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(22S,25S)-5alpha-solanidanin-3beta-ol + UDP-glucose
?
-
demissidine 1.4% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(22S,25S)-epoxy-furost-5-en-3beta,26-diol + UDP-glucose
?
-
nuatigenin, 16.1% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(25R)-5alpha-spirostan-3beta-ol + UDP-glucose
?
-
tigogenin, 2.1% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(25R)-5alpha-spirostan-3beta-ol-12-one + UDP-glucose
?
-
hecogenin, 6.3% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(25R)-spirost-5-en-3beta,25beta-diol + UDP-glucose
?
-
isonuatigenin, 13.4% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(25R)-spirost-5-en-3beta-ol + UDP-glucose
?
-
diosgenin, 3.5% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
(25S)-5alpha,22betaN-spirosolanin-3beta-ol + UDP-glucose
?
-
tomatidine, 2.8% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
24-methylene cholesterol + UDP-glucose
UDP + 24-methylene-cholesterol 3-beta-D-glucoside
-
-
-
-
?
3beta-hydroxy-16,17alpha-epoxypregnenolone + UDP-alpha-D-glucose
3beta-hydroxy-16,17alpha-epoxypregnenolone 3-beta-D-glucoside + UDP
-
-
-
-
?
3beta-hydroxy-pregna-5,16-dien-20-one + UDP-glucose
UDP + 3beta-20-oxopregna-5,16-dien-3-yl beta-D-glucopyranoside
5alpha-cholest-7-en-3beta-ol + UDP-glucose
?
-
14.1% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
5alpha-cholestan-3beta-ol + UDP-glucose
?
-
cholestanol, 12.0% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
5alpha-cholestan-3beta-ol + UDP-glucose
UDP + 3beta,5alpha-cholestan 3-beta-D-glucoside
-
-
-
-
?
androst-5-en-3beta-ol-17-one + UDP-glucose
?
-
androstenolon, 16.0% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
beta-sitosterol + UDP-glucose
UDP + beta-sitosterol 3-beta-D-glucoside
brassicasterol + UDP-glucose
UDP + brassicasterol 3-beta-D-glucoside
-
-
-
-
?
cholest-5-en-22-on-3beta-ol + UDP-glucose
?
-
22-oxycholesterol, 133.1% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholest-5-en-3beta,19-diol + UDP-glucose
?
-
9.2% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholest-5-en-3beta,20alpha-diol + UDP-glucose
?
-
90.8% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholest-5-en-3beta,25-diol + UDP-glucose
?
-
25-hydroxycholesterol, 89.4% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholest-5-en-3beta-ol + UDP-glucose
?
-
cholesterol, 98.5% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholest-5-en-3beta-ol-7-one + UDP-glucose
?
-
5.6% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
cholesterol + UDP-glucose
UDP + cholesterol 3-beta-D-glucoside
dehydroepiandrosterone + UDP-glucose
UDP + dehydroepiandrosterone 3-beta-D-glucoside
diosgenin + UDP-glucose
UDP + diosgenin 3-beta-D-glucoside
-
-
-
-
?
ergosterol + UDP-glucose
UDP + ergosterol 3-beta-D-glucoside
-
-
-
-
?
pregn-5-en-3beta-ol-20-one + UDP-glucose
?
-
pregnenolon, 33.1% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
pregnenolene + UDP-glucose
UDP + pregnenolone 3-beta-D-glucoside
-
-
-
-
?
pregnenolone + UDP-glucose
UDP + pregnenolone 3-beta-D-glucoside
-
-
-
-
?
solasodine + UDP-glucose
UDP + solasodine 3-beta-D-glucoside
-
-
-
-
?
stigmasta-5,22-dien-3beta-ol + UDP-glucose
?
-
stigmasterol, 49.2% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
stigmasta-5,24(28)-dien-3beta-ol + UDP-glucose
?
-
82.4% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
stigmastan-3beta-ol + UDP-glucose
?
-
38.7% of the activity with sitosterol (stigmast-5-en-3beta-ol)
-
-
?
stigmasterol + UDP-glucose
UDP + stigmasterol 3-beta-D-glucoside
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
UDP-glucose + 3beta-hydroxy-16,17alpha-epoxypregnenolone
?
-
-
-
?
UDP-glucose + 3beta-hydroxy-16,17alpha-epoxypregnenolone
UDP + 3beta-hydroxy-16,17alpha-epoxypregnenolone 3-beta-D-glucoside
-
-
-
-
?
UDP-glucose + 3beta-hydroxy-pregna-5,16-dien-one
UDP + 3beta-20-oxopregna-5,16-dien-3-yl beta-D-glucopyranoside
-
-
-
?
UDP-glucose + 4-demethyl-obtusifoliol
UDP + 4-demethyl-obtusifoliol 3-beta-glucoside
-
58% of the activity with sitosterol
-
?
UDP-glucose + 5-alpha-cholestanol
UDP + 5-alpha-cholestanol 3-beta-D-glucoside
-
8% of the activity with sitosterol
-
?
UDP-glucose + 5-cholestenol
UDP + 5-cholestenol 3-beta-D-glucoside
-
12% of the activity with sitosterol
-
?
UDP-glucose + 7-dehydrocholesterol
UDP + 7-dehydrocholesterol 3-beta-D-glucoside
-
6% of the activity with sitosterol
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
UDP-glucose + alpha-spinasterol
UDP + alpha-spinasterol 3-beta-D-glucoside
-
31% of the activity with sitosterol
-
?
UDP-glucose + beta-sitosterol
UDP + beta-sitosterol 3-beta-D-glucoside
UDP-glucose + brassicasterol
UDP + brassicasterol 3-beta-D-glucoside
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
UDP-glucose + dehydroepiandrosterone
UDP + dehydroepiandrosterone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + epiandrosterone
UDP + epiandrosterone 3-beta-glucoside
-
best substrate
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
UDP-glucose + isofucosterol
UDP + isofucosterol 3-beta-glucoside
-
73% of the activity with sitosterol
-
?
UDP-glucose + poriferasterol
UDP + poriferasterol 3-beta-glucoside
-
synthesis of poriferasterol monoglucoside may be involved in differentiation
-
-
?
