDS-PAGE, 1 * 44298, MALDI TOF-MS
456000
-
neutral invertase, gel filtration
46700
-
1 * 46700 + 1 * 26900, SDS-PAGE
48000
-
invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter, SDS-PAGE
48500
-
non-denaturing PAGE
50000
-
4 * 50000, isozymes SAI and CWI, SDS-PAGE
504000
-
alkaline invertase, gel filtration
53000
-
x * 53000, SDS-PAGE
53800
mature protein after removal of the signal peptide, calculated from sequence
54870
x * 55000, SDS-PAGE, x * 54870, MALDI-MS
55000
x * 55000, SDS-PAGE, x * 54870, MALDI-MS
585000
8 * 585000, calculated from amino acid sequence
58788
-
x * 58788, MALDI-TOF of deglycosylated isoforms EINV1-EINV4. x * 104000, MALDI-TOF of isoforms EINV1, EINV3, EINV4. x * 101000, MALDI-TOF of isoform EINV2
59156
x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE
59792
mature enzyme without signal peptide, calculated from sequence
60300
-
x * 66000, SDS-PAGE, x * 60300, MALDI TOF-MS
60566
x * 60566, calculated from amino acid sequence
60700
x * 60700, purified deglycosylated protein, SDS-PAGE
63000
-
x * 63000, SDS-PAGE
63450
-
calculated from DNA sequence
63900
-
x * 63900, calculated from amino acid sequence
64200
x * 64200, isoform Cwinv-1, calculated from amino acid sequence
66700
x * 66700, calculated from amino acid sequence
67500
-
2 * 67500, gel filtration
69000
-
x * 69000, SDS-PAGE
69114
x * 69114, mass spectrometry
70100
recombinant His-tagged isozyme betafruct2, gel filtration
70400
x * 70400, isoform Vinv-1, calculated from amino acid sequence
71000
-
theoretical from nanoLC-chip-MS/MS analysis
71500
x * 71500, isoform VINV3, calculated from amino acid sequence
72600
recombinant His-tagged isozyme betafruct3, gel filtration
73300
x * 73300, isoform VINV1, calculated from amino acid sequence
73500
x * 73500, isoform VINV2, calculated from amino acid sequence
75760
-
pH 9.4, monomeric enzyme form, gel filtration
76200
-
gel filtration chromatography
82500
-
2 * 82500, gel filtration
84300
estimated from amino acid sequence
94000
-
F-invertase, non-denaturing PAGE
100000
-
gel filtration
100000
-
x * 100000, SDS-PAGE
101000
SDS-PAGE
101000
-
x * 58788, MALDI-TOF of deglycosylated isoforms EINV1-EINV4. x * 104000, MALDI-TOF of isoforms EINV1, EINV3, EINV4. x * 101000, MALDI-TOF of isoform EINV2
108000
-
invertase II, gel filtration
108000
-
x * 108000, isoenzyme P-1, SDS-PAGE
115000
-
2 * 115000, SDS-PAGE
115000
-
2 * 115000, SDS-PAGE
116000
-
-
116000
-
invertase IIa, gel filtration
116000
x * 116000, purified glycoprotein, SDS-PAGE
130000
-
gel filtration
135000
-
-
135000
-
intracellular enzyme
136000
-
-
150000
-
-
150000
-
2 * 150000, SDS-PAGE
158000
-
gel filtration
158000
-
4°C, isoenzyme P-2, gel filtration
160000
-
-
160000
SDS-PAGE and amino acid sequencing
205000
-
or hexamer, 5 * or 6 * 205000, SDS-PAGE
205000
-
or pentamer, 6 * or 5 * 205000, SDS-PAGE
210000
-
equilibrium sedimentation centrifugation
210000
-
2 * 210000, SDS-PAGE
210000
-
1 * 210000, SDS-PAGE of extracellular enzyme
220000
-
gel filtration
220000
-
isozymes SAI and CWI
240000
-
gel filtration
240000
-
isozyme IT I, gel filtration
270000
-
gel filtration
270000
-
equilibrium sedimentation
270000
-
extracellular enzyme, gel filtration
28000
-
gel filtration
280000
-
gel filtration
280000
-
S-form, nondenaturing PAGE
300000
-
gel filtration
300000
-
non-denaturing PAGE
340000
-
-
430000
-
-
430000
-
TSK Super SW3000 column HPLC
45000
-
SDS-PAGE
45000
-
x * 22000 and x * 45000, acid invertase, x * 30000, alkaline invertase, SDS-PAGE
46000
-
deglycosylated invertase INVB, SDS-PAGE
46000
-
native invertase INVB, SDS-PAGE
47000
-
-
47000
-
gel filtration and PAGE
47000
-
2 * 47000, SDS-PAGE
47000
-
2 * 47000, SDS-PAGE
57000
-
gel filtration
57000
-
8 * 57000, neutral invertase, SDS-PAGE
57000
-
deglycosylated invertase INVA, SDS-PAGE
57000
-
native invertase INVA, SDS-PAGE
58000
-
-
58000
-
4 * 58000, SDS-PAGE
58000
-
x * 58000, SDS-PAGE
59000
-
invertase I, gel filtration
59000
-
1 * 59000, SDS-PAGE
60000
-
-
60000
