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(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-xylose 1-phosphate
alpha-D-xylose-(1,4-alpha-D-glucosyl)n + phosphate
-
polysaccharide substrate is starch, very low activity
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
(maltodextrin)n + phosphate
(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
?
(maltodextrin)n-1 + alpha-D-glucose 1-phosphate
(maltodextrin)n + phosphate
-
maltodextrin phosphorylase is involved in the utilization of maltodextrins
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
(maltooligosaccaride)n-1 + alpha-D-glucose 1-phosphate
(maltooligosaccharide)n + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
alpha-D-glucose-1-phosphate + maltohexaose
amylose + phosphate
-
-
in presence of lipids, spontaneous formation and precipitation of amylose-lipid complexes. Presence of lipid also leads to lower amylose degrees of polymerization. Lipid chain length defines degree of amylose polymerization, which increases in the order myristic acid, glyceryl monostearate, stearic acid and docosanoic acid. Thermal stability of complexes increases in the same manner
-
?
amylopectin + alpha-D-glucose 1-phosphate
amylopectin + phosphate
-
-
-
?
amylopectin + glucose 1-phosphate
amylopectin + phosphate
amylopectin + phosphate
amylopectin + D-glucose-1-phosphate
amylose + glucose 1-phosphate
amylose + phosphate
amylose + phosphate
amylose + D-glucose-1-phosphate
amylose + phosphate
amylose + glucose 1-phosphate
debranched amylopectin + glucose 1-phosphate
debranched amylopectin + phosphate
-
most effective primer glucan for chloroplastic enzyme
-
r
dextrin + alpha-D-glucose 1-phosphate
dextrin + phosphate
dextrin DP11 + phosphate
dextrin DP10 + alpha-D-glucose 1-phosphate
-
-
-
-
?
dextrin DP13 + alpha-D-glucose 1-phosphate
dextrin DP14 + phosphate
dextrin DP14 + phosphate
dextrin DP13 + alpha-D-glucose 1-phosphate
dextrin DP18 + alpha-D-glucose 1-phosphate
dextrin DP19 + phosphate
-
prolongation of the dextrin molecule with one glucose monomer
-
-
r
dextrin DP19 + phosphate
dextrin DP18 + alpha-D-glucose 1-phosphate
-
-
-
-
r
dextrin DP3 + alpha-D-glucose 1-phosphate
dextrin DP4 + phosphate
-
prolongation of the dextrin molecule with one glucose monomer
-
-
r
dextrin DP4 + phosphate
dextrin DP3 + alpha-D-glucose 1-phosphate
-
-
-
-
r
dextrin DP9 + phosphate
dextrin DP8 + alpha-D-glucose 1-phosphate
-
-
-
-
?
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
glycogen + glucose 1-phosphate
glycogen + phosphate
glycogen + phosphate
? + alpha-D-glucose 1-phosphate
-
-
-
r
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
alpha-D-glucose 1-phosphate + ?
-
-
-
-
?
glycogen + phosphate
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
glycogen + glucose 1-phosphate
glycogen DP14 + phosphate
glycogen DP13 + alpha-D-glucose 1-phosphate
-
-
-
-
r
granulose + glucose 1-phosphate
granulose + phosphate
-
-
-
?
maltodecaheptaose + phosphate
maltodecahexaose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltodecaose + alpha-D-glucose 1-phosphate
? + phosphate
-
low activity
-
-
r
maltodextrin + phosphate
? + alpha-D-glucose 1-phosphate
-
-
-
r
maltoheptadecaose + glucose 1-phosphate
maltooctadecaose + phosphate
-
-
-
r
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
maltohexaose + arsenate
maltopentaose + glucose 1-arsenate
-
-
-
?
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
maltohexaose + phosphate
maltopentaose + alpha-D-glucose 1-phosphate
maltononaose + alpha-D-glucose 1-phosphate
maltodecaose + phosphate
-
low activity
-
-
r
maltooctaose + alpha-D-glucose 1-phosphate
maltononaose + phosphate
-
low activity
-
-
r
maltooctaose + glucose 1-phosphate
maltononaose + phosphate
maltopentaose + alpha-D-glucose 1-phosphate
maltohexaose + phosphate
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
maltopentaose + phosphate
?
-
-
-
?
maltopentaose + phosphate
maltotetraose + alpha-D-glucose 1-phosphate
maltose + alpha-D-glucose 1-phosphate
?
-
-
-
-
?
maltose + alpha-D-glucose 1-phosphate
maltotriose + phosphate
maltotetraose + 2-amino-2-deoxy-alpha-D-glucopyranosyl 1-phosphate
GlcNAc-alpha-(1->4)-Glc-alpha-(1->4)-Glc-alpha-(1->4)-Glc-alpha-(1->4)-Glcalpha + phosphate
-
-
alpha-glucosamine is positioned at the non-reducing end of the oligosaccharide
-
?
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
maltotetraose + D-glucose-1-phosphate
maltopentaose + phosphate
-
-
-
-
?
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
maltotriose + phosphate
maltobiose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltotriose + phosphate
maltose + alpha-D-glucose 1-phosphate
pyridylamino-maltohexaose + alpha-D-glucose 1-phosphate
pyridylamino-maltoheptaose + phosphate
-
-
-
r
soluble heteroglycan + alpha-D-glucose 1-phosphate
? + phosphate
-
substrate is a soluble heteroppolysaccharide containing a high percentage of arabinogalactan-like linkages but also minor components, namely glucosyl, mannosyl, rhamnosyl, and fucosyl residues, and is isolated from pea leaf cytosol, 3 different variants, overview
-
-
?
soluble starch + alpha-D-glucose 1-phosphate
?
Voandzeia subterranea
-
-
-
-
?
soluble starch + phosphate
?
-
-
-
-
?
soluble starch + phosphate
? + alpha-D-glucose 1-phosphate
-
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
starch + glucose 1-phosphate
starch + phosphate
starch + phosphate
? + alpha-D-glucose 1-phosphate
-
-
-
r
starch + phosphate
starch + D-glucose 1-phosphate
-
-
-
?
starch + phosphate
starch + D-glucose-1-phosphate
starch DP24 + phosphate
starch DP23 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
additional information
?
-
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen
-
-
?
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is bovine liver glycogen
-
-
?
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrate is glycogen, mobilization of glucose 1-phosphate as readily useable energy source
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrates are glycogen and starch, phosphorolysis is the preferred reaction
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrates are starch and glycogen, phosphorolysis is the preferred reaction, maltotetraose is the smallest substrate accepted
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrate is glycogen
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen, phosphorolysis is the preferred reaction
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is starch, phosphorolysis is the physiologic reaction of the starch degrading enzyme
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrates are soluble starch and Zulkowsky soluble starch, amylopectin, glycogen, and dextrin, amyylopectin is the best substrate
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen
-
-
?
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
the cytosolic isozyme is involved in the processing of incoming carbohydrate during rapid tissue growth, plastidic isozyme is associated with transitory leaf starch metabolism and with the initiation of seed endosperm reserve starch accumulation, but it plays no role in the degradation of the reserve starch
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
the cytosolic isozyme utilizes amylopectin, amylose, soluble starch, and glycogen as polysaccharide substrates, while the plastidic isozyme prefers starch
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
?
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
maltodextrin phosphorylase, preferred substrate
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
preferred substrate
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
not phosphorylase B
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
less effective than starch, amylose or glycogen
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
achrodextrin
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
corn dextrin, phosphorolysis at 85% the rate of glycogen phosphorolysis
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
corn dextrin, phosphorolysis at 85% the rate of glycogen phosphorolysis
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
best substrate
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
preferred substrate
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
corn dextrin
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(dextrin)n-1 + glucose 1-phosphate
(dextrin)n + phosphate
-
-
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
phosphorolysis activity ceases when maltodextrins are degraded to maltotetraose
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
glucosylation at 96% the rate of maltoheptaose glucosylation
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 5 glucose units per maltodextrin molecule
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 4 glucose units per maltodextrin molecule
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
maltodextrin with up to 11 glucose units
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 5 glucose units per maltodextrin molecule
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 4 glucose units per maltodextrin molecule
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
-
-
?
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
-
-
r
(maltooligosaccaride)n-1 + alpha-D-glucose 1-phosphate
(maltooligosaccharide)n + phosphate
-
-
-
r
(maltooligosaccaride)n-1 + alpha-D-glucose 1-phosphate
(maltooligosaccharide)n + phosphate
preferred substrate
-
-
r
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
r
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
r
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
r
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
best substrate
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
potato amylopectin
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
preferred substrate
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
glucosylation at 23% the rate of maltoheptaose glucosylation
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
waxy maize amylopectin
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
less effective than starch, amylose or glycogen
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
potato amylopectin
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
waxy rice or pea cotyledon
-
-
?
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
effective primer
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
-
?
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
-
-
r
amylopectin + glucose 1-phosphate
amylopectin + phosphate
-
best substrate
-
-
?
amylopectin + phosphate
amylopectin + D-glucose-1-phosphate
-
-
-
-
?
amylopectin + phosphate
amylopectin + D-glucose-1-phosphate
-
-
-
-
?
amylopectin + phosphate
amylopectin + D-glucose-1-phosphate
-
-
-
-
?
amylopectin + phosphate
amylopectin + D-glucose-1-phosphate
-
-
-
r
amylose + glucose 1-phosphate
amylose + phosphate
-
-
-
?
amylose + glucose 1-phosphate
amylose + phosphate
-
glucosylation at 7% the rate of maltoheptaose glucosylation
-
?
amylose + glucose 1-phosphate
amylose + phosphate
-
best substrate
-
?
amylose + glucose 1-phosphate
amylose + phosphate
-
-
-
?
amylose + glucose 1-phosphate
amylose + phosphate
-
effective primer
-
r
amylose + glucose 1-phosphate
amylose + phosphate
-
potato amylose
-
r
amylose + glucose 1-phosphate
amylose + phosphate
-
-
-
r
amylose + phosphate
amylose + D-glucose-1-phosphate
-
-
-
-
?
amylose + phosphate
amylose + D-glucose-1-phosphate
-
-
-
-
?
amylose + phosphate
amylose + glucose 1-phosphate
-
-
-
?
amylose + phosphate
amylose + glucose 1-phosphate
-
pea cotyledon amylose
-
?
amylose + phosphate
amylose + glucose 1-phosphate
-
arsenate can replace phosphate
-
?
dextrin + alpha-D-glucose 1-phosphate
dextrin + phosphate
-
-
-
?
dextrin + alpha-D-glucose 1-phosphate
dextrin + phosphate
-
-
-
-
?
dextrin DP13 + alpha-D-glucose 1-phosphate
dextrin DP14 + phosphate
-
prolongation of the dextrin molecule with one glucose monomer
-
-
r
dextrin DP13 + alpha-D-glucose 1-phosphate
dextrin DP14 + phosphate
-
prolongation of the dextrin molecule with one glucose monomer
-
-
r
dextrin DP14 + phosphate
dextrin DP13 + alpha-D-glucose 1-phosphate
-
-
-
-
r
dextrin DP14 + phosphate
dextrin DP13 + alpha-D-glucose 1-phosphate
-
-
-
-
r
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
enzyme catalyzes the initial degradation of glycogen
-
-
?