UDP-glucose + pregnenolone
UDP + pregnenolone 3-beta-D-glucoside
UDP-glucose + pregnenolone
UDP + pregnenolone 3-beta-glucoside
-
57% of the activity with epiandrosterone
-
?
UDP-glucose + protopanaxadiol
UDP + protopanaxadiol 3-beta-D-glucoside
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
UDP-glucose + solasodine
UDP + solasodine 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
UDP-glucose + transandrosterone
UDP + transandrosterone 3beta-D-glucoside
UDP-glucose + withaferin A
UDP + ?
-
-
-
?
UDP-glucose + withanolide A
UDP + ?
-
-
-
?
additional information
?
-
3beta-hydroxy-pregna-5,16-dien-20-one + UDP-glucose
UDP + 3beta-20-oxopregna-5,16-dien-3-yl beta-D-glucopyranoside
-
-
-
-
?
3beta-hydroxy-pregna-5,16-dien-20-one + UDP-glucose
UDP + 3beta-20-oxopregna-5,16-dien-3-yl beta-D-glucopyranoside
-
-
-
-
?
beta-sitosterol + UDP-glucose
UDP + beta-sitosterol 3-beta-D-glucoside
-
-
-
-
?
beta-sitosterol + UDP-glucose
UDP + beta-sitosterol 3-beta-D-glucoside
-
-
-
-
?
cholesterol + UDP-glucose
UDP + cholesterol 3-beta-D-glucoside
-
-
-
-
?
cholesterol + UDP-glucose
UDP + cholesterol 3-beta-D-glucoside
-
-
-
-
?
dehydroepiandrosterone + UDP-glucose
UDP + dehydroepiandrosterone 3-beta-D-glucoside
-
-
-
-
?
dehydroepiandrosterone + UDP-glucose
UDP + dehydroepiandrosterone 3-beta-D-glucoside
-
-
-
-
?
stigmasterol + UDP-glucose
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
-
?
stigmasterol + UDP-glucose
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-alpha-D-glucose + testosterone
UDP + testosterone 17-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + a sterol
UDP + a sterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + beta-sitosterol
UDP + beta-sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + beta-sitosterol
UDP + beta-sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + beta-sitosterol
UDP + beta-sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + brassicasterol
UDP + brassicasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + brassicasterol
UDP + brassicasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
-
4% of the products
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
80% of the activity with poriferasterol
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
28% of the activity with sitosterol
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
best substrate
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + campesterol
UDP + campesterol 3-beta-D-glucoside
-
68% of the activity with sitosterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme exhibits equal activity to the purified protein
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
with sitosterol, best substrates
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme exhibits equal activity to the purified protein
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme exhibits equal activity to the purified protein
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
best substrate
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
23% of the activity with sitosterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
12% of the activity with poriferasterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
cloned enzyme glucosylates cholesterol
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + cholesterol
UDP + cholesterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
69% of the activity with sitosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
11% of the activity with sitosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
9% of the activity with poriferasterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
cloned enzyme glucosylates ergosterol
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + ergosterol
UDP + ergosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estradiol
UDP + estradiol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + estrone
UDP + estrone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + pregnenolone
UDP + pregnenolone 3-beta-D-glucoside
-
-
-
-
?
UDP-glucose + pregnenolone
UDP + pregnenolone 3-beta-D-glucoside
-
-
-
?
UDP-glucose + protopanaxadiol
UDP + protopanaxadiol 3-beta-D-glucoside
an unnatural substrate of enzyme mutant 7_1
-
-
?
UDP-glucose + protopanaxadiol
UDP + protopanaxadiol 3-beta-D-glucoside
an unnatural substrate of enzyme mutant 7_1
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
with cholesterol, best substrates
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
88% of the activity with epiandrosterone
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
75% of the product
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
best substrate
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
maximal activity, the same as poriferasterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
greater activity than with other sterols
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
cloned enzyme glucosylates sitosterol
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
-
-
-
?
UDP-glucose + sitosterol
UDP + sitosterol 3-beta-D-glucoside
-
best substrate
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
63% of the activity with sitosterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
122% of the activity with epiandrosterone, highest specificity
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
6% of the product
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
14% of the activity with poriferasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
50% of the activity with sitosterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
cloned enzyme glucosylates stigmasterol
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + stigmasterol
UDP + stigmasterol 3-beta-D-glucoside
-
-
-
?
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
cloned enzyme glucosylates tomatidine
-
?
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
cloned enzyme glucosylates tomatidine
-
?
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
cloned enzyme glucosylates tomatidine
-
?
UDP-glucose + tomatidine
UDP + tomatidine 3-beta-glucoside
cloned enzyme glucosylates tomatidine
-
?
UDP-glucose + transandrosterone
UDP + transandrosterone 3beta-D-glucoside
-
-
-
-
?
UDP-glucose + transandrosterone
UDP + transandrosterone 3beta-D-glucoside
-
-
-
?
additional information
?
-
-
the enzyme only shows activity with sterols having hydroxyl group at C-3 position. Utilises only UDP-glucose, UDP-galactose cannot serve as the sugar donor.
-
-
?
additional information
?
-
-
yamogenin is not substrate of this enzyme
-
-
?
additional information
?
-
-
UDP-glucose is an effective glucose donor but not so UDP-mannose, UDP-galactose or UMP-glucose
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
-
the enzyme is a fungal virulence factor
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
-
almost no activity with androsterone, digitoxigenin, digitoxin and testosterone
-
-
?
additional information
?
-
-
UDP-glucose is an effective glucose donor but not so ADP-glucose, CDP-glucose, TDP-glucose, GDP-glucose, UDP-galactose or UDP-mannose
-
-
?
additional information
?
-
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
sterol glucosyltransferase Ugt51/Paz4 is essential for pexophagy (peroxisome degradation), but not for macroautophagy in the methylotrophic yeast. Deletion of the catalytic domain does not impair protein localization, but abolishes pexophagy, suggesting that SG synthesis is required for this process
-
-
?
additional information
?
-
-
sterol glucosyltransferase Ugt51/Paz4 is essential for pexophagy (peroxisome degradation), but not for macroautophagy in the methylotrophic yeast. Deletion of the catalytic domain does not impair protein localization, but abolishes pexophagy, suggesting that SG synthesis is required for this process
-
-
?
additional information
?