native PAGE, SDS-PAGE produced only fragments of 46.3, 27.7, 18.6, and 16.8 kDa, in red fruits additionally a 44 kDa fragment, and a 35 kDa fragment shown to be produced by in planta proteolysis of invertase
60000
-
4 * 60000, isozyme IT I, SDS-PAGE
60000
-
x * 60000, native enzyme, SDS-PAGE
60000
x * 60000, recombinant His-tagged enzyme, SDS-PAGE
60000
x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE
60000
enzyme expressed in Escherichia coli, SDS-PAGE
62000
-
F-form, non-denaturing PAGE
62000
-
x * 62000, SDS-PAGE
62500
calculated from sequence
62500
-
1 * 62500, F-form, SDS-PAGE
64000
-
invertase I, gel filtration
64000
-
2 * 64000, SDS-PAGE
64000
x * 64000, SDS-PAGE
65000
-
SDS-PAGE
65000
x * 65000, SDS-PAGE
65000
x * 65000, MALDI-TOF mass spectrometry
66000
-
gel filtration
66000
-
neutral invertase, gel filtration
66000
-
isoenzyme AIV I, gel filtration
66000
after treatment with PNGase F representing the unglydosylated enzyme, thus N-linked oligosaccharides appear to represent about 60% (the other part) of the total protein mass
66000
-
2 * 66000, SDS-PAGE
66000
-
x * 66000 + x * 43000 + x * 40000, SDS-PAGE
66000
-
x * 66000, SDS-PAGE, x * 60300, MALDI TOF-MS
67000
-
-
67000
-
6xHis-tagged enzyme INVA, 57 kDa from INVA, SDS-PAGE
67000
-
1 * 67000, isozyme IT II, SDS-PAGE
68000
-
isozyme IT II, gel filtration
68000
1 * 68000, recombinant His-tagged enzyme
68000
-
invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter, SDS-PAGE
68200
1 * 77500, recombinant His-tagged isozyme betafruct2, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct2, SDS-PAGE
68200
1 * 77500, recombinant His-tagged isozyme betafruct3, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct3, SDS-PAGE
70000
Corynebacterium murisepticum
-
x * 70000, SDS-PAGE
70000
-
1 * 70000, SDS-PAGE
70000
x * 70000, calculated from amino acid sequence
70000
x * 70000, deglycosylated protein, SDS-PAGE
72000
-
gel filtration
73000
-
1 * 73000, SDS-PAGE
73000
x * 73000, mass spectrometry
74000
-
-
77500
1 * 77500, recombinant His-tagged isozyme betafruct2, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct2, SDS-PAGE
77500
1 * 77500, recombinant His-tagged isozyme betafruct3, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct3, SDS-PAGE
78000
-
gel filtration
78000
-
chimeric fusion enzyme INVA-CBD, 57 kDa from INVA, SDS-PAGE
78000
-
2 * 78000, S-invertase, SDS-PAGE
79000
-
2 * 79000, SDS-PAGE
79000
x * 79000, glycoprotein, SDS-PAGE
80000
-
-
80000
-
1 * 80000, isoenzyme AIV I, SDS-PAGE
84000
-
-
84000
-
x * 84000, isoenzyme P-2, SDS-PAGE
85000
-
2 * 85000, SDS-PAGE
85000
enzyme expressed in Pichia pastoris, SDS-PAGE
92000
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heptamer
-
7 * 11000, gel filtration in presence of SDS
heterodimer
-
1 * 46700 + 1 * 26900, SDS-PAGE
pentamer
-
or hexamer, 5 * or 6 * 205000, SDS-PAGE
trimer
-
x * 66000 + x * 43000 + x * 40000, SDS-PAGE
?
x * 64200, isoform Cwinv-1, calculated from amino acid sequence
?
x * 70400, isoform Vinv-1, calculated from amino acid sequence
?
-
x * 60000, native enzyme, SDS-PAGE
?
-
x * 60000, native enzyme, SDS-PAGE
-
?
-
x * 120000-130000, two enzyme forms, SDS-PAGE
?
-
x * 120000-130000, two enzyme forms, SDS-PAGE
-
?
-
x * 66000, SDS-PAGE, x * 60300, MALDI TOF-MS
?
-
x * 66000, SDS-PAGE, x * 60300, MALDI TOF-MS
-
?
x * 60000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 59156, calculated for recombinant protein. x * 60000, SDS-PAGE
?
Corynebacterium murisepticum
-
x * 70000, SDS-PAGE
?
x * 59792, mature enzyme without signal peptide, calculated from sequence
?
-
x * 84000, isoenzyme P-2, SDS-PAGE
?
-
x * 108000, isoenzyme P-1, SDS-PAGE
?
x * 71500, isoform VINV3, calculated from amino acid sequence
?
x * 73300, isoform VINV1, calculated from amino acid sequence
?
x * 73500, isoform VINV2, calculated from amino acid sequence
?
-
x * 63900, calculated from amino acid sequence
?
-
x * 63900, calculated from amino acid sequence
-
?
-
x * 22000 and x * 45000, acid invertase, x * 30000, alkaline invertase, SDS-PAGE
?
-
x * 210000-270000, SDS-PAGE
?