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
75% of the activity with maltose, 64% of the activity with maltoheptaose
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
rabbit liver glycogen
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: rabbit liver
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
rabbit liver glycogen
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
preferred substrate of glycogen phosphorylase
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
Indocibium guttattam
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: rabbit liver
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glucosylation at 14.4% the rate of maltoheptaose glucosylation
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
best substrate
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
not phosphorylase B
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from shell fish
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
yeast or rabbit enzyme
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
endogenous glycogen
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: rabbit liver
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
best substrate
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
best substrate
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from Streptococcus salivarius
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from Streptococcus salivarius
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
rabbit liver glycogen
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
phytoglycogen
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
favoured reaction
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
yeast or rabbit enzyme
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
favoured reaction
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: rabbit liver
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
about half as effective as dextrin
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from: oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
poor substrate
-
-
?
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
-
-
-
-
r
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
-
-
-
-
r
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
-
-
-
-
r
glycogen + phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
-
-
-
r
glycogen + phosphate
glycogen + alpha-D-glucose 1-phosphate
-
-
-
r
glycogen + phosphate
glycogen + alpha-D-glucose 1-phosphate
-
-
-
-
?
glycogen + phosphate
glycogen + glucose 1-phosphate
-
-
-
-
?
glycogen + phosphate
glycogen + glucose 1-phosphate
-
-
-
?
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
-
low activity
-
-
r
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
80% of the activity with maltose
-
-
r
maltoheptaose + alpha-D-glucose 1-phosphate
maltooctaose + phosphate
the cytosolic isozyme
-
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
best substrate
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
poor substrate
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
best substrate
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
isozyme I
-
r
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
-
-
r
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
-
-
-
r
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
35% of the activity with maltoheptaose
-
-
r
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
-
-
-
-
?
maltoheptaose + phosphate
maltohexaose + alpha-D-glucose 1-phosphate
the cytosolic isozyme
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
-
low activity
-
-
r
maltohexaose + alpha-D-glucose 1-phosphate
maltoheptaose + phosphate
82% of the activity with maltose
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltohexaose + phosphate
maltopentaose + alpha-D-glucose 1-phosphate
-
-
-
r
maltohexaose + phosphate
maltopentaose + alpha-D-glucose 1-phosphate
85% of the activity with maltoheptaose
-
-
r
maltooctaose + glucose 1-phosphate
maltononaose + phosphate
-
-
-
r
maltooctaose + glucose 1-phosphate
maltononaose + phosphate
-
-
-
r
maltopentaose + alpha-D-glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + alpha-D-glucose 1-phosphate
maltohexaose + phosphate
-
-
-
-
r
maltopentaose + alpha-D-glucose 1-phosphate
maltohexaose + phosphate
86% of the activity with maltose
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
?
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
cytoplasmic enzyme, glucosylation at the same rate of glucosylation of debranched amylopectin, chloroplastic enzyme, glucosylation at 50% the rate of glucosylation of debranched amylopectin
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
isozyme I
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltopentaose + phosphate
maltotetraose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltopentaose + phosphate
maltotetraose + alpha-D-glucose 1-phosphate
-
-
-
r
maltopentaose + phosphate
maltotetraose + alpha-D-glucose 1-phosphate
78% of the activity with maltoheptaose
-
-
r
maltopentaose + phosphate
maltotetraose + alpha-D-glucose 1-phosphate
-
-
-
-
?
maltose + alpha-D-glucose 1-phosphate
maltotriose + phosphate
-
not phosphorylase B
-
?
maltose + alpha-D-glucose 1-phosphate
maltotriose + phosphate
-
less effective than starch, amylose or glycogen
-
?
maltose + alpha-D-glucose 1-phosphate
maltotriose + phosphate
-
-
-
?
maltose + alpha-D-glucose 1-phosphate
maltotriose + phosphate
-
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
-
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
-
-
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
90% of the activity with maltose
-
-
r
maltotetraose + alpha-D-glucose 1-phosphate
maltopentaose + phosphate
the cytosolic isozyme
-
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
best substrate
-
ir
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
ir
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
smallest acceptor for synthesis
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
glucosylation at 22% the rate of maltoheptaose glucosylation
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
ir
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
ir
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
?
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
cytoplasmic enzyme: poor substrate
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
ir
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
-
-
-
r
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
61% of the activity with maltoheptaose
-
-
r
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
-
50% of the activity with maltopentaose
-
-
?
maltotetraose + phosphate
maltotriose + alpha-D-glucose 1-phosphate
-
-
-
-
r
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
maltotriose is the smallest substrate accepted for the synthetic reaction direction, maltotetraose is the smallest substrate accepted for the phosphorolytic reaction direction
-
-
r
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
95% of the activity with maltose
-
-
r
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
-
-
-
-
r
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
-
-
-
-
?
maltotriose + alpha-D-glucose 1-phosphate
maltotetraose + phosphate
-
-
-
-
r
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
-
-
-
r
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
-
less effective than starch, amylose or glycogen
-
r
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
-
-
r
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
-
-
-
r
maltotriose + glucose 1-phosphate
maltotetraose + phosphate
-
-
-
ir
maltotriose + phosphate
maltose + alpha-D-glucose 1-phosphate
-
-
-
r
maltotriose + phosphate
maltose + alpha-D-glucose 1-phosphate
35% of the activity with maltoheptaose
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
-
prolongation of the starch molecule with one glucose monomer
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
-
prolongation of the starch molecule with one glucose monomer
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
-
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
preferred substrate
-
-
r
starch + alpha-D-glucose 1-phosphate
starch + phosphate
-
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
-
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
-
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
best substrate
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
poor substrate
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
phosphorolysis at 31% the rate of glycogen phosphorolysis
-
r
starch + glucose 1-phosphate
starch + phosphate
-
phosphorolysis at 31% the rate of glycogen phosphorolysis
-
r
starch + glucose 1-phosphate
starch + phosphate
-
best substrate
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
native chloroplast grains
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
-
-
?
starch + glucose 1-phosphate
starch + phosphate
-
best substrate
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
potato enzyme
-
r
starch + glucose 1-phosphate
starch + phosphate
-
glucosylation at 32% the rate of dextrin glucosylation
-
?
starch + glucose 1-phosphate
starch + phosphate
-
-
-
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
glucosylation of native starch granules occurs at 82%, isozyme P-1, or 11.5%, isozyme P-2, the rate of soluble starch, phosphorolysis at the same rate as soluble starch
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
starch + phosphate
starch + D-glucose-1-phosphate
-
-
-
-
?
starch + phosphate
starch + D-glucose-1-phosphate
-
-
-
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
ineffective primer: glucose
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
key step in cellular differentiation of Dictyostelium discoideum
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with glucose 6-phosphate, fructose 6-phosphate, and fructose 1,6-diphosphate
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
strict specificity for glucose 1-phosphate
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
pathway in starch
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
pathway in starch
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with Schardinger dextrin and cellulose
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
favoured reaction
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
catalyzes incorporation of glucose into alpha-1,4-glucosidic linkage on exterior chains of primer, glycogen synthesis is preferred
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
Gracilaria sordida
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
Gracilaria sordida
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
Gracilaria sordida Harv. W. Nelsen
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
the liver enzyme catalyzes the forward reaction
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
Indocibium guttattam
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with pullulan
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with dextran
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with sucrose
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with glucose 6-phosphate, fructose 6-phosphate, and fructose 1,6-diphosphate
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with ribose 5-phosphate
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
strict specificity for glucose 1-phosphate
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with Schardinger dextrin and cellulose
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
glycogen metabolism
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
bovine liver glycogen, effects of the C-terminal domain on enzyme binding to glycogen, overview
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
usage of four different assay methods
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
no activity with pullulan
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
broad substrate specificity in both the synthesis and degradation of maltooligosaccharides In the synthetic direction of the enzymatic reaction, the lowest oligosaccharide required for the chain elongation is maltose. In the degradative direction the archaeal enzyme can produce D-glucose-1-phosphate from maltotriose or longer maltooligosaccharides including both glycogen and starch
-
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
glycogen metabolism
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
unprimed reaction: lag-phase, product presumably protein-bound glucan
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
maltose is the minimum primer for glucan synthesis and maltotriose is the minimum substrate for degradation
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
glycogen metabolism
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
Voandzeia subterranea
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
polyglucose primer required
-
r
additional information
?
-
-
broad substrate specificities for different chain length dextrins and soluble starch, enzyme efficiency on dextrin DP4 is approximately 5fold lower than that on dextrin DP14 although kcat on dextrin DP4 is higher than on dextrin DP14
-
-
?
additional information
?
-
-
broad substrate specificities for different chain length dextrins and soluble starch, enzyme efficiency on dextrin DP4 is approximately 5fold lower than that on dextrin DP14 although kcat on dextrin DP4 is higher than on dextrin DP14
-
-
?
additional information
?