-
-
the UGT51 gene is required for pexophagy and other vacuole related processes
-
-
?
additional information
?
-
sterol glucosyltransferase Ugt51/Paz4 is essential for pexophagy (peroxisome degradation), but not for macroautophagy in the methylotrophic yeast. Deletion of the catalytic domain does not impair protein localization, but abolishes pexophagy, suggesting that SG synthesis is required for this process
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
-
DELTA5-sterols are glucosylated at higher rate than DELTA7-sterols
-
-
?
additional information
?
-
-
glucose 1-phosphate, GDP-glucose and ADP-glucose are inactive substrates
-
-
?
additional information
?
-
-
presence and localization of double bonds in the ring system exert a pronounced effect on the rate of glucosylation
-
-
?
additional information
?
-
-
the presence of a DELTA22 double bond decreases affinity of the sterol for the enzyme
-
-
?
additional information
?
-
-
enzyme can use CDP-glucose and TDP-glucose at 6 times slower rate
-
-
?
additional information
?
-
-
coprostanol and epicholestanol are not glucosylated
-
-
?
additional information
?
-
-
sterols possessing an alkyl group at C-24 are better substrates than C27 sterols
-
-
?
additional information
?
-
-
stanols and sterols with conjugated double bonds in ring B are poor substrates
-
-
?
additional information
?
-
-
all 3-B-OH sterols containing a double bond in position 5 are glucosylated and a double bond at C24 reduces glucosylation
-
-
?
additional information
?
-
-
UDP-glucose is an effective glucose donor, not so ADP-glucose, CDP-glucose or GDP-glucose
-
-
?
additional information
?
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
-
UDP-glucose best glucose donor, CDP-glucose, GDP-glucose and UDP-xylopyranose are used but at significantly lower rates and UDP-mannose, UDP-glucaronic acid, GDP-mannose and TDP-glucose are not effective glucose donor
-
-
?
additional information
?
-
experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
-
-
?
additional information
?
-
-
experimental results suggest that the enzyme is not involved in the cytoplasm to vacuole targeting pathway, macroautophagy and pexophagy
-
-
?
additional information
?
-
substrate molecular docking and structure analysis of wild-type and mutant enzymes, sugar donor binding mechanism of UGT51, overview
-
-
-
additional information
?
-
-
substrate molecular docking and structure analysis of wild-type and mutant enzymes, sugar donor binding mechanism of UGT51, overview
-
-
-
additional information
?
-
substrate molecular docking and structure analysis of wild-type and mutant enzymes, sugar donor binding mechanism of UGT51, overview
-
-
-
additional information
?
-
-
enzyme is absolute specific to UDP-glucose
-
-
?
additional information
?
-
-
glucose 1-phosphate, GDP-glucose and ADP-glucose are inactive substrates
-
-
?
additional information
?
-
-
all 3-B-OH sterols containing a double bond in position 5 are glucosylated and a double bond at C24 reduces glucosylation
-
-
?
additional information
?
-
SGT activity assays are carried out with a plant sterol mixture consisting of approximately 13% brassicasterol, 26% campesterol, 7% stigmasterol, and 53% beta-sitosterol in ethanol, and UDP-glucose
-
-
-
additional information
?
-
SGT activity assays are carried out with a plant sterol mixture consisting of approximately 13% brassicasterol, 26% campesterol, 7% stigmasterol, and 53% beta-sitosterol in ethanol, and UDP-glucose
-
-
-
additional information
?
-
SGT activity assays are carried out with a plant sterol mixture consisting of approximately 13% brassicasterol, 26% campesterol, 7% stigmasterol, and 53% beta-sitosterol in ethanol, and UDP-glucose
-
-
-
additional information
?
-
SGT activity assays are carried out with a plant sterol mixture consisting of approximately 13% brassicasterol, 26% campesterol, 7% stigmasterol, and 53% beta-sitosterol in ethanol, and UDP-glucose
-
-
-
additional information
?
-
-
SGT activity assays are carried out with a plant sterol mixture consisting of approximately 13% brassicasterol, 26% campesterol, 7% stigmasterol, and 53% beta-sitosterol in ethanol, and UDP-glucose
-
-
-
additional information
?
-
-
may participate in the regulating of free sterol concentration in the cell
-
-
?
additional information
?
-
-
UDP-galactose, TDP-glucose and CDP-glucose are also suitable as a sugar source for sterol glucosylation but with distinctly lower rates
-
-
?
additional information
?
-
-
no activity with solasodine (25R-22alphaN-spirosol-5-enin-3beta-ol), solanidine (22S,25S-solanid-5-enin-3beta-ol), sarsasapogenin (25S-5beta-spirostan-3beta-ol), yamogenin (25S-spirost-5-en-3beta-ol), thiocholesterol (cholest-5-en-3beta-tiol), 5beta-cholestan-3beta-ol (coprostanol), 5alpha-cholestan-3alpha-ol (epicholestanol), 5beta-cholestan-3alpha-ol (epicoprostanol), lanosterol (4,4,14-trimethyl-5alpha-cholest-8-en-3beta-ol), and beta-amyrin (olean-12-en-3beta-ol) do not serve as glucose acceptors
-
-
?
additional information
?
-
-
the enzyme is highly specific to sterols and shows no activity with non steroidal substrates. Amongst the sterols, the enzyme is position specific and works only with C-3 hydroxyl sterols, but the extradiol C-3 hydroxyl group is not glucosylated. Sterols with A-B ring 5-en (e.g. deacetyl-16-DPA) are glucosylated more efficiently than those with 5alpha-H. For the cytosolic enzyme, the relative substrate specificity of the membrane-bound enzyme is different. The membrane enzyme is more specific towards phytosterols and brassicasterol. It shows no activity towards secondary metabolits and flavonoids and isoflavonoids.
-
-
?
additional information
?
-
the enzyme only shows activity with sterols having hydroxyl group at C-3 position. SGTL1 is more active toward sterols without side chain. Utilises only UDP-glucose, UDP-galactose can not serve as the sugar donor.
-
-
?
additional information
?
-
-
the enzyme only shows activity with sterols having hydroxyl group at C-3 position. SGTL1 is more active toward sterols without side chain. Utilises only UDP-glucose, UDP-galactose can not serve as the sugar donor.