-
x * 58788, MALDI-TOF of deglycosylated isoforms EINV1-EINV4. x * 104000, MALDI-TOF of isoforms EINV1, EINV3, EINV4. x * 101000, MALDI-TOF of isoform EINV2
?
x * 116000, purified glycoprotein, SDS-PAGE
?
x * 30900, calculated from amino acid sequence
?
x * 31300, electrospray ionization mass spectrometry
?
x * 60700, purified deglycosylated protein, SDS-PAGE
?
-
x * 180000, SDS-PAGE
-
?
x * 73000, mass spectrometry
?
x * 60566, calculated from amino acid sequence
?
x * 69114, mass spectrometry
?
x * 70000, deglycosylated protein, SDS-PAGE
?
x * 79000, glycoprotein, SDS-PAGE
?
x * 70000, calculated from amino acid sequence
?
x * 55000, SDS-PAGE, x * 54870, MALDI-MS
?
x * 65000, MALDI-TOF mass spectrometry
?
x * 66700, calculated from amino acid sequence
?
-
x * 46000, deglycosylated invertase INVB, SDS-PAGE
?
-
x * 46000, native invertase INVB, SDS-PAGE
?
-
x * 48000, invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter, SDS-PAGE
?
-
x * 57000, deglycosylated invertase INVA, SDS-PAGE
?
-
x * 57000, native invertase INVA, SDS-PAGE
?
-
x * 68000, invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter, SDS-PAGE
?
-
x * 46000, deglycosylated invertase INVB, SDS-PAGE
-
?
-
x * 46000, native invertase INVB, SDS-PAGE
-
?
-
x * 48000, invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter, SDS-PAGE
-
?
-
x * 57000, deglycosylated invertase INVA, SDS-PAGE
-
?
-
x * 57000, native invertase INVA, SDS-PAGE
-
dimer
-
2 * 115000, SDS-PAGE
dimer
-
2 * 115000, SDS-PAGE
-
dimer
-
2 * 78000, S-invertase, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 115000, SDS-PAGE
dimer
-
2 * 66000, SDS-PAGE
dimer
-
2 * 66000, SDS-PAGE
-
dimer
-
2 * 32000, invertase 2, SDS-PAGE
dimer
-
2 * 32000, invertase 2, SDS-PAGE
-
dimer
-
2 * 150000, SDS-PAGE
dimer
-
2 * 210000, SDS-PAGE
dimer
-
2 * 102000, S-form, SDS-PAGE
dimer
-
2 * 64000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
hexamer
invertase InvA exists as a hexamer in both crystal and solution
hexamer
-
or pentamer, 6 * or 5 * 205000, SDS-PAGE
homodimer
-
2 * 79000, SDS-PAGE
homodimer
-
2 * 67500, gel filtration
homodimer
the enzyme forms homodimers in solution which are formed via the interaction of beta-sandwich domains
homodimer
-
the enzyme forms homodimers in solution which are formed via the interaction of beta-sandwich domains
-
homodimer
-
2 * 85000, SDS-PAGE
homodimer
-
2 * 82500, gel filtration
monomer
-
1 * 84000, SDS-PAGE
monomer
-
1 * 110000, F-invertase, SDS-PAGE
monomer
-
1 * 59000, SDS-PAGE
monomer
1 * 77500, recombinant His-tagged isozyme betafruct2, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct2, SDS-PAGE
monomer
1 * 77500, recombinant His-tagged isozyme betafruct3, SDS-PAGE, 1 * 68200, deglycosylated recombinant His-tagged isozyme betafruct3, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
monomer
-
1 * 62500, F-form, SDS-PAGE
monomer
1 * 68000, recombinant His-tagged enzyme
monomer
-
1 * 73000, SDS-PAGE
monomer
-
1 * 73000, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 210000, SDS-PAGE of extracellular enzyme
monomer
-
1 * 67000, isozyme IT II, SDS-PAGE
monomer
-
1 * 80000, isoenzyme AIV I, SDS-PAGE
monomer
-
1 * 28000, native and subunit molecular mass almost identical on SDS-PAGE
monomer
glycosylated monomer composed of several splitting fragments that have to be tightly associated for enzyme activity to occur
monomer
-
1 * 47000, SDS-PAGE, 1 * 44298, MALDI TOF-MS
monomer
-
1 * 58000, SDS-PAGE
octamer
-
8 * 57000, neutral invertase, SDS-PAGE
octamer
8 * 585000, calculated from amino acid sequence
tetramer
-
4 * 126000, alkaline invertase, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 50000, isozymes SAI and CWI, SDS-PAGE
tetramer
-
4 * 60000, isozyme IT I, SDS-PAGE
additional information
-
the enzyme is highly polymorphic
additional information
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct2, overview
additional information
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct2, overview
additional information
-
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct2, overview
additional information
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct3, overview
additional information
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct3, overview
additional information
-
analysis of conserved notifs and segments in the secondray structure of isozyme lbbetafruct3, overview
additional information
-
may be composed of more than one type of subunit
additional information
-
two protein bands with MW of 19000 Da and 21000 Da are detected by SDS-PAGE
additional information
-
the intracellular enzyme exists as a monomer at pH 9.4, a dimer at pH 8.3, and an apparent octamer at pH 4.9
additional information
-
the native extracellular enzyme is oligomeric, the native intracellular enzyme is monomeric
additional information
three-dimensional structure analysis
additional information
-
three-dimensional structure analysis
additional information
the enzyme is bimodular with a five bladed beta-propeller catalytic domain linked to a beta-sandwich, three-dimensional structure, overview
additional information
-
the enzyme is bimodular with a five bladed beta-propeller catalytic domain linked to a beta-sandwich, three-dimensional structure, overview