-
-
the cell volume affects the activity in hepatocytes, thus the enzyme activity is a function of medium osmolarity, activity is increased in hyperosmotic media, overview
-
-
?
additional information
?
-
maltotriose is the smallest substrate accepted for the synthetic reaction direction, maltotetraose is the smallest substrate accepted for the phosphorolytic reaction direction
-
-
?
additional information
?
-
enzyme is involved in storage starch synthesis
-
-
?
additional information
?
-
enzyme is involved in storage starch synthesis
-
-
?
additional information
?
-
-
enzyme is involved in storage starch synthesis
-
-
?
additional information
?
-
-
phosphorylase GlgP catalyzes glycogen breakdown and affects glycogen structure by removing glucose units from the polysaccharide outer chains
-
-
?
additional information
?
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
additional information
?
-
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
additional information
?
-
the enzyme specifically binds to mastoparan, a wasp venom toxin
-
-
?
additional information
?
-
-
the enzyme specifically binds to mastoparan, a wasp venom toxin
-
-
?
additional information
?
-
-
GPa reduces arsenate (As(V)) to the more toxic arsenite (As(III)) in a glutathione (GSH)-dependent fashion
-
-
?
additional information
?
-
-
a maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase
-
-
?
additional information
?
-
-
the catalytic site binds glucose 1-phosphate, glycogen, glucose, and glucose analogues
-
-
?
additional information
?
-
the assay of enzyme activity at micromolar concentration of maltooligosyl-substrate is about 100 times lower than that in conventional enzyme assays using glycogen
-
-
?
additional information
?
-
-
substrate specificity, no or nearly no activity with glucose, maltose, and maltotriose, overview
-
-
?
additional information
?
-
-
enzyme is involved in starch degradation during submergence stress in rice plants
-
-
?
additional information
?
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
additional information
?
-
-
Pho1 not only degrades maltohexaose but also extends them to synthesize longer malto-oligosaccharides, production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate
-
-
?
additional information
?
-
-
increased enzyme activity increases 5-phosphoribosyl-1-diphosphate availability in hepatocyte cultures and vice versa, glycogenolysis is a major contributor to PRPP generation in liver tissue in the basal state
-
-
?
additional information
?
-
-
the enzyme regulates the association of glycogen synthase with a proteoglycogen substrate in hepatocytes
-
-
?
additional information
?
-
-
glycogen phosphorylase is dynamically regulated during and after status in the adult rat, and may have an important role in the pilocarpine model of epilepsy
-
-
?
additional information
?
-
glycogen phosphorylase activity is measured in the direction of glycogen degradation (phosphorolysis)
-
-
?
additional information
?
-
-
no substrate in direction of glucose 1-phosphate synthesis: pullulan, maltotriose
-
-
?
additional information
?
-
substrate specificity of cytosolic isozyme
-
-
?
additional information
?
-
-
substrate specificity of cytosolic isozyme
-
-
?
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(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(2-naphthyl)-1,4,2-oxathiazole
-
-
(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(4-methoxyphenyl)-1,4,2-oxathiazole
-
-
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-1H-pyrrolo[2,3-c]pyridin-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-6-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-7-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2alpha)-3-hydroxyolean-12-en-28-oic acid
-
-
(2alpha,3beta)-2,3-bis(acetyloxy)olean-12-en-28-oic acid
-
-
(2alpha,3beta)-2,3-bis(butanoyloxy)olean-12-en-28-oic acid
-
-
(2alpha,3beta)-2,3-bis(propanoyloxy)olean-12-en-28-oic acid
-
-
(2beta)-2-hydroxyurs-12-en-28-oic acid
-
-
(2beta)-3-hydroxyolean-12-en-28-oic acid
-
-
(2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oic acid
-
-
(2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oic acid
-
-
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
-
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
-
(2E,2'E)-N,N'-butane-1,4-diylbis[3-(3,4-dichlorophenyl)-acrylamide]
-
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
crystallization data
(2R)-2-cyclohexyl-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]propanoic acid
-
potent in vitro inhibition, reduced inhibition of CYP2C9 and good pharmacokinetic properties
(2R,3R,4S,5R,6R)-3,4,5,9-tetrahydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
-
(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
-
(2S)-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]heptanoic acid
-
(2S)-cyclohexyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
-
-
(2S)-cyclopentyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
-
-
(2Z)-2-(hydroxyimino)olean-12-en-28-oic acid
-
-
(2Z)-2-(hydroxyimino)urs-12-en-28-oic acid
-
-
(3beta)-28-[(2-[[2-(acetylamino)ethyl]amino]ethyl)amino]-28-oxoolean-12-en-3-yl acetate
-
-
(3beta)-28-[(3-aminopropyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
-
-
(3beta)-28-[(6-aminohexyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
-
-
(3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oic acid
-
-
(3beta)-N-(6-aminohexyl)-3,23-dihydroxylup-20(29)-en-28-amide
-
-
(3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oic acid
-
-
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
-
-
(4aS,6aS,6bR,8aR,14aR,14bR,16bS)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinoxaline-4a(2H)-carboxylic acid
-
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(2-naphthyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-methoxyphenyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-toluyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
-
(5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane 2,2-dioxide
-
-
(5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(5,6,7,8-tetrahydronaphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-2-thioxo-6-oxa-1,3-diazaspiro[4.5]decan-4-one
-
-
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
-
(6aS,6bR,8aR,16aR,16bR,18bS)-2,2,6a,6b,9,9,16a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,16,16a,16b,17,18b-hexadecahydrochryseno[1,2-b]phenazine-4a(2H)-carboxylic acid
-
-
(NH4)2SO4
-
50-300 mM, weak inhibition
1'-(methylsulfonyl)pyrazolo[4,3-b]olean-12-en-28-oic acid
-
-
1'-acetylpyrazolo[4,3-b]olean-12-en-28-oic acid
-
-
1'-propanoylpyrazolo[4,3-b]olean-12-en-28-oic acid
-
-
1,3,5-tris-4'-2''-[3'''-C-(beta-D-glucopyranosyl)-1''',2''',4'''-oxadiazol-5'''-yl]ethyl-1',2',3'-triazol-1'-ylmethylbenzene
-
trivalent inhibitor. The valency of the molecules influences slightly the inhibition of the enzyme whereas the presence of a spacer arm between the core and the pharmacophore moieties does not
1,3,5-tris[3'-C-(beta-D-glucopyranosyl)-1',2',4'-oxadiazol-5'-yl]-benzene
-
trivalent inhibitor. The valency of the molecules influences slightly the inhibition of the enzyme whereas the presence of a spacer arm between the core and the pharmacophore moieties does not
1,4-dideoxy-1,4-imino-D-arabinitol
-
inhibits Pa-catalyzed As(V) reduction, inhibition of As(V) reduction is not influenced by glucose or AMP
1,5-anhydro-2,3,4,6-tetra-O-benzyl-1-methylidene-D-glucitol
-
-
1,5-gluconolactone
-
strong inhibition of muscle isozyme a and b
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
1-(2-naphthyl)-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
1-(beta-D-glucopyranosyl)-4-hydroxymethyl-1,2,3-triazole
-
-
1-(beta-D-glucopyranosyl)-4-phenyl-1,2,3-triazole
-
-
1-(beta-D-glucopyranosyl)-5-(hept-1-yn-1-yl)uracil
-
-
1-(beta-D-glucopyranosyl)-5-(pent-1-yn-1-yl)uracil
-
-
1-(beta-D-glucopyranosyl)-5-ethynyluracil
-
cytotoxic effect on Hep-G2 cells
1-(beta-D-glucopyranosyl)-5-iodouracil
-
-
1-deoxy-1-methoxycarbonylamino-beta-D-glucopyranose
-
1-methyl-3-([4-(2-thienylmethyl)phenyl]amino)quinoxalin-2(1H)-one
-
50% inhibition at 0.00011 mM in glycogenolysis assay, no bioavailability in vivo
1-phenyl-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
1-[6-(acetyloxy)hexyl] 4-(7-[[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]heptyl) (2R)-2-hydroxybutanedioate
-
-
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclodecanecarboxylic acid
-
-
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclooctanecarboxylic acid
-
potent in vitro inhibition, reduced inhibition of CYP2C9 and good pharmacokinetic properties
2,2',2''-tris[(2E)-4-hydroxybut-2-en-1-yl] 1,1',1''-(3b,5x,9x,13x,18x)-lup-20(29)-ene-3,23,28-triyl triethanedioate
-
-
2,3,4,6-tetra-O-acetyl-1-O-[(2alpha,3beta)-2,3-dihydroxy-28-oxoolean-12-en-28-yl]-beta-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-(hydroxymethyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-(iodomethyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-({[(4-methylphenyl)sulfonyl]oxy}methyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-({[2-(1H-indol-3-yl)ethyl]amino}methyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-methyl-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(chlorooxy)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(hydroxyamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(naphthalen-2-ylamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(pyridin-2-ylamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-{[(4-methoxyphenyl)amino]methyl}-alpha-D-glucopyranose