-
-
?
additional information
?
-
-
the enzyme is specific for the 3beta-hydroxy position and has a catalytic specificity to glycosylate withanolide and sterols
-
-
?
additional information
?
-
-
the enzyme is specific for the 3beta-hydroxy position and has a catalytic specificity to glycosylate withanolide and sterols
-
-
?
additional information
?
-
-
the UGT51 gene is required for utilization of decane, but not for pexophagy
-
-
?
additional information
?
-
-
p-nitrophenol, estrone and 4-alpha,10-beta-dimethyl-trans-decal-3-beta-ol are not substrates
-
-
?
stigmast-5-en-3beta-ol + UDP-glucose
additional information
-
-
sitosterol, 100% of the activity
3-O-beta-D-monoglucopyranoside of sitosterol and 3-O-beta-D-monogalactopyranoside of sitosterol identified as products
-
?
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evolution
the enzyme is a member of SGT gene family
evolution
phylogenetic tree of UGT80- and UGT713-related proteins, overview
evolution
UGT80 proteins belong to a third family that is hypothesized to be involved in sterol glucoside synthesis, phylogenetic tree of UGT80- and UGT713-related proteins, overview
evolution
enzyme UGT51 is a member of the GT1 family, GT-B fold group, comprising two Rossman-like domains
evolution
the enzyme belongs to the UDP-glucose sterol glycosyltransferases family of developmental and stress regulated genes that encode cytosolic and membrane-associated forms of the enzyme. Identification and functional characterization of the four members, SlSGT1-4, of the tomato cv. Micro-Tom
evolution
the genome of Arabidopsis thaliana contains two genes coding for UDP-Glc:sterol-glucosyltransferases, UGT80A2 and UGT80B1, and studies of mutant lines indicate that they are only partially redundant
evolution
-
phylogenetic tree of UGT80- and UGT713-related proteins, overview
-
evolution
-
UGT80 proteins belong to a third family that is hypothesized to be involved in sterol glucoside synthesis, phylogenetic tree of UGT80- and UGT713-related proteins, overview
-
evolution
-
the genome of Arabidopsis thaliana contains two genes coding for UDP-Glc:sterol-glucosyltransferases, UGT80A2 and UGT80B1, and studies of mutant lines indicate that they are only partially redundant
-
evolution
-
enzyme UGT51 is a member of the GT1 family, GT-B fold group, comprising two Rossman-like domains
-
malfunction
-
the atg26 mutant is defective in Appressorium-mediated host invasion
malfunction
ugt80B1 mutants displaya a significant reduction only in campesteryl, brassicasteryl, and cholesteryl glucosides, but not sitosteryl or stigmasteryl glucosides
malfunction
analysis of the function of SGTs by silencing SGTL1, SGTL2 and SGTL4 in Withania somnifera. Downregulation of SGTs by artificial miRNAs leads to the enhanced accumulation of withanolide A, withaferin A, sitosterol, stigmasterol and decreased content of withanoside V in virus induced gene silencing (VIGS) lines. This is further correlated with increased expression of WsHMGR, WsDXR, WsFPPS, WsCYP710A1, WsSTE1 and WsDWF5 genes, involved in withanolide biosynthesis. These variations of withanolide concentrations in silenced lines result in pathogen susceptibility as compared to control plants. The infection of Alternaria alternata causes increased salicylic acid, callose deposition, superoxide dismutase and H2O2 in aMIR-VIGS lines. The expression of biotic stress related genes, namely, WsPR1, WsDFS, WsSPI and WsPR10 is also enhanced in aMIR-VIGS lines in time dependent manner. Salicylic acid level increases the expression of defence related genes in silenced lines. A positive feedback regulation of withanolide biosynthesis occurs by silencing of SGTLs which results in reduced biotic tolerance
malfunction
inactivation of UDP-glucose sterol glucosyltransferases enhances Arabidopsis thaliana resistance to Botrytis cinerea infection, which correlates with increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. Analysis of the response to necrotrophic fungus Botrytis cinerea in an Arabidopsis thaliana mutant that is severely impaired in steryl glycosides biosynthesis due to the inactivation of the two sterol glucosyltransferases, UGT80A2 and UGT80B1. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level. After fungus infection, the expression of genes involved in the indole glucosinolate biosynthesis is also upregulated at a higher degree in the ugt80A2;B1 mutant than in wild-type plants
malfunction
the plasma membrane cell fate regulator, SCRAMBLED (SCM), is mislocalized in ugt80B1 mutants, underscoring the aberrant root epidermal cell patterning. GFP-tagged SCM is localized to the cytoplasm in a non cell type dependent manner instead of the hair (H) cell plasma membrane in these mutants. Abnormal root hair cell patterning in ugt80B1 mutants is likely the direct result of expression of GL2 in H cell files in this mutant. The aberrant expression of GL2 is caused by the mislocalization of SCM away from the cell periphery, reducing the capacity of the receptor to mediate positional information to the cell. Reductions in specific sterol glucosides might be responsible for the disruption of cell fate regulators in these ugt80B1 mutants. The mislocalization of SCM to the cytoplasm can point to a role for sterol glucosides in vesicular trafficking or plasma membrane protein targeting. Deficiencies in specific sterol glucosides are sufficient to disrupt normal cell function and point to a possible role for sterol glucosides in cargo transport and/or protein targeting to the plasma membrane. Aberrant subcellular localization of SCM:GFP in ugt80B1 epidermal cells from the elongation zone of the root
malfunction
-
inactivation of UDP-glucose sterol glucosyltransferases enhances Arabidopsis thaliana resistance to Botrytis cinerea infection, which correlates with increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. Analysis of the response to necrotrophic fungus Botrytis cinerea in an Arabidopsis thaliana mutant that is severely impaired in steryl glycosides biosynthesis due to the inactivation of the two sterol glucosyltransferases, UGT80A2 and UGT80B1. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level. After fungus infection, the expression of genes involved in the indole glucosinolate biosynthesis is also upregulated at a higher degree in the ugt80A2;B1 mutant than in wild-type plants
-
malfunction
-
the plasma membrane cell fate regulator, SCRAMBLED (SCM), is mislocalized in ugt80B1 mutants, underscoring the aberrant root epidermal cell patterning. GFP-tagged SCM is localized to the cytoplasm in a non cell type dependent manner instead of the hair (H) cell plasma membrane in these mutants. Abnormal root hair cell patterning in ugt80B1 mutants is likely the direct result of expression of GL2 in H cell files in this mutant. The aberrant expression of GL2 is caused by the mislocalization of SCM away from the cell periphery, reducing the capacity of the receptor to mediate positional information to the cell. Reductions in specific sterol glucosides might be responsible for the disruption of cell fate regulators in these ugt80B1 mutants. The mislocalization of SCM to the cytoplasm can point to a role for sterol glucosides in vesicular trafficking or plasma membrane protein targeting. Deficiencies in specific sterol glucosides are sufficient to disrupt normal cell function and point to a possible role for sterol glucosides in cargo transport and/or protein targeting to the plasma membrane. Aberrant subcellular localization of SCM:GFP in ugt80B1 epidermal cells from the elongation zone of the root