additional information
-
three-dimensional structure analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
W440Y
almost doubled transglycosylation activity
C294Y
-
i.e. mutant sicy-192. Mutation leads to inhibition of cotyledon greening by treatments with sugars such as sucrose, glucose, and fructose. The greening of cotyledons in the knock-out INV-E lines is not inhibited by treatment with the sugars. A recombinant INV-E:C294Y protein has the same enzymatic activity as a recombinant INV-E protein, suggesting that the Cys-294 residue of INV-E is important for its functions in the chloroplasts. On treatment with sucrose, the expression of photosynthesis-related genes is weaker in seedlings of mutant plants than wild-type seedlings, whereas the activity of nitrate reductase is stronger in the mutant plants than wild-type plants
D239A
-
shows a 6fold increase in KM and 1-kestose exohydrolase activity
S547A
the mutant is unable to interact with 14-3-3 protein
C317A
-
2.5fold invertase activity increase, 20.7% activity with substrate raffinose compared to wild-type
D135E
-
no invertase activity
D135N
-
no invertase activity
D260E
-
no invertase activity
D260N
-
no invertase activity
E316A
-
no invertase activity
E316Q
-
67.3% invertase activity retained, 15.5% activity with substrate raffinose compared to wild-type
R259K
-
no invertase activity
Rs59L
-
no invertase activity
W159F
-
4.7fold invertase activity increase, 41% activity with substrate raffinose compared to wild-type
W159L
-
11.7% invertase activity retained, 33.2% activity with substrate raffinose compared to wild-type
D181A
mutant enzyme shows no detectable activity
D63A
catalytic efficiency (kcat/Km) of the mutant enzyme is 1.6% compared to the catalytic efficiency of the wild-type enzyme
E234A
catalytic efficiency (kcat/Km) of the mutant enzyme is 1.8% compared to the catalytic efficiency of the wild-type enzyme
R429A
catalytic efficiency (kcat/Km) of the mutant enzyme is 9% compared to the catalytic efficiency of the wild-type enzyme
R429N
catalytic efficiency (kcat/Km) of the mutant enzyme is 20% compared to the catalytic efficiency of the wild-type enzyme
R430A
mutant enzyme shows no detectable activity
R430N
catalytic efficiency (kcat/Km) of the mutant enzyme is 16% compared to the catalytic efficiency of the wild-type enzyme
R205G
-
mutant Oscyt-inv1 shows abnormal phenotypes with short primary, adventitious, and lateral roots (reduced cell lengths, disarray of cells but radial pattern conserved), floral transition delay, low seed setting rate, low pollen fertility
D22N
-
activity bleow detection limit with sucrose. Increase in transfructosylating activity
F82W
-
71% of wild-type activity
K185R
mutant enzyme K185R shows higher stability than wild-type enzyme at 40°C-50°C. These results suggest that the deubiquitination of K185 slightly affects the thermal stability of SUC2
N21S
-
104% of wild-type activity with sucrose. Large increase in transfructosylating activity
N228A
-
138% of wild-type activity
N228A/N21S
-
20% of wild-type activity
N228R
-
23% of wild-type activity, no transfructosylating activity
N228R/N21S
-
4% of wild-type activity
N24S
-
17% of wild-type activity with sucrose. Large increase in transfructosylating activity
P205V
-
112% of wild-type activity with sucrose. Large increase in transfructosylating activity
P205V/W19Y/N21S
-
3% of wild-type activity with sucrose. Large increase in transfructosylating activity
W19Y
-
175% of wild-type activity with sucrose. Increase in transfructosylating activity
W19Y/N21S
-
41% of wild-type activity with sucrose. Large increase in transfructosylating activity
W19Y/N21S/N24S
-
2% of wild-type activity with sucrose. Large increase in transfructosylating activity
W19Y/N24S
-
8% of wild-type activity with sucrose. Large increase in transfructosylating activity
W287Y
-
4% of wild-type activity with sucrose. Increase in transfructosylating activity
W291Y
-
32% of wild-type activity with sucrose. Increase in transfructosylating activity
K185R
-
mutant enzyme K185R shows higher stability than wild-type enzyme at 40°C-50°C. These results suggest that the deubiquitination of K185 slightly affects the thermal stability of SUC2
-
D50A
-
no catalytic activity
E230A
-
no catalytic activity
N142Y
-
large decrease in activity against nystose
N254A
-
large decrease in activity against nystose
Q176E
-
moderate change in catalytic activity
Q176S
-
moderate change in catalytic activity
Q228V
-
strikingly large reduction in the catalytic efficiency of sucrose , inulin and especially nystose
Q435A
-
significant decrease in catalytic efficiency against inulin
S281I
-
strikingly large reduction in the catalytic efficiency of sucrose , inulin and especially nystose
Y462A
-
significant decrease in catalytic efficiency against inulin
N119D
the mutant shows reduced activity compared to the wild type enzyme
N184D
the mutant shows reduced activity compared to the wild type enzyme
N516D
the mutation dramatically affects the folding of the protein. The mutant is inactive
N52D
the mutant shows reduced activity compared to the wild type enzyme
N52D/N119D/N184D
the mutant shows reduced activity compared to the wild type enzyme