-
-
2,3-dichloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.002 microM
2,3-dichloro-N-(1-[3-hydroxy-2-(hydroxymethyl)propyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.038 microM
2,3-dichloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.007 microM
2,3-dihydroisooxazolyl oleanolic acid benzyl ester
-
50% inhibition at 0.0196 mM
2,3-diphosphoglycerate
-
5 mM, 30% inhibition
2,4-dinitrophenol
-
5 mM, 67% inhibition
2-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)-4-methoxybutanoic acid
-
-
2-(phenylamino)ethyl (3beta)-3-hydroxyurs-12-en-28-oate
-
-
2-amino-3,4-dihydroxy-5-methoxybenzoic acid
-
-
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-bromoethyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
2-bromoethyl (3beta)-3-hydroxyurs-12-en-28-oate
-
-
2-chloro-N-((3R)-1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.040 microM
2-chloro-N-((3R)-1-[(2S)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.021 microM
2-chloro-N-((3S)-1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.027 microM
2-chloro-N-((3S)-1-[(2S)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.012 microM
2-chloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.029 microM
2-chloro-N-(1-[2-(methylsulfinyl)ethyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.048 microM
2-chloro-N-(2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.041 microM
2-chloro-N-[1-(2-hydroxybutyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.044 microM
2-chloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.026 microM
2-chloro-N-[1-(2-methoxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.05 microM
2-chloro-N-[1-(3-hydroxypropyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.021 microM
2-chloro-N-[1-(cyanomethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.028 microM
2-Cresol
-
5 mM, 67% inhibition
2-ethoxy-2-oxoethyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
2-ethoxy-2-oxoethyl (2beta,3alpha,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2,3-dihydroxyolean-12-en-28-oate
-
50% inhibition at 0.019 mM
2-ethylimidazole
weak inhibition of wild-type activity, inhibition of mutant enzyme H334G
2-hydroxymethenyl oleanonic acid benzyl ester
-
50% inhibition at 0.0063 mM
2-methylimidazole
weak inhibition of wild-type activity
2-O-acetyl-3-oxomaslinic acid benzyl ester
-
50% inhibition at 0.029 mM
2-oxours-12-en-28-oic acid
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (1S,2R,4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-1,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-2,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
-
-
2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]-N-(3'',4''-dichlorobenzyl)acetamide
-
-
2beta,3alpha-dihydroxyurs-12-en-28-oic acid
-
-
3,5-dinitrobenzoic acid
-
5 mM, 47% inhibition
3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)propanoic acid
-
-
3-(beta-D-glucopyranosyl)-1-(2-naphthyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(beta-D-glucopyranosyl)-1-phenyl-1H-1,2,4-triazol-5(4H)-one
-
3-(beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(beta-D-glucopyranosyl)-6-pentyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
-
3-(beta-D-glucopyranosyl)-6-propyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
-
3-Aminophenol
-
5 mM, 20% inhibition
3-methoxypterolactone
-
-
3-Nitrophenol
-
5 mM, 83% inhibition
3-O-[1-(methyl 6-deoxy-alpha-D-glucopyranosid-6-yl)-1H-1,2,3-triazol-4-yl]methyl 3b-hydroxyolean-12-en-28-oate
inhibitor is predicted to bind at the T-state allosteric site exclusively. The binding position of the oleanolic acid moiety occupies the same location as the T-state allosteric site of asiatic acid in the crystal structure. The newly attached sugar moiety shields the carboxyl group of oleanolic acid from forming the salt bridge with Arg310, and consequently reverses the orientation of the oleanolic acid as well as propelled the sugar moiety to extend more deeply into the alloteric dimer interface. As a result, a new hydrogen-bonding network forms between the sugar hydroxyls and the carboxyl of Asp227 plus the guanidino of Arg193, respectively, enhancing their contribution to the stability of the complex
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)amino]-3-oxopropanoic acid
-
-
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]propanoic acid
-
-
3-[(4-isoxazolidin-3-ylphenyl)amino]-1-methylquinoxalin-2(1H)-one
-
50% inhibition at 0.00011 mM in glycogenolysis assay, no bioavailability in vivo
4-((E)-azobenzene)-beta-D-glucoside
-
4-((Z)-azobenzene)-beta-D-glucoside
-
4-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)butanoic acid
-
-
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
4-Cresol
-
5 mM, 67% inhibition
4-hydroxy-3-methoxybenzoic acid
-
-
4-nitrophenol
-
5 mM, 56% inhibition, enhances inhibition by glucose, glucose-6-phosphate and ATP
4-oxo-4-[(pyrazolo[4,3-b]olean-12-en-28-yl)oxy]butanoic acid
-
-
4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose
-
-
4-[(4-methyl-3-oxo-3,4-dihydroquinoxalin-2-yl)amino]-N-(2-thienylmethyl)benzamide
-
50% inhibition at 0.00014 mM in glycogenolysis assay, no bioavailability in vivo
4-[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfonyl]butanoic acid
-
-
5-(beta-D-glucopyranosyl)-3-(2-naphthyl)-1,2,4-oxadiazole
-
-
5-(beta-D-glucopyranosyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
-
-
5-chloro-N-(1,3,6,6-tetrafluoro-(R)-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
docking study. Hydrophobic residues, such as Phe53, Pro188, and Gly186, around the two aliphatic fluorine atoms suggest that the lipophilic contact among them is an important driver of activity increases. Hydrophobic residues Leu39 and Lys191 are close to one of the aromatic fluorine atoms
5-chloro-N-(1,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(1-hydroxy-2,3-dihydro-1H-inden-5-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-1H-indole-2-carboxamide
-
50% inhibition at 0.044 microM
5-chloro-N-(3,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(6,6-difluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-1H-indole-2-carboxamide
-
50% inhibition at 0.017 microM
5-chloro-N-[2-chloro-4-(1,2-dihydroxyethyl)-phenyl]-1H-indole-2-carboxamide
-
5-chloro-N-[4-(1,2-dihydroxyethyl)-3-(trifluoromethyl)phenyl]-1H-indole-2-carboxamide
-
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
5-chloro-N-[4-(2-hydroxyethyl)phenyl]-1H-indole-2-carboxamide
-
5-chloro-N-[5-(1,2-dihydroxyethyl)pyrazin-2-yl]-1H-indole-2-carboxamide
-
5-chloro-N-[5-(1,2-dihydroxyethyl)pyridin-2-yl]-1H-indole-2-carboxamide
-
6-(butylamino)hexyl (3beta)-3-hydroxyolean-12-en-28-oate
-
-
6-aminohexyl (3beta)-3-hydroxyolean-12-en-28-oate
-
-
6-[(4-methylphenyl)amino]hexyl (3beta)-3-hydroxyolean-12-en-28-oate
-
-
6-[4-(methyl 2,3,4-tri-O-benzyl-alpha-D-glucopyranosiduronylmethyl)-1H-1,2,3-triazol-1-yl]hexyl 3beta-hydroxyolean-12-en-28-oate
-
acarbose
-
poor inhibition
acetate
weak inhibition of wild-type activity, no effect on the activity of the H334G mutant
alpha-cyclodextrin
-
mixed-type competitive inhibition, inhibitor is not bound into the enzyme crystal
alpha-cyclodextrin dialdehyde I
-
alpha-cyclodextrin dialdehyde II
-
5 mM, 50% inhibition after 30 min
-
alpha-D-Glucopyranose-1,2-cyclic phosphate
-
competitive vs. glucose 1-phosphate
alpha-D-glucopyranosyl fluoride
alpha-D-glucose
-
physiological inhibitor
alpha-D-glucose 6-phosphate
-
binds at the allosteric site
alpha-D-glucose-1-methylenephosphonate
alpha-D-glucose-methylenephosphonate
-
competitive inhibitor
alpha-methylglucoside
-
-
aniline
-
5 mM, 50% inhibition
Antibodies to skeletal muscle phosphorylase
-
heart enzyme
-
Antiserum of purified phosphorylase
-
-
-
azide
weak inhibition of wild-type activity
baicalein
-
50% inhibition of phosphorylated, active enzyme at 0.0112 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0102 mM
BAY U6751
-
inhibits Pa-catalyzed As(V) reduction, glucose enhances inhibitory effect of the inhibitor on As(V) reduction, AMP at high concentration alleviates the inhibition
benzyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
benzyl (2beta)-2-hydroxyurs-12-en-28-oate
-
-
benzyl (2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oate
-
-
benzyl (2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oate
-
-
benzyl (2beta,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-hydroxy-3-oxoolean-12-en-28-oate
-
50% inhibition at 0.029 mM
benzyl (2Z)-2-(hydroxyimino)olean-12-en-28-oate
-
-
benzyl (2Z)-2-(hydroxyimino)urs-12-en-28-oate
-
-
benzyl (2Z,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-[[(2,4-dichlorobenzyl)oxy]imino]-3-oxoolean-12-en-28-oate
-
50% inhibition at 0.008 mM
benzyl (3beta)-3-[(pyridinium-1-ylacetyl)oxy]olean-12-en-28-oate chloride
-
-
benzyl (3beta)-3-[([4-[(4-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl]phenoxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
-
-
benzyl (3beta)-3-[([4-[(dodecanoyloxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
-
-
benzyl (3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oate
-
-
benzyl (3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oate
-
-
benzyl (3beta,12beta,13xi)-3,12-dihydroxyoleanan-28-oate
-
-
benzyl (5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-hydroxy-3-oxooleana-1,12-dien-28-oate
-
50% inhibition at 0.030 mM
benzyl 1'-(2,4-dichlorobenzyl)pyrazolo[4,3-b]olean-12-en-28-oate