-
malfunction
-
ugt80B1 mutants displaya a significant reduction only in campesteryl, brassicasteryl, and cholesteryl glucosides, but not sitosteryl or stigmasteryl glucosides
-
metabolism
crosstalk between hormone signaling pathways, particularly those mediated by salicylate and jasmonate, has been found to contribute to plant resistance to different types of pathogens. The results suggest that the salicylate-mediated defense pathway is not involved in the response of the ugt80A2;B1 mutant to Bortrytis cinerea infection. But camalexin and, probably, also indole glucosinolates are actively involved in the enhanced resistance of the ugt80A2;B1 mutant to Bortrytis cinerea infection. The synthesis of alkylglucosinolates in the ugt80A2;B1 mutant is not affected by Bortrytis cinerea infection
metabolism
UGT51 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
metabolism
-
crosstalk between hormone signaling pathways, particularly those mediated by salicylate and jasmonate, has been found to contribute to plant resistance to different types of pathogens. The results suggest that the salicylate-mediated defense pathway is not involved in the response of the ugt80A2;B1 mutant to Bortrytis cinerea infection. But camalexin and, probably, also indole glucosinolates are actively involved in the enhanced resistance of the ugt80A2;B1 mutant to Bortrytis cinerea infection. The synthesis of alkylglucosinolates in the ugt80A2;B1 mutant is not affected by Bortrytis cinerea infection
-
metabolism
-
UGT51 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
-
physiological function
-
required for full virulence of Colletotrichum orbiculare
physiological function
-
the enzyme is a cholesteryl glucoside synthetase, whose activity in lipid rafts might act as a potential factor in the thermal sensing reaction. It is involved in induction of heat shock protein factors Hsp70 and HSF-1 under heat stress
physiological function
the membrane-bound enzyme, UDP-glucose:sterol glucosyltransferase, controls the steryl glycoside synthesis
physiological function
-
ectopic enzyme overexpression in Withania somnifera promotes growth, enhances glycowithanolide and provides tolerance to abiotic and biotic stresses. Glycosylation not only stabilizes the products but also alters their physiological activities and governs intracellular distribution
physiological function
no role in steryl glucoside synthesis for UGT713B1/At5g24750
physiological function
steryl glucoside may be specific only for cellulose biosynthesis in cotton fibers because mature fibers contain more than 95% of cellulose
physiological function
steryl glucoside may be specific only for cellulose biosynthesis in cotton fibers because mature fibers contain more than 95% of cellulose. Isozyme GhSGT2 mainly participates in catalyzing glucosylation of membrane sterols
physiological function
UGT80A2 accounts for most of the sitosteryl and stigmasteryl glucoside production in seeds
physiological function
UGT80B1 plays a specialized role in steryl glucoside synthesis
physiological function
sterol glycosyltransferases (SGTs) catalyse transfer of glycon moiety to sterols and their related compounds to produce diverse glyco-conjugates or steryl glycosides with different biological and pharmacological activities. SGTs from Withania somnifera play a role in abiotic stresses
physiological function
sterol glycosyltransferases (SGTs) catalyze the formation of a variety of glycosylated sterol derivatives and are involved in producing a plethora of bioactive natural products. Sterol glycosyltransferases as members of UGTs are involved in transferring a sugar from UDP-sugar to various SGs metabolites, including hormones and secondary metabolites
physiological function
sterol glycosyltransferases (SGTs) catalyze the glycosylation of the free hydroxyl group at C-3 position of sterols to produce sterol glycosides. Solanum contain very high levels of glycosylated sterols, which in the case of tomato may account for more than 85% of the total sterol content. Tomato SGT isozymes show the ability to glycosylate different sterol species including cholesterol, brassicasterol, campesterol, stigmasterol, and beta-sitosterol, which is consistent with the occurrence in their primary structure of the putative steroid-binding domain found in steroid UDP-glucuronosyltransferases and the UDP-sugar binding domain characteristic for a superfamily of nucleoside diphosphosugar glycosyltransferases. The SlSGT isozyme are differentially regulated in response to biotic and abiotic stress conditions. Changes in the relative proportions of sterols alter membrane fluidity and permeability and hence regulate different membrane functions such as simple and carrier-mediated diffusion, active transport across the membrane, and the activity of membrane-associated proteins. Tomato SGT isozymes play overlapping but not completely redundant biological functions involved in mediating developmental and stress responses
physiological function
sterol glycosyltransferases (SGTs) catalyze the glycosylation of the free hydroxyl group at C-3 position of sterols to produce sterol glycosides. Solanum contain very high levels of glycosylated sterols, which in the case of tomato may account for more than 85% of the total sterol content. Tomato SGT isozymes show the ability to glycosylate different sterol species including cholesterol, brassicasterol, campesterol, stigmasterol, and beta-sitosterol, which is consistent with the occurrence in their primary structure of the putative steroid-binding domain found in steroid UDP-glucuronosyltransferases and the UDP-sugar binding domain characteristic for a superfamily of nucleoside diphosphosugar glycosyltransferases. The SlSGT isozyme are differentially regulated in response to biotic and abiotic stress conditions. Tomato SGT isozymes play overlapping but not completely redundant biological functions involved in mediating developmental and stress responses. Changes in the relative proportions of sterols alter membrane fluidity and permeability and hence regulate different membrane functions such as simple and carrier-mediated diffusion, active transport across the membrane, and the activity of membrane-associated proteins
physiological function
-
ectopic enzyme overexpression in Withania somnifera promotes growth, enhances glycowithanolide and provides tolerance to abiotic and biotic stresses. Glycosylation not only stabilizes the products but also alters their physiological activities and governs intracellular distribution