N52D/N119D/N184D/N516D
the mutations dramatically affect the folding of the protein. The mutant is inactive
E190A
site-directed mutagenesis, inactivated mutant
E190D
site-directed mutagenesis, inactivated mutant
additional information
upon introduction to Arabidopsis thaliana, GhVIN1 complements the short-root phenotype of a VIN T-DNA mutant and enhances the elongation of root cells in the wild type
additional information
-
upon introduction to Arabidopsis thaliana, GhVIN1 complements the short-root phenotype of a VIN T-DNA mutant and enhances the elongation of root cells in the wild type
additional information
-
isolation of mutant with a premature stop codon and with missense mutations. Recovery of homozygous mutants is problematic, but their phenotype shows a severe reduction in growth of the root and the shoot, a change in cellular development, and impaired flowering. The cellular organization of both roots and leaves is altered, leaves are smaller and thicker with extra layers of cells and roots show an extended and broader zone of cell division. Moreover, anthers contain no pollen. Both heterozygotes and homozygous mutants show decreased amounts of enzyme activity in nodules and shoot tips. Shoot tips also contain up to a 9fold increased level of sucrose. However, mutants are capable of forming functional root nodules
additional information
isolation of mutant with a premature stop codon and with missense mutations. Recovery of homozygous mutants is problematic, but their phenotype shows a severe reduction in growth of the root and the shoot, a change in cellular development, and impaired flowering. The cellular organization of both roots and leaves is altered, leaves are smaller and thicker with extra layers of cells and roots show an extended and broader zone of cell division. Moreover, anthers contain no pollen. Both heterozygotes and homozygous mutants show decreased amounts of enzyme activity in nodules and shoot tips. Shoot tips also contain up to a 9fold increased level of sucrose. However, mutants are capable of forming functional root nodules
additional information
-
isolation of mutant with a premature stop codon, mutation has no effect on enzyme activity nor does it show a visible phenotype
additional information
isolation of mutant with a premature stop codon, mutation has no effect on enzyme activity nor does it show a visible phenotype
additional information
-
construction of transgenic plants: tissue-specific suppression of cell wall-bound isozyme Inv-CW or Nin88 by antisense expression leads to a developmental block during early stages of pollen development, the phenotype can be rescued by external supply of sucrose or glucose, expression of Chenopodium rubrum cell wall-bound isozyme Cin1 in transgenic tobacco plants leads to delayed senescence with the recombinant enzyme substituting cytokinin in function
additional information
expression of CIN1 in roots of Arabidopsis thaliana leads to early flowering and an increase in whole plant biomass
additional information
-
enzyme immobilized on montmorillonite K-10 clay shows improved pH and thermal stabilities
additional information
-
enzyme in cells immobilized in gelatin hydrogels are analyzed concerning kinetics, thermostability, and reusability, overview
additional information
-
mutant UME-2 is a hyperproducer of FFase, mutant MNNG-5 gives an approximately 3fold increase in FFase production, mutants are created randomly by exposure to N-methyl-N-nitro-N-nitroso-guanidine and ethyl-methane sulfonate
additional information
-
isolation of 14 invertase mutants, random spore and functional analysis, partitioning into four groups, activities and degree of repression, overview
additional information
-
maize plant mutants miniature-1, mn-1, are deficient in cell wall-bound isozyme Inv-CW and show a defective development of endosperm in kernels, overview
additional information
-
chimeric fusion enzyme INVA-CBD gene produced from enzyme gene invA and binding domain gene bcd from Cellulomonas fimi
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10 - 50
-
recombinant truncated cytosolic protein
100
-
20 min, about 35% loss of activity of S-form, about 15% loss of activity of the f-form
22
after 6 h of incubation the percentage of activity is 85%
25 - 40
-
chimeric fusion enzyme INVA-CBD: free enzyme retains 90-100% activity at 25°C, while immobilized one drops to about 42% after 3 h, at 40°C free chimeric fusion enzyme INVA-CBD retains 20% activity after 20 min, while immobilized enzyme's activity ceases
25 - 50
at 50°C or higher, no activity can be detected, whereas at lower temperatures, the SucB specific activity remains relatively high, with 50% activity remaining at 25°C
30 - 50
-
INVA: 100% activity retained after 7 h in free and immobilized INVA at 30°C, about 50% retained at 40°C in both enzyme forms, after 1 h at 50°C INVA activity ceases quickly retaining less than 20% activity while the immobilized INVA retains 70% activity after 10 min, 50 mM acetate buffer, pH 5.5
30 - 60
-