-
-
benzyl 1'-(carboxymethyl)pyrazolo[4,3-b]olean-12-en-28-oate
-
-
benzyl 1'-benzylpyrazolo[4,3-b]olean-12-en-28-oate
-
-
benzyl 1'-methylpyrazolo[4,3-b]olean-12-en-28-oate
-
-
benzyl 1'-[(ethoxycarbonyl)methyl]pyrazolo[4,3-b]olean-12-en-28-oate
-
-
benzyl 2-oxoolean-12-en-28-oate
-
-
benzyl 2-oxours-12-en-28-oate
-
-
benzyl 3-O-propargyl-3beta-hydroxyolean-12-en-28-oate
-
benzyl 3beta-(2-(diethylamino)acetoxy)olean-12-en-28-oate
-
-
benzyl 3beta-(2-azidoacetoxy)olean-12-en-28-oate
-
-
benzyl 3beta-(2-chloroacetoxy)olean-12-en-28-oate
-
-
benzyl 3beta-(4-aminobenzoyloxy)olean-12-en-28-oate
-
-
benzyl 3beta-(4-nitrobenzoyloxy)olean-12-en-28-oate
-
-
benzyl pyrazolo[4,3-b]olean-12-en-28-oate
-
-
beta-cyclodextrin
-
mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide
-
competitive
beta-D-glucopyranosyl 1-(ethoxy(oxo)acetyl)-amide
-
competitive
beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide
-
competitive
beta-D-glucopyranosyl 1-oxalylamide
-
competitive
beta-D-glucopyranosyl bismethoxyphosphoramidate
weak competitive inhibitor, binds at the catalytic site and induces conformational changes in the vicinity of the site, inhibition mechanism, overview
beta-O-trans-caffeoyl-morolic acid
-
-
bis(6-([(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy)hexyl) (2R)-2-hydroxybutanedioate
-
-
bredemolic acid
-
allosteric site inhibitor
butyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
cAMP
-
5 mM, weak inhibition
cyanidin
-
50% inhibition of phosphorylated, active enzyme at 0.003 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.009 mM
Cyclodextrin-dialdehyde
-
cyclohexaamylose
Gracilaria sordida
-
-
cysteine
-
1 mM, 86% inhibition
D-Fructose 1-phosphate
-
-
D-fructose 6-phosphate
-
strong inhibition
D-gluconic acid 1,5-lactone
-
-
D-glucono-delta-lactone
-
0.05 mM, 90% inhibition of glucan phosphorolysis
D-glucose 6-phosphate
-
-
D-mannose 1-phosphate
-
strong inhibition
delphinidin
-
50% inhibition of phosphorylated, active enzyme at 0.0031 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0107 mM
deoxypyridoxine
-
weak inhibition of phosphorylase I, not II
diethyldicarbonate
-
0.84 mM, 50% inhibition
diethyldithiocarbamate
-
1 mM, 94% inhibition
dithiothreitol
-
1 mM, 56% inhibition
DL-phenylalanine
-
1 mM, 33% inhibition of phosphorylase B
DL-tryptophan
-
1 mM, 41% inhibition of phosphorylase B
EGTA
-
i.e. ethylene glycol bis(beta-aminoethylether)-N,N'-tetraacetic acid, 1 mM, 53% inhibition
epicatechin gallate
-
50% inhibition of phosphorylated, active enzyme at 0.0125 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.050 mM
epigallocatechin-3-gallate
-
50% inhibition of phosphorylated, active enzyme at 0.0077 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0339 mM
ethyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
formate
5fold reduction of wild-type activity, no effect on the activity of the H334G mutant
FR258900
the inhibitor binds at the allosteric activator site, where the physiological activator AMP binds. The contacts from FR258900 to glycogen phosphorylase are dominated by nonpolar van der Waals interactions with Gln71, Gln72, Phe196, and Val459 (from the symmetry-related subunit), and also by ionic interactions from the carboxylate groups to the three arginine residues (Arg242, Arg309, and Arg310) that form the allosteric phosphate-recognition subsite. The binding of FR258900 to the protein promotes conformational changes that stabilize an inactive T-state quaternary conformation of the enzyme
gamma-cyclodextrin
-
mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity
glucopyranosylidene spirohydantoin
-
most effective glucose analogue inhibitor for glycogen phosphorylase b
glucopyranosylidene spirothiohydantoin
-
muscle and liver phosphorylase b, strong competitive inhibition vs. phosphate and glycogen
glucose
-
above 5 mM, diminishes GPa-catalyzed As(V) reduction
glucose 2-phosphate
-
weak
guanidine hydrochloride
-
study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation
hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyl) (3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate)
-
-
high salt concentration
-
-
-
hydrogencarbonate
-
weak inhibition
imidazole
weak inhibition of wild-type enzyme
iminobis[ethane-2,1-diylimino(3beta)-28-oxoolean-12-ene-28,3-diyl]diacetate
-
-
KCl
-
80 mM, 50% loss of activity, 200 mM, 90% loss of activity
maslinic acid 5-bromopentyl ester
-
50% inhibition at 0.007 mM
maslinic acid-(2-piperidin-1-yl)ethyl ester
-
50% inhibition at 0.031 mM
methyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](4-hydroxyphenyl)ethanoate
-
-
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](phenyl)ethanoate
-
-
methyl 6-deoxy-6-[4-([[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]methyl)-1H-1,2,3-triazol-1-yl]-alpha-D-glucopyranoside
-
-
methyl [3-([(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino)-2-oxo-3,4-dihydroquinolin-1(2H)-yl]acetate
-
50% inhibition at 0.084 microM
Mg-ATP
-
reversible by AMP
molybdate
-
5 mM, more than 50% inhibition of glucan phosphorolysis
N-(1-phenyl-1H-1,2,3-triazole-4-carbonyl)-beta-D-glucopyranosylamine
-
N-(3-carboxypropanoyl)-beta-D-glucopyranosylamine
-
-
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
N-(3-phenyl-1,2-oxazole-5-carbonyl)-beta-D-glucopyranosylamine
-
N-(acetylcarbamoyl)-beta-D-glucopyranosylamine
-
-
N-(azidoacetyl)-beta-D-glucopyranosylamine
-
-
N-(benzoylcarbamoyl)-beta-D-glucopyranosylamine
N-(beta-D-glucopyranosyl)-3-(napht-1-yl)-1,2,4-oxadiazol-5-carboxamide
-
N-(beta-D-glucopyranosyl)-3-phenyl-1,2,4-oxadiazol-5-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(napht-1-yl)-1,3,4-oxadiazole-2-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(naphth-1-yl)-1,2,4-oxadiazol-3-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(naphth-2-yl)-1,3,4-oxadiazole-2-carboxamide
-
N-(beta-D-glucopyranosyl)-5-phenyl-1,2,4-oxadiazol-3-carboxamide
-
N-(beta-D-glucopyranosyl)-5-phenyl-1,3,4-oxadiazole-2-carboxamide
-
N-(dimethoxyphosphoryl)-beta-D-glucopyranosylamine
-
-
N-(naphthalen-2-ylcarbonyl)-beta-D-glucopyranosylamine
-
-
N-(naphthalene-1-carbonyl)-beta-D-glucopyranosylamine
-
N-(naphthalene-2-carbonyl)-beta-D-glucopyranosylamine
-
N-(trifluoroacetyl)-beta-D-glucopyranosylamine
-
-
N-([(2E)-2-[4-(trifluoromethyl)benzylidene]hydrazinyl]carbonothioyl)-beta-D-glucopyranosylamine
-
-
N-([4-[(benzyloxy)carbonyl]benzoyl]carbamoyl)-beta-D-glucopyranosylamine
-
-
N-acetyl-beta-D-glucopyranosylamine
-
-
N-Acetylimidazole
-
glucose 1-phosphate prevents
N-benzoyl-beta-D-glucopyranosylamine
-
N-benzyl-2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]acetamide
-
-
N-carbamoyl-beta-D-glucopyranosylamine
-
-
N-phenyl-beta-D-glucopyranosylamine
-
-
N-[(2E)-3-(5,6,7,8-tetrahydronaphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-(naphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-([1,1'-biphenyl]-4-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-[4-(propan-2-yl)phenyl]prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2R)-2-methyl-3-[4-(propan-2-yl)phenyl]propanoyl]-beta-D-glucopyranosylamine
-
N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-norleucine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
N-[(3S)-3-(4-ethylphenyl)butanoyl]-beta-D-glucopyranosylamine
-
N-[(4-aminobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-carboxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-chlorobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-hydroxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-methoxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-methylbenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(4-nitrobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[(biphenyl-4-ylcarbonyl)carbamoyl]-beta-D-glucopyranosylamine
-
-
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
N-[1-(naphthalen-1-yl)-1H-1,2,3-triazole-4-carbonyl]-beta-D-glucopyranosylamine
-
N-[3-(naphthalen-1-yl)-1,2-oxazole-5-carbonyl]-beta-D-glucopyranosylamine
-
N-[methoxy(oxo)acetyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(2-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(2-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-fluorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-methoxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-methylbenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(pyridin-4-ylmethylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[([1,1'-biphenyl]-4-yl)oxy]acetyl]-beta-D-glucopyranosylamine
-
N-[[4-(methoxycarbonyl)benzoyl]carbamoyl]-beta-D-glucopyranosylamine
-
-
N1-(2,4-dinitrophenyl)-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-carbamoyl-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-ethoxycarbonyl-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
-
NaAsO2
-
competitive inhibitor with respect to phosphate
NADPH
-
also oxidized form, less effective than nucleotide sugars, not NAD(H)
NaF
-
200 mM, complete inhibition
NaNO3
-
strong inhibition
NEM
-
inhibits GPa-catalyzed As(V) reduction
O-(1-methylcyclopentyl)-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
-
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-serine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
oleanolic acid 3-O-[(2E)-3-(4-chlorophenyl)acrylic acid] ester
-
50% inhibition at 0.0033 mM
oleanolic acid 3-O-[(2E)-3-(4-methoxyphenyl)acrylic acid] ester
-
50% inhibition at 0.0169 mM
oleanonic acid
-
50% inhibition at 0.0179 mM
oleanonic acid 2,3-oxadiazole
-
50% inhibition at 0.0112 mM