-
physiological function
-
steryl glucoside may be specific only for cellulose biosynthesis in cotton fibers because mature fibers contain more than 95% of cellulose. Isozyme GhSGT2 mainly participates in catalyzing glucosylation of membrane sterols
-
physiological function
-
steryl glucoside may be specific only for cellulose biosynthesis in cotton fibers because mature fibers contain more than 95% of cellulose
-
physiological function
-
no role in steryl glucoside synthesis for UGT713B1/At5g24750
-
physiological function
-
UGT80A2 accounts for most of the sitosteryl and stigmasteryl glucoside production in seeds
-
physiological function
-
UGT80B1 plays a specialized role in steryl glucoside synthesis
-
physiological function
-
sterol glycosyltransferases (SGTs) catalyze the formation of a variety of glycosylated sterol derivatives and are involved in producing a plethora of bioactive natural products. Sterol glycosyltransferases as members of UGTs are involved in transferring a sugar from UDP-sugar to various SGs metabolites, including hormones and secondary metabolites
-
additional information
-
alteration of the membrane physical state caused by heat stress may be linked to activate sterol glucosyltransferase to form cholesteryl glucoside
additional information
a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. A short, conserved sequence of S847-M851 is identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations revealing the sugar acceptor specificity, overview. The N- and C-terminal domains predominantly dictate acceptor and donor specificities, respectively. The donor substrate binds in a deep inter-domain pocket and a hydrophobic crevice on the surface of the N-terminal domain, which is proposed to be the binding site of the aglycone substrate
additional information
-
a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. A short, conserved sequence of S847-M851 is identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations revealing the sugar acceptor specificity, overview. The N- and C-terminal domains predominantly dictate acceptor and donor specificities, respectively. The donor substrate binds in a deep inter-domain pocket and a hydrophobic crevice on the surface of the N-terminal domain, which is proposed to be the binding site of the aglycone substrate
additional information
sterol glucosides patterns of wild-type and mutant roots, overview. The ugt80B1 mutant shows a significant reduction in stigmasteryl glucosides only
additional information
-
sterol glucosides patterns of wild-type and mutant roots, overview. The ugt80B1 mutant shows a significant reduction in stigmasteryl glucosides only
-
additional information
-
a long hydrophobic cavity, 9.2 A in width and 17.6 A in length located at the N-terminal domain of UGT51, is suitable for the accommodation of sterol acceptor substrates. A short, conserved sequence of S847-M851 is identified at the bottom of the hydrophobic cavity, which might be the steroid binding site and play an important role for the UGT51 catalytic specificity towards sterols. Molecular docking simulations revealing the sugar acceptor specificity, overview. The N- and C-terminal domains predominantly dictate acceptor and donor specificities, respectively. The donor substrate binds in a deep inter-domain pocket and a hydrophobic crevice on the surface of the N-terminal domain, which is proposed to be the binding site of the aglycone substrate
-
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S801A/L802A/V804A/K812A/E816K/S849A/N892D
Y642P
amino acid substitution within the GRAM domain abolished this association as well as micropexophagy
Y642P
-
amino acid substitution within the GRAM domain abolished this association as well as micropexophagy
-
S801A/L802A/V804A/K812A/E816K/S849A/N892D
site-directed mutagenesis, the changed unique interaction network in mutant M7_1 with an 1800fold activity improvement toward an unnatural substrate protopanaxadiol (PPD), might influence its substrate preference
S801A/L802A/V804A/K812A/E816K/S849A/N892D
-
site-directed mutagenesis, the changed unique interaction network in mutant M7_1 with an 1800fold activity improvement toward an unnatural substrate protopanaxadiol (PPD), might influence its substrate preference
-
additional information
mutation of isoform UGT80B1 principally alters embryonic development and seed suberin accumulation and cutin formation in the seed coat, leading to abnormal permeability and tetrazolium salt uptake, mutations in UGT80A2 and USG80B1 genes result in reduced seed size, transparent testa, and salt uptake phenotypes
additional information
a T-DNA insertion mutant of UGT713B1/At5g24750 shows a phenotype that seems to be indistinguishable from Col-0 wild-type. A homozygous mutant for ugt713B1, mutation in the in the 5' UTR, seems to express mRNA in semi-quantitative RT-PCR experiments. Construction of an ugt80A2,713B1 double mutant which has a similar sterol profile to the ugt80A2 single mutant showing reduced steryl glucoside content
additional information
a T-DNA insertion mutant of UGT713B1/At5g24750 shows a phenotype that seems to be indistinguishable from Col-0 wild-type. A homozygous mutant for ugt713B1, mutation in the in the 5' UTR, seems to express mRNA in semi-quantitative RT-PCR experiments. Construction of an ugt80A2,713B1 double mutant which has a similar sterol profile to the ugt80A2 single mutant showing reduced steryl glucoside content
additional information
a T-DNA insertion mutant of UGT713B1/At5g24750 shows a phenotype that seems to be indistinguishable from Col-0 wild-type. A homozygous mutant for ugt713B1, mutation in the in the 5' UTR, seems to express mRNA in semi-quantitative RT-PCR experiments. Construction of an ugt80A2,713B1 double mutant which has a similar sterol profile to the ugt80A2 single mutant showing reduced steryl glucoside content
additional information
-
a T-DNA insertion mutant of UGT713B1/At5g24750 shows a phenotype that seems to be indistinguishable from Col-0 wild-type. A homozygous mutant for ugt713B1, mutation in the in the 5' UTR, seems to express mRNA in semi-quantitative RT-PCR experiments. Construction of an ugt80A2,713B1 double mutant which has a similar sterol profile to the ugt80A2 single mutant showing reduced steryl glucoside content
additional information
construction of ugt80A2,713B1 and ugt80A2,B1 double mutants which have similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
construction of ugt80A2,713B1 and ugt80A2,B1 double mutants which have similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
construction of ugt80A2,713B1 and ugt80A2,B1 double mutants which have similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
-
construction of ugt80A2,713B1 and ugt80A2,B1 double mutants which have similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