high stability at 30°C (after 13 days 40% remaining activity). At 60°C, a residual invertase activity of about 14% is observed, and above 65°C, all invertase activities are inactivated due enzyme denaturation within 30 min. For 45°C, an invertase activity loss of about 45 and 70% is observed within 3 and 6 h, respectively, with the total enzyme denaturation occurring within around 24 h
35
-
t1/2 of invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter is 900 min, invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter is 80 min
35 - 45
-
after deglycosylation of the enzymes, denoted D-INVAAOX1and D-INVBAOX1, they exhibit a 1.3- to 5-fold lower thermal stability than the glycosylated forms at temperatures of 35-45°C
4 - 55
1 h, the enzyme retains at least 80% of its activity
40 - 50
mutant enzyme K185R shows higher stability than wild-type enzyme at 40°C-50°C
40 - 85
minor activity loss after 40 days at 40-50°C, 50% retained after 1 d at 60°C, inactivation after 10 min at 85°C, pre-incubation for 10-120 min at 60-85°C: 50% activity loss from 66-71°C, 50 mM sodium phosphate buffer, pH 5.5, remaining activity measured at 42°C
46
-
30 min, 50% loss of activity
53.8
Tm-value, thermal denaturations transition of Bmsuc1 is a cooperative process
55 - 70
-
the enzyme remains stable for 1 h at 55°C when diluted in water. The extracellular invertase is fully stable at lower temperatures, but half-lives of 40 and 5 min are estimated at 60 and 70°C, respectively
60 - 70
recombinant enzyme shows drastic loss of activity from 60°C to 70°C
60 - 80
-
the activity slowly decreases at 60°C, drops significantly at 70°C, and is almost wholly lost at 80°C
61
-
melting point, isoform EINV4
61.8
-
melting point, isoform EINV3
62.5
-
melting point, isoform EINV2
64
-
melting point, isoform EINV1
72
-
20 min, pH 9.0, thermal denaturation starts with 30% sorbitol
73
-
20 min, pH 9.0, thermal denaturation starts with 20% xylitol or 40% sorbitol
79
-
20 min, pH 4.5, thermal denaturation starts with 10% glycerol or xylitol, or 20% sorbitol
80 - 85
-
retains at least 50% of initial activity for 6 h
81
-
20 min, pH 4.5, thermal denaturation starts with 30% sorbitol
82
-
20 min, pH 4.5, thermal denaturation starts with 20% glycerol or xylitol, or 40% sorbitol
84
-
20 min, pH 4.5, thermal denaturation starts with 30% and 40% xylitol or 40% glycerol
0 - 50
-
stable
20
-
rapid loss of activity above
20
30 min, recombinant enzyme is stable deglycosylated enzyme loses 40% of the initial activity
20
-
180 min, more than 90% of initial activity of enzyme expressed in Hansenula polymorpha and Pichia pastoris remains
20
temperatures above 20°C result in a rapid loss of enzyme activity
25 - 60
-
free enzyme: 50% activity after 20 min at 30°C and 10 min at 40°C
25 - 60
-
immobilized enzyme: 50% activity after 3600 min at 4°C, after 150 min at 25°C, after 100 min at 30°C, after 70 min at 40°C
30
-
at pH 5 or higher, stable for at least 30 min, invertase II
30
30 min, recombinant enzyme loses 20% of the initial activity, deglycosylated enzyme loses 60% of initial activity
30
-
40 min, enzyme is slightly inactivated
30
-
pH 3-7, 2 h, extracellular enzyme, stable
37
-
2 h, stable
37
after 6 h of incubation the percentage of activity is 71%
40
-
15 min, purified enzyme, over 90% remaining activity
40
-
half-life: 44 h, invertase 2
40
30 min, recombinant enzyme loses 50% of the initial activity, deglycosylated enzyme loses 90% of initial activity
40
-
40 min, 20% loss of activity
40
-
1 h, purified enzyme, pH 5.0, stable
40
-
above, enzyme entraped into calcium alginate beads is more stable than the soluble one
45
-
stable at 45°C for 1 h
45
-
pH 4.5-7.0, stable below
45
-
free enzyme, rapid loss of activity above
45
-
t1/2 of invertase INVA expressed in Pichia pastoris under the control of the strong AOX1 promoter is 480 min, invertase INVB expressed in Pichia pastoris under the control of the strong AOX1 promoter is 50 min
47
-
pH 4.5, 5 min, 50% loss of activity
47
after 6 h of incubation the percentage of activity is 52%
50
-
pH 5.0, 30 min, above 81% of initial activity
50
-
15 min, native enzyme retains 98% of activity, deglycosylated enzyme retains 7% of its original activity
50
recombinant His-tagged isozyme betafruct2, complete loss of activity
50
recombinant His-tagged isozyme betafruct3, complete loss of activity
50
-
pH 4.5, 15 min, stable
50
30 min, recombinant enzyme loses 80% of the initial activity, deglycosylated enzyme loses 95% of initial activity
50
-
20 min, 60% loss of invertase 1 activity, 8% loss of invertase 2 activity
50
-
5 min, 70% loss of activity
50
-
30 min, 50% loss of activity
50
-
10 min, both isozymes IT I and IT II retain over 70% activity
50
-
heterologous enzyme is stable below
50
-
free enzyme, stable up to
50
-
irreversibly denatured above
50
-
4 min, soluble enzyme retains 60% of its activity, cell-wall bound enzyme retains only 20% of its activity
55
-
half-life: 14.9 h, invertase 2
55
-
50% loss of beta-fructofuranosidase activity after 30 min, 50% loss of invertase activity after 75 min
55
-
10 min, complete loss of activity of isoenzyme P-1, 20% loss of activity of isoenzyme P-2
55
-
5 min, complete inactivation
55
-
quite stable in reversed micelles for long duration
55
-
5 min, complete inactivation
56
-
pH 5.4, 20 min, stable up to
56
-