oleanonic acid 3-oxime
-
50% inhibition at 0.0208 mM
oxygen
-
activity in undialyzed cell extracts
p-chloromercuribenzene sulfonate
-
inhibits GPa-catalyzed As(V) reduction
p-chloromercuriphenylsulfonic acid
-
1 mM, 88% inhibition of stromal phosphorylase
pelargonidin
-
50% inhibition of phosphorylated, active enzyme at 0.0436 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0062 mM
peonidin
-
50% inhibition of phosphorylated, active enzyme at 0.0251 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0176 mM
phenol
-
5 mM, 45% inhibition
Phenylglyoxal
-
12 mM, 50% inhibition
phosphoenol pyruvate
slight inhibition
Phosphorylase phosphatase
-
proline
-
concentrations of 0.1 M have a slight accelerating effect on thermal aggregation of glycogen phosphorylase b. The suppression aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule
prop-2-en-1-yl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
propyl (2beta)-2-hydroxyolean-12-en-28-oate
-
-
pyrazolo[4,3-b]olean-12-en-28-oic acid
-
-
pyridine 3-aldehyde
-
weak inhibition of phosphorylase I, not II
pyridine 4-aldehyde
-
inhibition of phosphorylase I, not II
pyridoxal
-
phosphorylase I, not II
pyridoxal 5'-phosphate
-
74 and 76% inhibition of phosphorylase II and I respectively
pyridoxamine
-
weak inhibition of phosphorylase I, not II
pyridoxamine 5'-phosphate
-
weak inhibition of phosphorylase I, not II
quercetagetin
-
noncompetitive
resorcinol
-
1 mM, 50% inhibition of phosphorylase A and B, 23% inhibition of phosphorylase C
riboflavin
inhibition of the liver enzyme, counteracted by AMP
sodium dodecylsulfate
-
-
Tannic acid
-
0.005 mg, complete inhibition of phosphorylase B, 63% and 50% inhibition of phosphorylase A and C respectively
TDPglucose
-
competitive inhibition
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
uric acid
inhibition of the liver enzyme, counteracted by AMP
vanadate
-
5 mM, more than 50% inhibition of glucan phosphorolysis
[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]acetic acid
-
-
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
[1-(6-[4-[(acetyloxy)methyl]-1H-1,2,3-triazol-1-yl]hexyl)-1H-1,2,3-triazol-4-yl]methyl (3b)-3-hydroxyolean-12-en-28-oate
-
-
[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfanyl]acetic acid
-
-
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
i.e. AVE9423. Inhibitor fully exploits the volume of the binding pocket and show pronounced binding entropy
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
-
-
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
-
i.e. CP-403700, 50% inhibition at 0.1 microM in presence of 1 mM phosphate. In presence of 1 mM phosphate plus 8 mM glucose, 50% inhibition at 0.05 microM. Presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
-
i.e. CP-403700, indole-site inhibitor, suppression of hepatic glycogenolysis
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
i.e. AVE2865. Inhibitor fully exploits the volume of the binding pocket and show pronounced binding entropy
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
-
-
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
i.e. AVE5688, binding to enzyme is exclusively enthalpic
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
-
-
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
crystallization data
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
-
inhibitor shows oral hypoglycemic activity in diabetic db/db mice
ADP
-
1.6 mM, 50% inhibition of starch phosphorolysis, 0.23 mM, 50% inhibition of starch synthesis, allosteric inhibition, kinetics
ADP
-
5 mM, 8% inhibition of glucan phosphorolysis
ADP
-
at physiological levels diminishes GPa-catalyzed As(V) reduction
ADP-glucose
maximal inhibition achieved is 70%; maximal inhibition achieved is 95%
ADP-glucose
-
strong inhibition
ADP-glucose
2fold inhibition at 4 mM
ADPglucose
-
-
ADPglucose
-
competitive inhibition
ADPglucose
-
competitive inhibition
ADPglucose
-
strong inhibition
ADPglucose
Gracilaria sordida
-
-
ADPglucose
-
reversible by Mg2+
ADPglucose
-
4 mM, 60% inhibition of chloroplast phosphorylase
ADPglucose
-
1.3 mM, 50% inhibition of phosphorylase II, glucan phosphorolysis; strong inhibition of phosphorolysis, isozyme I
ADPglucose
-
weak inhibition
ADPglucose
-
5 mM, 30% inhibition
ADPglucose
-
2.5 mM, 80% inhibition of stromal phosphorylase
Ag+
-
strong inhibition
Ag+
-
2 mM, 78% inhibition
Ag+
-
1 mM, complete inhibition
alpha-cyclodextrin dialdehyde I
-
5 mM, 50% inhibition after 131 min
-
alpha-cyclodextrin dialdehyde I
-
0.4 mM, 50% inhibition after 15 min, 1.6 mM, 50% inhibition after 4.7 min
-
alpha-D-glucopyranosyl fluoride
-
strong inhibition of phosphorylase b, kinetics; weak inhibition
alpha-D-glucopyranosyl fluoride
-
weak inhibition
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
AMP
-
1-20 mM, weak inhibition
AMP
-
reversible by Mg2+; weak
AMP
-
10 mM, 55% inhibition, competitive to glucose 1-phosphate
AMP
-
yeast or potato enzyme
AMP
-
yeast or potato enzyme
aromatic amino acid
-
-
aromatic amino acid
-
inhibition of phosphorylase B, not A or C
arsenate
-
-
ATP
-
2.9 mM, 50% inhibition of starch phosphorolysis, 1.4 mM, 50% inhibition of starch synthesis
ATP
-
less effective than nucleotide sugars
ATP
-
5 mM, 10% inhibition of glucan phosphorolysis
ATP
-
1 mM, 20% inhibition of phosphorylase B, 5 mM, 90% inhibition; phosphorylase A or C are not inhibited
ATP
-
1 mM, 50% inhibition, at non-saturating levels of glucose 1-phosphate; additive inhibition together with tyrosine
ATP
-
rabbit muscle enzyme
ATP
-
complete inhibition of heart phosphorylase IIIb
ATP
-
at physiological levels diminishes GPa-catalyzed As(V) reduction
beta-amylase
-
noncompetitive vs. glucose 1-phosphate
-
Ca2+
-
weak
Ca2+
-
1 mM, stimulation at 10 mM
Caffeine
-
-
Caffeine
inhibition of the liver enzyme, counteracted by AMP
Caffeine
-
5 mM, complete inhibition of phosphorylase b, strong inhibition of phosphorylases ab and a
Caffeine
-
strong inhibition of muscle enzyme
Caffeine
-
5 mM, 95% inhibition of heart phosphorylase Ib in the presence of 1 mM AMP, 30% inhibition of heart phosphorylase IIb
CH3Hg+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA, about 80% inhibition at 0.03 mM
CH3Hg+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
chrysin
-
50% inhibition of phosphorylated, active enzyme above 0.0275 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0153 mM
Co2+
-
Co2+
-
1 mM, no inhibition at 10 mM
CP-316819
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP-316819
-
indole-site inhibitor, oral administration to diabetic ob/ob mice results in lowering of plasma glucose concentration by 40% at 50 mg per kg. Measured drug concentration in the liver is about 100fold higher than the in vitro IC50 values
CP-316819
-
indole-site inhibitor, suppression of hepatic glycogenolysis
CP-320626
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP-320626
-
indole-site inhibitor, suppression of hepatic glycogenolysis
CP-380867
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP-380867
-
indole-site inhibitor, suppression of hepatic glycogenolysis
CP320626
-
hypoglycaemic drug, potent inhibitor of liver and muscle glycogen phosphorylase a
CP320626
-
inhibits Pa-catalyzed As(V) reduction, glucose enhances inhibitory effect of the inhibitor on As(V) reduction, AMP at high concentration alleviated the inhibition
Cu2+
-
1 mM, strong inhibition
Cu2+
-
2 mM, 73% inhibition
Cu2+
-
10 mM, complete inhibition
Cu2+
-
4 mM, more than 50% inhibition
Cu2+
-
2 mM, 98% inhibition
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; weak inhibition
-
cyclodextrin
-
alpha- or beta-, not gamma-cyclodextrin; i.e. structure analogue of alpha-1,4-linked starch molecule
-
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; weak inhibition
-
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; strong inhibition
-
Cyclodextrin-dialdehyde
-
-
-
Cyclodextrin-dialdehyde
-
-
-
Cyclodextrin-dialdehyde
-
-
-
D-glucose
-
50 mM, 30% inhibition of glucan phosphorolysis
D-glucose
-
non-competitive
D-glucose
liver GPa is inhibited by glucose
D-glucose
-
5 mM and 8.5 mM, 50% inhibition of phosphorylase ab at 8 mM and 16 mM glucose 1-phosphate, 23 mM and 40 mM, 50% inhibition of phosphorylase a
D-glucose
physiological inhibitor
D-glucose
-
1 mM, significant inhibition of kidney dephosphophosphorylase
DTNB
-
-
EDTA
-
slight activation
EDTA
-
10 mM, 88% inhibition
EDTA
-
1 mM, 61% inhibition
ellagic acid
-
50% inhibition of phosphorylated, active enzyme at 0.0032 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0121 mM
ellagic acid
competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. Ellagic acid functions with glucose in a strongly synergistic mode. Determination of crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes, overview
Fe2+
-
weak inhibition
Fe2+
-
2 mM, 73% inhibition
Fe2+
-
10 mM, stimulation at 1 mM
Fe2+
-
1 mM, approx. 40% inhibition of synthesis
Fe2+
-
2 mM, 60% inhibition in the presence of 1 mM AMP
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
-
fructose 6-phosphate
-
-
fructose 6-phosphate
-
weak
gallic acid
-
-
gallic acid
competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP
GDPglucose
-
-
GDPglucose
-
0.05 mM, 50% inhibition, competitive inhibition of phosphorolysis
gluconolactone
-
-
gluconolactone
-
competitive inhibitor
glucose 1-phosphate
-
not inhibited
glucose 1-phosphate
-
kinetics
glucose 1-phosphate
-
above 2 mM; substrate inhibition
glucose 1-phosphate
-
completely reversible by 5'-AMP; kinetics