homozygous mutants for ugt80B1, mutation at the exon-intron boundary following the second exon, is a mRNA knockdown allel. Construction of ugt80A2,B1 double mutant which has a similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
homozygous mutants for ugt80B1, mutation at the exon-intron boundary following the second exon, is a mRNA knockdown allel. Construction of ugt80A2,B1 double mutant which has a similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
homozygous mutants for ugt80B1, mutation at the exon-intron boundary following the second exon, is a mRNA knockdown allel. Construction of ugt80A2,B1 double mutant which has a similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
-
homozygous mutants for ugt80B1, mutation at the exon-intron boundary following the second exon, is a mRNA knockdown allel. Construction of ugt80A2,B1 double mutant which has a similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
additional information
generation of a ugt80A2;B1 double mutant that is more resistant ot infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level, Mutant phenotype, overview
additional information
generation of a ugt80A2;B1 double mutant that is more resistant ot infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level, Mutant phenotype, overview
additional information
generation of a ugt80A2;B1 double mutant that is more resistant to infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level. Mutant phenotype, overview
additional information
generation of a ugt80A2;B1 double mutant that is more resistant to infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level. Mutant phenotype, overview
additional information
generation of ugt80B1 mutants. Sterol glucosides patterns of wild-type and mutant roots, overview. The ugt80B1 mutant shows a significant reduction in stigmasteryl glucosides only. Root hair patterning and GL2 expression are aberrant in ugt80B1 mutants. Expression of upstream cell fate regulators, SCM and WER, is altered in ugt80B1 mutants. Phenotype, overview. The ugt80B1 mutant phenotype is complemented with pro35S:UGT80B1:GFP or with proUGT80B1:UGT80B1:GFP as observed by rescue of the transparent testa phenotype
additional information
-
a T-DNA insertion mutant of UGT713B1/At5g24750 shows a phenotype that seems to be indistinguishable from Col-0 wild-type. A homozygous mutant for ugt713B1, mutation in the in the 5' UTR, seems to express mRNA in semi-quantitative RT-PCR experiments. Construction of an ugt80A2,713B1 double mutant which has a similar sterol profile to the ugt80A2 single mutant showing reduced steryl glucoside content
-
additional information
-
construction of ugt80A2,713B1 and ugt80A2,B1 double mutants which have similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
-
additional information
-
generation of ugt80B1 mutants. Sterol glucosides patterns of wild-type and mutant roots, overview. The ugt80B1 mutant shows a significant reduction in stigmasteryl glucosides only. Root hair patterning and GL2 expression are aberrant in ugt80B1 mutants. Expression of upstream cell fate regulators, SCM and WER, is altered in ugt80B1 mutants. Phenotype, overview. The ugt80B1 mutant phenotype is complemented with pro35S:UGT80B1:GFP or with proUGT80B1:UGT80B1:GFP as observed by rescue of the transparent testa phenotype
-
additional information
-
homozygous mutants for ugt80B1, mutation at the exon-intron boundary following the second exon, is a mRNA knockdown allel. Construction of ugt80A2,B1 double mutant which has a similar sterol profiles to the ugt80A2 and ugt80B1 single mutants, respectively, showing reduced steryl glucoside content
-
additional information
-
generation of a ugt80A2;B1 double mutant that is more resistant to infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level. Mutant phenotype, overview
-
additional information
-
generation of a ugt80A2;B1 double mutant that is more resistant ot infection by Bortrytis cinerea than the wild-type and shows increased levels of jasmonic acid (JA) and upregulation of two marker genes (PDF1.2 and PR4) of the ERF branch of the JA signaling pathway. The mutant also accumulates higher levels of camalexin, the major Arabidopsis thaliana phytoalexin, than wild-type plants. Camalexin accumulation correlates with enhanced transcript levels of several cytochrome P450 camalexin biosynthetic genes, as well as of their transcriptional regulators WRKY33, ANAC042, and MYB51, suggesting that the Botrytis-induced accumulation of camalexin is coordinately regulated at the transcriptional level, Mutant phenotype, overview
-
additional information
null mutant by deletion of ugt52 gene with no enzyme activity
additional information
-
null mutant by deletion of ugt52 gene with no enzyme activity
additional information
-
WsGTL1 transgenic plants overexpressing the enzyme display a number of alterations at phenotypic and metabolic level in comparison to wild-type plants which include: (1) early and enhanced growth with leaf expansion and increase in number of stomata, (2) increased production of glycowithanolide (majorly withanoside V) and campesterol, stigmasterol and sitosterol in glycosylated forms with reduced accumulation of withanolides (withaferin A, withanolide A and withanone), (3) tolerance towards biotic stress, improved survival capacity under abiotic stress (cold stress), (4) enhanced recovery capacity after cold stress, as indicated by better photosynthesis performance, chlorophyll, anthocyanin content and better quenching regulation of PSI and PSII, phenotype overview
additional information
-
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifer. Phenotype, overview
additional information
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifer. Phenotype, overview
additional information
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifer. Phenotype, overview
additional information
-
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifera. Phenotype, overview
additional information
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifera. Phenotype, overview
additional information
analysis of the function of SGTs by virus-induced gene silencing (VIGS) of SGTL1, SGTL2 and SGTL4 in Withania somnifera. Phenotype, overview
additional information
-
WsGTL1 transgenic plants overexpressing the enzyme display a number of alterations at phenotypic and metabolic level in comparison to wild-type plants which include: (1) early and enhanced growth with leaf expansion and increase in number of stomata, (2) increased production of glycowithanolide (majorly withanoside V) and campesterol, stigmasterol and sitosterol in glycosylated forms with reduced accumulation of withanolides (withaferin A, withanolide A and withanone), (3) tolerance towards biotic stress, improved survival capacity under abiotic stress (cold stress), (4) enhanced recovery capacity after cold stress, as indicated by better photosynthesis performance, chlorophyll, anthocyanin content and better quenching regulation of PSI and PSII, phenotype overview
-
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Kalinowska, M.; Wojciechowski, Z.A.