15 min stable at pH 4.9, very unstable above pH 6, extracellular enzyme. Intracellular enzyme is unstable above pH 6, stable at pH 4.9 for 10 min
60
-
purified enzyme, pH 5.5, over 90% remaining activity after 5 h, rapid inactivation above
60
-
half-life is 60 min at 60°C
60
-
half-life: 2 h, invertase 2
60
-
without substrate, stable for a maximum of 20 h
60
-
10 min, not very stable even in presence of sulfhydryl compounds
60
30 min, recombinant enzyme loses 85% of the initial activity, deglycosylated enzyme completely loses activity
60
-
10 min, invertase II retains 25% of its activity. Invertase III retains 40% of its activity, invertase I completely loses activity
60
-
5 min, 91% loss of activity
60
-
stable for 1 h, both extracellular and cell extract enzyme
60
-
substitution of D2O for H2O results in a half-life which is four times greater
60
-
10 min, enzyme expressed in Hansenula polymorpha shows optimal stability towards thermal inactivation at pH 5.5. Enzyme expressed in Pichia pastoris shows optimal stability towards thermal inactivation at pH 6
60
-
free enzyme, stable up to
60
-
10 min, 80% residual activity for isoform EINV1, 60% for isoform EINV2, 25% for isoform EINV3, 45% for isoform EINV4
60
-
14 days, 59% loss of activity
65
-
10 min, stable below
65
-
immobilized enzyme, stable up to
65
-
5 min, complete inactivation of the CM-cellulose adsorbed enzyme
70
-
10 min, about 10% loss of activity
70
-
20 min, pH 9.0, thermal denaturation starts without solvent or with 20% sorbitol
70
-
half-life 10 min, both extracellular and cell extract enzyme
70
-
5 min, enzyme embedded within a polyacrylamide gel loses 85% loss of activity
70
-
14 days, 76% loss of activity
75
-
20 min, pH 4.5, thermal denaturation starts without solvent
75
-
20 min, pH 9.0, thermal denaturation starts with 30% xylitol
77
-
20 min, pH 4.5, thermal denaturation starts with 10% sorbitol
77
-
20 min, pH 9.0, thermal denaturation starts with 40% xylitol
80
-
90 min, about 25% loss of activity of S-form, F-form is stable
80
-
20 min, pH 4.5, 70% residual activity retained with 40% glycerol
80
-
20 min, pH 4.5, 80% residual activity with 40% xylitol
80
-
20 min, pH 4.5, maximum of 45% residual activity above 20% to 40% sorbitol
80
-
inactivation of free enzyme
80
-
5 h, retains at least 85% of its initial activity
85
-
20 min, pH 4.5, thermal denaturation starts with 30% glycerol
85
-
5 h, 15% loss of activity
90
-
90 min, about 45% loss of activity of S-form, F-form is stable
90
-
inactivation of immobilized enzyme
90
-
5 h, substantial loss of activity
additional information
-
the deglycosylated enzyme is more sensitive than the glycosylated enzyme at 40-50°C
additional information
-
the thermal stability of the enzyme that is covalently bound via glutaraldehyde to a macroporous polystyrene anion-exchanger, silica and porous glass is higher than that of the soluble enzyme. Immobilization of invertase to the polystyrene anion-exchanger by benzoquinone and trichlorotriazine provides enzyme derivatives with lower thermal stability
additional information
-
enzyme in cells immobilized in gelatin hydrogels are analyzed concerning kinetics, thermostability, and reusability, overview
additional information
-
stabilization of enzyme against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents of various lengths. Crosslinking with 1,4-diisocyanatobutane is most effective in enhancing thermostability. Stability is improved dramatically by crosslinking 0.5 mg/ml of protein with 30 micromol/ml of the reagent. Molecular engineering by crosslinking reduces the first-order thermal denaturation constant at 60°C from 1.567 per min for the native enzyme to 0.437 per min for the stabilized enzyme. The best crosslinking treatment increases the activation energy for denaturation from 391 kJ per mol for the native protein to 466 kJ per mol for the stabilized enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alkaline invertase, enzyme I and II, partial
-
ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration
-
ammonium sulfate fractionation, DEAE-Sephadex A-25 column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate fractionation, DEAE-Sephadex-A50 chromatography, and HPLC gel filtration on Protein Pak 300 SW
-
ammonium sulfate precipitation and Sephacryl S-200 gel filtration
ammonium sulfate precipitation, dialysis, Hiload anion exchange chromatography, elution at about 640 mM NaCl, hydrophobic interaction chromatography with phenyl superose column, and gel filtration chromatography on a Pharmacia FPLC unit
-
both soluble acid and alkaline invertase
-
centrifugation after homogenization
-
centrifugation of cell culture medium, supernatants diluted in 50 mM MES-buffer, pH 5.6
centrifugation of must and filtration through 0.45 micrometre membrane, dialysation against distilled water, ultrafiltration with hydrophilic polysulfone membrane with 10 kDa cutoff, concentrate freeze-dried, solubilized in 50 mM Tris-HCl buffer, pH 7.5, purified on Q-Sepharose Fast Flow anion exchange column, gradient of 0-500 mM NaCl in buffer, fractions of around 60 kDa pooled and desalted
-