glucose 1-phosphate
-
not inhibited
glucose 6-phosphate
inhibits the phosphorylated and unphosphorylated enzyme forms. Binding of glucose 6-phosphate to the muscle isozyme is competitive with binding of AMP, but it also stabilizes a conformation that is more tense than the native T-state enzyme. Inhibition of muscle GPa enzyme activity by G6P is additive with inhibition by glucose
glucose 6-phosphate
-
complete inhibition of heart phosphorylase IIIb
glucose 6-phosphate
-
above 5 mM
glucose 6-phosphate
-
5 mM, 54% inhibition
glucose 6-phosphate
-
weak inhibition
guanine
-
-
Hg2+
-
0.1 mM, complete inhibition
Hg2+
-
1 mM, strong inhibition
Hg2+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA, about 90% inhibition at 0.0125 mM Hg2+, 80% at 0.01 mM
Hg2+
-
0.05 mM, 21% inhibition of phosphorylase A, 73% inhibition of phosphorylase
Hg2+
-
2 mM, complete inhibition
Hg2+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
Hg2+
-
4 mM, more than 50% inhibition
Hg2+
-
1 mM, complete inhibition
Hg2+
-
1 mM, 77% inhibition of stromal phosphorylase
iodoacetate
-
weak inhibition
iodoacetate
-
weak inhibition
L-tyrosine
-
noncompetitive inhibition
L-tyrosine
-
1 mM, 48% inhibition of phosphorylase B
L-tyrosine
-
additive inhibition together with ATP
luteolin
-
50% inhibition of phosphorylated, active enzyme at 0.0156 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0288 mM
mannose
-
weak inhibition
mannose
-
weak inhibition
maslinic acid
-
50% inhibition at 0.028 mM
Mg2+
-
-
Mn2+
-
strong inhibition at 1 mM
Mn2+
-
reaction without glucan primer
monohydroxyphenols
-
10 mM, 50, 40 and 65% inhibition of phosphorylases A, B and C
-
monohydroxyphenols
-
10 mM, no inhibition at 1 mM
-
N-(benzoylcarbamoyl)-beta-D-glucopyranosylamine
-
-
N-(benzoylcarbamoyl)-beta-D-glucopyranosylamine
-
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.135 microM
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
-
Na2SO4
-
50-300 mM, weak inhibition
NaHSO3
-
kinetics, completely reversible by dilution or dialysis
NaHSO3
-
kinetics, completely reversible by dilution or dialysis
oleanolic acid
-
-
oleanolic acid
-
50% inhibition at 0.014 mM
oleanolic acid
-
a naturally existing pentacyclic triterpene
p-chloromercuribenzoate
-
1 mM, 55% inhibition
p-chloromercuribenzoate
-
0.5 mM, 60% inhibition, reversible by 10 mM 2-mercaptoethanol
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
glucose 1-phosphate prevents
p-hydroxymercuribenzoate
-
2 mM, 96% inhibition
peroxynitrite
-
the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration
peroxynitrite
the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration
peroxynitrite
1 mM, almost complete inactivation. After the exposure to 1 mM peroxynitrite, the molar content of Cys residues decreases from 8.63 to 3.43 and 4.24 in the absence and in the presence of bicarbonate, respectively. The addition of 1 mM DTT in 10 min after peroxynitrite treatment does not significantly reverse loss of either activity or molar content of DTNB-reactive Cys residues. No involvement of Tyr613 nitration in the control of enzymatic function. The enzymatic activity does not directly correlate with the protein nitration levels
phosphate
-
1 mM
phosphate
Pho1 activity is strongly competitively inhibited by product phosphate in the synthesis reaction when amylopectin is the primer substrate, but this inhibition is less pronounced when short alpha-glucan chains are used as primers
Phosphorylase phosphatase
-
characterization
-
Phosphorylase phosphatase
-
reactivation by phosphorylase kinase
-
quercetin
-
50% inhibition of phosphorylated, active enzyme at 0.0048 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0209 mM
quercetin
-
inhibits Pa-catalyzed As(V) reduction, inhibition of As(V) reduction is not influenced by glucose or AMP
Sn2+
-
sulfate
-
-
UDP
-
at high glucose 1-phosphate concentration, glycogen synthesis, not phosphorolysis
UDP-glucose
-
-
UDP-glucose
-
strong inhibition
UDPglucose
-
competitive to glucose 1-phosphate, non-competitive to phosphate
UDPglucose
-
strong inhibition
UDPglucose
Gracilaria sordida
-
-
UDPglucose
-
weak inhibition
UDPglucose
-
1 mM, 43, 27 and 18% inhibition of phosphorylases A, B and C respectively
UDPglucose
-
10 mM, 44% inhibition at non-saturating levels of glucose 1-phosphate
UDPglucose
-
competitive to glucose 1-phosphate, non-competitive to phosphate
UDPglucose
-
strong inhibition; weak inhibition
UDPglucose
-
reversible by Mg2+
UDPglucose
-
2-3 mM, 50% inhibition of phosphorylase II, glucan phosphorolysis
UDPglucose
-
5 mM, 42% inhibition
UDPglucose
-
weak inhibition
UDPglucose
-
weak inhibition
Zn2+
-
0.1 mM, complete inhibition; strong inhibition
Zn2+
-
2 mM, complete inhibition
Zn2+
-
4 mM, more than 50% inhibition
Zn2+
-
2 mM, 63% inhibition in the presence of 1 mM AMP
Zn2+
Voandzeia subterranea
-
1 mM, 27% inhibition
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
-
competitive vs. glucose 1-phosphate
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
-
competitive vs. glucose 1-phosphate
additional information
-
activity is decreased in hyposmotic media
-
additional information
-
not inhibited by glucose
-
additional information
-
not inhibited by GMP; not inhibited by TMP; not inhibited by UMP, CMP, CTP
-
additional information
-
not inhibited by maltose, maltotriose, maltotetraose
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by acetate, acetylphosphate, butyrylphosphate, 6-phosphogluconate; not inhibited by fructose 6-phosphate
-
additional information
-
not inhibited by cyclodextrin
-
additional information
-
maltohexaose causes negligible substrate inhibition with Ki of 360 mM
-
additional information
-
not inhibited by aromatic compounds
-
additional information
-
not inhibited by K+, Na+
-
additional information
-
not inhibited by Mg2+ and Mn2+
-
additional information
-
-
-
additional information
-
the more active phosphorylated form of the enzyme, glycogen phosphorylase a, is a homodimer having an inhibitory allosteric binding site at the dimer interface for which synthetic ligands
-
additional information
-
muscle enzyme is not inhibited by beta-amylose
-
additional information
-
muscle enzyme is not inhibited by beta-amylose
-
additional information
-
not inhibited by AMP
-
additional information
-
-
-
additional information
molecular and kinetic mechanisms of enzyme inhibition by mercury, overview
-
additional information
-
not inhibited by 2-mercaptoethanol; not inhibited by non-aromatic amino acids; not inhibited by p-coumaric acid, caffeic acid or cinnamic acid
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by adenosine, cytosine; not inhibited by F-, ClO4-; not inhibited by fructose 6-phosphate; not inhibited by GMP; not inhibited by non-aromatic amino acids; not inhibited by succinate, 2-oxoglutarate, malate
-
additional information
-
-
-
additional information
-
-
-
additional information
-
binding and inhibition mechanism, no inhibition by (2,3,6-tri-O-methyl)-gamma-cyclodextrin
-
additional information
-
preference for hydrophobic group at C-28 of maslinic acid for enzyme inhibition
-
additional information
pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
-
additional information
-
pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
-
additional information
-
inhibitor screening, native ligand docking of inhibitor tautomers supplemented by QM/MM calculations, modeling of free state ligands and bound ligands, detailed overview
-
additional information
-
inhibitory efficiency and inhibition kinetics of beta-D-glucopyranosyl-thiosemicarbazone derivatives as glycogen phosphorylase inhibitors, binding analysis, overview
-
additional information
-
N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase, synthesis and evaluation by kinetic and crystallographic data, NMR structure analysis, molecular docking and modelling, overview. N-(trifluoroacetyl)-alpha-D-glucopyranosylamine and N-(trifluoroacetyl)-alpha-D-glucopyranosylamine are not inhibitory
-
additional information
-
the purine inhibitory site binds purine derivatives as well as pentacyclic triterpenes. Synthesis and inhibitory potencies of triazole-linked oleanolic acid dimers as enzyme inhibitors, overview. No inhibition by hexane-1,6-diyl(3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate) and dibenzyl (3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oate
-
additional information
-
evaluation of pentacyclic triterpenes as a class of inhibitors against glycogen phosphorylase, by receptor-based comparative molecular field analysis, and comparative molecular similarity analysis to investigate the quantitative structure-activity relationships of 106 compounds, detailed overview
-
additional information
-
synthesis of glucopyranonucleosides in the 5-alkynyl- and 6-alkylfurano[2,3-d]pyrimidine series, overview
-
additional information
-
synthesis of C-glucosylated spiro-sulfamide enzyme inhibitors via nucleophilic displacement of 1-O-tosyl or 1-deoxy-1-iodo-alpha-D-gluco-hept-2-ulopyranose tetra-O-benzylated derivative using aryl amines, followed by the formation of the corresponding cyclic sulfamide, overview
-
additional information
synthesis, enzyme kinetics and computational evaluation of N-(beta-D-glucopyranosyl) oxadiazolecarboxamides as glycogen phosphorylase inhibitors, overview. The compounds have promising oral drug-like properties without any toxicity. No inhibition by N-(beta-D-glucopyranosyl)-5-(naphth-2-yl)-1,2,4-oxadiazol-3-carboxamide, N-(beta-D-glucopyranosyl)-3-(napht-2-yl)-1,2,4-oxadiazol-5-carboxamide, N-[3-(naphthalen-2-yl)-1,2-oxazole-5-carbonyl]-beta-D-glucopyranosylamine, and N-[1-(naphthalen-2-yl)-1H-1,2,3-triazole-4-carbonyl]-beta-D-glucopyranosylamine