Modulation of activities of steryl glucoside hydrolase and UDPG:sterol glucosyltransferase from Sinapis alba by detergents and lipids
Phytochemistry
25
45-49
1986
Sinapis alba
-
brenda
Kalinowska, M.; Wojciechowski, Z.A.
Enzymatic synthesis of nuatigenin 3-beta-D-glucoside in oat (Avena sativa) leaves
Phytochemistry
25
2525-2529
1986
Avena sativa
-
brenda
Kalinowska, M.; Wojciechowski, Z.A.
Subcellular localization of UDPG:nuatigenin glucosyltransferase in oat leaves
Phytochemistry
26
353-357
1987
Avena sativa
-
brenda
Wojciechowski, J.; Zimowski, J.; Tyski, S.
Enzymatic synthesis of steryl 3-beta-D-monoglucosides in the slime mold Physarum polycephalum
Phytochemistry
16
911-914
1977
Physarum polycephalum
-
brenda
Murakami-Murofushi, K.; Ohta, J.
Expression of UDP-glucose: poriferasterol glucosyltransferase in the process of differentiation of a true slime mold, Physarum polycephalum
Biochim. Biophys. Acta
992
412-415
1989
Physarum polycephalum
brenda
Ullmann, P.; Bouvier-Nave, P.; Benveniste, P.
Regulation by phospholipids and kinetic studies of plant membrane-bound UDP-glucose sterol beta-D-glucosyl transferase
Plant Physiol.
85
51-55
1987
Zea mays
brenda
Esders, T.W.; Light, R.J.
Occurrence of a uridine diphosphate glucose: sterol glucosyltransferase in Candida bogoriensis
J. Biol. Chem.
247
7494-7497
1972
Pseudohyphozyma bogoriensis
brenda
Yoshikawa, T.; Furuya, T.
Purification and properties of sterol:UDPG glucosyltransferase in cell culture of Digitalis purpurea
Phytochemistry
18
239-241
1979
Digitalis purpurea
-
brenda
Wojciechowski, Z.A.; Zimowski, J.; Zimowski, J.G.; Lyznik, A.
Specificity of sterol-glucosylating enzymes from Sinapis alba and Physarum polycephalum
Biochim. Biophys. Acta
570
363-370
1979
Physarum polycephalum, Sinapis alba
brenda
Ury, A.; Benveniste, P.; Bouvier-Nave, P.
Phospholipid dependence of plant UDP-glucose sterol beta-D-glucosyl transferase
Plant Physiol.
91
567-573
1989
Zea mays
brenda
Paczkowski, C.; Zimowski, J.; Krawczyk, D.; Wojciechowski, Z.A.
Steroid-specific glucosyltransferase in Asparagus plumosus shoots
Phytochemistry
29
63-70
1990
Asparagus setaceus
-
brenda
Fang, T.Y.; Baisted, D.J.
UDPG:sterol glucosyltransferase in etiolated pea seedlings
Phytochemistry
15
273-278
1976
Pisum sativum
-
brenda
Staver, M.J.; Glick, K.; Baisted, D.J.
Uridine diphosphate glucose-sterol glucosyltransferase and nucleoside diphosphatase activities in etiolated pea seedlings
Biochem. J.
169
297-303
1978
Pisum sativum
brenda
Forsee, W.T.; Laine, R.A.; Elbein, A.D.
Solubilization of a particulate UDP-Glucose:sterol beta-glucosyltransferase in developing cotton fibers and seeds and characterization of steryl 6-acyl-D-glucosides
Arch. Biochem. Biophys.
161
248-259
1974
Gossypium hirsutum
-
brenda
Bouvier-Nave, P.; Ullmann, P.; Rimmele, D.; Benveniste, P.
Phospholipid-dependence of plant UDP-glucose-sterol-beta-D-glucosyltransferase. I. Detergent-mediated delipidatio by selective solubilization
Plant Sci. Lett.
36
19-27
1984
Zea mays
-
brenda
Quantin-Martenot, E.; Benveniste, P.; Hartmann, M.A.; Bouvier-Nave, P.
Activation of etiolated maize coleoptiles plasma membrane-bound uridine-diphosphate-glucose-sterol-beta-D-glucosyltransferase by triton X-100, hydroxyl ions and phospholipase A2
Plant Sci. Lett.
29
305-314
1983
Zea mays
-
brenda
Ullmann, P.; Rimmele, D.; Benveniste, P.; Bouvier-Nave, P.
Phospholipid-dependence of plant UDP-glucose-sterol-beta-D-glucosyltransferase. II. Acetone-mediated delipidation and kinetic studies
Plant Sci. Lett.
36
29-36
1984
Zea mays
-
brenda
Ullmann, P.; Ury, A.; Rimmele, D.; Benveniste, P.; Bouvier-Nave, P.
UDP-glucose sterol beta-D-glucosyltransferase, a plasma membrane-bound enzyme of plants: Enzymic properties and lipid dependence
Biochimie
75
713-723
1993
Zea mays
brenda
Warnecke, D.C.; Heinz, E.
Purification of a membrane-bound UDP-glucose:sterol beta-D-glucosyltransferase based on its solubility in diethyl ether
Plant Physiol.
105
1067-1073
1994
Avena sativa
brenda
Warnecke, D.C.; Baltrusch, M.; Buck, F.; Wolter, F.P.; Heinz, E.
UDP-glucose:sterol glucosyltransferase: cloning and functional expression in Escherichia coli
Plant Mol. Biol.
35
597-603
1997
Avena sativa (O22678), Arabidopsis thaliana (Q9M8Z7), Avena sativa ugt80A1 (O22678)
brenda
Warnecke, D.; Erdmann, R.; Fahl, A.; Hube, B.; Muller, F.; Zank, T.; Zahringer, U.; Heinz, E.
Cloning and functional expression of UGT genes encoding sterol glucosyltransferases from Saccharomyces cerevisiae, Candida albicans, Pichia pastoris, and Dictyostelium discoideum
J. Biol. Chem.
274
13048-13059
1999
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Saema, S.; Rahman, L.U.; Singh, R.; Niranjan, A.; Ahmad, I.Z.; Misra, P.
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Castillo, N.; Pastor, V.; Chavez, A.; Arro, M.; Boronat, A.; Flors, V.; Ferrer, A.; Altabella, T.
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