concentration through a 30000MWCO PES, dialyzation in 20 mM sodium phosphate, pH 7, purification with DEAE-Sephacel chormatography column, elution with 0-0.2 M NaCl gradient, invertase active fractions pooled, dialyzed in sodium acetate buffer, pH 5, applied to a DEAE-Sephacel chromatography volumn and eluted
DEAE-cellulose chromatography and Sephacryl S-200 gel filtration
-
DEAE-cellulose column chromatography and Sephacryl S-200 gel filtration
-
DEAE-cellulose DE52 column chromatography, Toyopearl butyl-650M column chromatography, and Sepharose CL-4B column chromatography
-
DEAE-Sephacel chromatography
-
disrupted cells centrifuged, supernatant and pellet, combined purification and immobilization of chimeric gene product on Avicel (cellulose), or purification of 6-His-tagged enzyme by nickel affinity chromatography with Ni-NTA resin, elution with imidazol gradient (10-250 mM), dialyzed against 50 mM Tris-HCl, pH 7.0, and following immobilization on Nylon-6 microbeads
-
external invertase isoforms EINV1, EINV2, EINV3 and EINV4
-
extracellular and intracellular enzyme
-
green and red tomato fruits homogenized separately in 10 mM NaOAc cold buffer, pH 4.6 containing 1 M NaCl, centrifuged, supernatant precipitated, resuspended in buffer, dialyzed, loaded onto invertase inhibitor of Solanum lycopersicum affinity column, washing with buffer, eluted with 50 mM potassium phosphate buffer, pH 7.5, fractions with invertase activity pooled, loaded onto Hiload 16/60 Superdex 75 column, eluted with 20 mM Na acetate, pH 4.6, containing 150 mM NaCl
high molecular weight form, S-form, and low molecular weight form, F-form
-
His tag affinity chromatography
immobilized metal ion affinity chromatography
intracellular and extracellular invertase
-
invertase I, IIa and Iib
-
isoenzyme AIV I and AIV II
-
isozymes partially from grape berries by ammonium sulfate fractionation and subcellular fractionation
-
leaf material frozen, ground, soluble proteins extracted, precipitated, dialyzed, purified by Con A chromatography, pH 6.8, to separate inhibitors from glycosylated invertase, invertase proteins bound to the Con A column are eluted with buffer containing 15% methyl-alpha-D-glucopyranoside
-
lysed cells centrifuged, supernatant purified by nickel-affinity chromatography
-
mitochondrial fraction isolated by several centrifugation steps from filtrate (cheesecloth) of ground and homogenized tubers, final centrifugation step with mannitol gradient (lower fraction excluding the bottom) followed by several washing steps of the pellet, resuspension in 10 mM morpholinepropanesulfonic acid + 70 mM mannitol buffer, pH 7.4, further centrifugation steps to separate mitoplast pellet from intermembrane space and outer membrane and separate the mitoplast pellet after repeated freeze-thawing rupture into matrix supernatant and inner membrane pellet, washed and resuspended in 10 mM morpholinepropanesulfonic acid buffer, pH 7.4
-
multiple isoforms: INV1, INV2, INV3
-
native enzyme 37fold by ammonium sulfate fractionation, dialysis, and two steps of ion exchange chromatography
-
native enzyme 53.4fold by ammonium sulfate fractionation, and two steps of gel filtration to homogeneity
-
native enzyme from strain IMI 303386 49.8fold to homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native isozymes soluble acid invertase SAI and cell wall-bound invertase CWI from fruits to homogeneity
-
native soluble alkaline isozyme IT I 144fold from cell suspension culture to homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration, and native soluble acid invertase isozyme IT II 130fold from cell suspension culture to homogeneity by ammonium sulfate fractionation, anion exchange and cation exchange chromatography, ConA affinity chromatography, and anion exchange chromatography
-
Ni-NTA affinity resin column chromatography
Ni-NTA column chromatography
nickel affinity column chromatography
Q-Sepharose column chromatography and Sephadex 200 gel filtration
recombinant enzyme containing a 6*His-tagged tail
-
recombinant His-tagged isozyme betafruct2 15.1fold from Pichia pastoris strain YIT2 by ammonium sulfate fractionation and cobalt affinity chromatography
recombinant His-tagged isozyme betafruct3 24.3fold from Pichia pastoris strain YIT3 by ammonium sulfate fractionation and cobalt affinity chromatography
recombinant His-tagged soluble, vacuolar isozyme lbbetafruct3 5fold from Pichia pastoris by nickel affinity chromatography
recombinant His-tagged soluble, vacuolar isozyme lbbetalbbetafruct2 7.6fold from Pichia pastoris by nickel affinity chromatography
recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged wild-type enzyme and mutants E190A and E190D from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant soluble, His-tagged CscA 238fold from Escherichia coli strain BL21(DE3) by metal affinity chromatography
recombinant truncated cytosolic protein
-
supernatant of medium of methanol-induced cell culture precipitated by 80% saturation of ammonium sulfate, centrifuged, resuspended in sodium phosphate buffer, pH 7, dialyzed, and mixed with cobalt-based IMAC resin for 1 h at 4°C, packed into a column, eluted with imidazole
-
truncated version of InvA (residues Lys9-Thr460)
-
-
partial
-
recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.