-
additional information
structure-based inhibitor design targeting glycogen phosphorylase b, virtual screening, synthesis, biochemical and biological assessment of N-acyl-beta-D-glucopyranosylamines, overview. In silico screening of 1888 N-acyl-beta-D-glucopyranosylamines putative enzyme inhibitors differing only in their R groups. Docking study for ligand binding affinities of the active sites and selection of six compounds and analysis of the inhibitory potency both in vitro and ex vivo
-
additional information
synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
-
additional information
-
synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
-
additional information
synthesis and evolution of C-glucopyranosyl-1,2,4-triazol-5-ones as inhibitors of glycogen phosphorylase, overview. No inhibition by 3-(beta-D-glucopyranosyl)-1-tosyl-1H-1,2,4-triazol-5(4H)-one and N1-(tert-butoxycarbonyl)-N2-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
-
additional information
-
synthesis and evolution of C-glucopyranosyl-1,2,4-triazol-5-ones as inhibitors of glycogen phosphorylase, overview. No inhibition by 3-(beta-D-glucopyranosyl)-1-tosyl-1H-1,2,4-triazol-5(4H)-one and N1-(tert-butoxycarbonyl)-N2-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
-
additional information
molecular and kinetic mechanisms of enzyme inhibition by mercury, overview
-
additional information
computationally motivated synthesis, using N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)-tetrazole-5-carboxamide as starting material, and enzyme kinetic evaluation of N-(beta-D-glucopyranosyl)-1,2,4-triazolecarboxamides as glycogen phosphorylase inhibitors, overview. No inhibition by 3b and 4b. Ki values are calculated from the IC50 values by the ChengPrusoff equation: Ki = IC50/(1 + [S]/Km). Comparison of the relative energies of different tautomers and conformations of the 1,2,4-triazole for models of the N-(beta-D-glucopyranosyl)-1,2,4-triazolecarboxamides, quantum mechanics/molecular mechanics calculations and modeling. No inhibition by 3b and 4b
-
additional information
-
no or poor inhibition by ribose 5-phosphate, glucose 6-phosphate, fructose-1,6-bisphosphate, ADP and UDP
-
additional information
-
not inhibited by 1,10-phenanthroline
-
additional information
-
not inhibited by fructose 6-phosphate; not inhibited by fructose, sucrose, dihydroxyacetone phosphate, 6-phosphogluconate, 2-phosphoglycollate, 2-phosphoglycerate, pyruvate
-
additional information
-
not inhibited by fructose 6-phosphate
-
additional information
structure-based inhibitor design targeting glycogen phosphorylase b, virtual screening, synthesis, biochemical and biological assessment of N-acyl-beta-D-glucopyranosylamines, overview. Determination of the effects of the enzyme inhibitors on conversion of glycogen phosphorylase a to b
-
additional information
slight inhibition by azobenzene glucosides. After irradiation and subsequent conversion to the (Z)-form, the inhibitory potency of the azobenzene glucoside does not significantly change for the rat muscle enzyme form. The anomeric ratio of alpha:beta form is approximately 1:4
-
additional information
-
not inhibited by IMP
-
additional information
-
not inhibited by glucose
-
additional information
-
not inhibited by glucose-6-phosphate
-
additional information
-
not inhibited by 2-mercaptoethanol; not inhibited by agarose; not inhibited by gibberellic acid, indolyl-3-acetic acid; not inhibited by Ni2+
-
additional information
-
not inhibited by azide
-
additional information
-
not inhibited by 2-mercaptoethanol; not inhibited by Sr2+
-
additional information
-
-
-
additional information
-
not inhibited by fructose 6-phosphate; not inhibited by GMP; not inhibited by GTP; not inhibited by UMP, CMP, CTP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.1 - 0.26
alpha-D-Glucan
0.054 - 22
alpha-D-glucose 1-phosphate
0.0046 - 0.03
amylopectin
22.7
arsenate
-
maltohexaose arsenolysis
0.33 - 0.96
D-glucose-1-phosphate
0.0418
Dextrin
-
pH 5.5, 37°C, synthesis reaction
1.22
dextrin DP9
-
phosphorolysis
0.05 - 20
glucose 1-phosphate
1 - 3.4
Glucose-1-phosphate
0.27 - 4.32
glycogen DP14
0.49
KF
-
glycogen synthesis
0.21 - 0.5
maltodecaheptaose
0.08 - 39.86
maltoheptaose
1.44
maltose
-
pH 6.2, 37°C, synthetic direction, wild-type enzyme
0.0106 - 0.15
soluble starch
-
0.47
starch DP24
-
synthesis
-
additional information
additional information
-
0.1
alpha-D-Glucan
-
-
0.054
alpha-D-glucose 1-phosphate
-
pH 6.8, 50°C, synthesis reaction
0.41
alpha-D-glucose 1-phosphate
pH 7.0, 30°C
0.68
alpha-D-glucose 1-phosphate
pH 7.0, 30°C
0.85
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, recombinant wild-type enzyme, synthesis
1.1
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, recombinant mutant H334Q, synthesis
1.2
alpha-D-glucose 1-phosphate
-
synthesis reaction, cosubstrate: maltotetraose, pH 6.5, 70°C
1.3
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, recombinant mutant H334N, synthesis
1.8
alpha-D-glucose 1-phosphate
-
pH 7.0, 30°C, recombinant mutant H334A, synthesis
2.1
alpha-D-glucose 1-phosphate
-
pH 5.5, 37°C, synthesis reaction
2.2
alpha-D-glucose 1-phosphate
-
-
2.78
alpha-D-glucose 1-phosphate
Voandzeia subterranea
-
in the presence of 5 mM AMP
3.5
alpha-D-glucose 1-phosphate
-
phosphorylase a
7.14
alpha-D-glucose 1-phosphate
Voandzeia subterranea
-
in the presence of 0.5 mM AMP
15
alpha-D-glucose 1-phosphate
-
phosphorylase b, pH 6.3
22
alpha-D-glucose 1-phosphate
-
phosphorylase b, pH 6.8
0.00003
AMP
-
phosphorylase a
0.007
AMP
-
phosphorylase ab
0.074
AMP
-
phosphorylase b
0.1
AMP
-
phosphorylase b
0.125
AMP
-
glycogen synthesis, in the presence of NaF
0.25
AMP
-
glycogen synthesis
0.27
AMP
-
phosphorylase b
1.11
AMP
Voandzeia subterranea
-
in the presence of 10 mM glucose 1-phosphate
2.7
AMP
Voandzeia subterranea
-
in the presence of 2 mM glucose 1-phosphate
0.0046
amylopectin
-
pH 5.5, 37°C, synthesis reaction
0.017
amylopectin
-
stromal phosphorylase, synthesis
0.028
amylopectin
-
stromal phosphorylase, phosphorolysis
0.03
amylopectin
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
0.03
amylopectin
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.71
amylose
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
1.1
amylose
-
fast isoenzyme, amylose phosphorolysis
3.01
amylose
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
3.1
amylose
-
slow isoenzyme, amylose phosphorolysis
14.3
amylose
-
slow isoenzyme, amylose synthesis
20
amylose
-
fast isoenzyme, amylose synthesis
0.33
D-glucose-1-phosphate
-
mutant T706I, 37°C, pH 5.5
0.48
D-glucose-1-phosphate
-
mutant F39L/N135S/T706I, 37°C, pH 5.5
0.56
D-glucose-1-phosphate
-
mutant N135S/T706I, 37°C, pH 5.5
0.57
D-glucose-1-phosphate
-
wild-type, 37°C, pH 5.5
0.59
D-glucose-1-phosphate
-
mutant N135S, 37°C, pH 5.5
0.62
D-glucose-1-phosphate
-
mutant F39L/N135S, 37°C, pH 5.5
0.76
D-glucose-1-phosphate
-
mutant F39L/T706I, 37°C, pH 5.5
0.96
D-glucose-1-phosphate
-
mutant F39L, 37°C, pH 5.5
0.5
dextrin DP11
-
phosphorolysis
46.48
dextrin DP11
-
synthesis
0.73
dextrin DP14
-
pH 7.2, 50°C, degradation reaction
1.2
dextrin DP14
-
pH 6.8, 50°C, synthesis reaction
0.39
dextrin DP19
-
pH 7.2, 50°C, degradation reaction
1.9
dextrin DP19
-
pH 6.8, 50°C, synthesis reaction
1.8
dextrin DP4
-
pH 7.2, 50°C, degradation reaction
17.1
dextrin DP4
-
pH 6.8, 50°C, synthesis reaction
0.05
glucose 1-phosphate
-
glucan synthesis
0.12
glucose 1-phosphate
-
glucan synthesis
0.4
glucose 1-phosphate
-
in the presence of Mg2+
0.55
glucose 1-phosphate
-
glucan synthesis
0.66
glucose 1-phosphate
-
starch synthesis
0.72
glucose 1-phosphate
-
chloroplast phosphorylase
0.86
glucose 1-phosphate
-
-
0.92
glucose 1-phosphate
-
cytoplasmic phosphorylase
0.96
glucose 1-phosphate
-
synthesis at pH 7.2
1
glucose 1-phosphate
-
-
1
glucose 1-phosphate
-
synthesis
1.04
glucose 1-phosphate
-
dextrin DP11 synthesis
1.19
glucose 1-phosphate
-
at 3.1 mM starch
1.2
glucose 1-phosphate
-
-
1.2
glucose 1-phosphate
-
synthesis
1.25
glucose 1-phosphate
-
at 6.2 mM starch
1.3
glucose 1-phosphate
-
-
1.38
glucose 1-phosphate
-
at 18.6 mM starch
1.4
glucose 1-phosphate
-
starch synthesis, phosphorylase A
1.51
glucose 1-phosphate
-
stromal phosphorylase
1.6
glucose 1-phosphate
-
-
1.7
glucose 1-phosphate
-
phosphorylase a
1.8
glucose 1-phosphate
-
-
2.2
glucose 1-phosphate
-
maltose synthesis, phosphorylase A
2.7
glucose 1-phosphate
-
starch synthesis, phosphorylase C
2.9
glucose 1-phosphate
-
-
3.3
glucose 1-phosphate
-
starch synthesis, phosphorylase B
3.4
glucose 1-phosphate
-
glycogen synthesis
3.56
glucose 1-phosphate
-
phosphorylase a
4
glucose 1-phosphate
-
maltose synthesis, phosphorylase C
4
glucose 1-phosphate
-
phosphorylase I
5
glucose 1-phosphate
-
glycogen synthesis, phosphorylase A
5.5
glucose 1-phosphate
-
phosphorylase b
5.5
glucose 1-phosphate
-
phosphorylase II
6
glucose 1-phosphate
-
heart phosphorylase I and III
8.3
glucose 1-phosphate
-
-
16
glucose 1-phosphate
-
-
18
glucose 1-phosphate
-
phosphorylase ab
20
glucose 1-phosphate
-
phosphorylase ab
1
Glucose-1-phosphate
-
-
3.4
Glucose-1-phosphate
-
glycogen synthesis
0.0138
glycogen
-
pH 5.5, 37°C, synthesis reaction
0.04
glycogen
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
0.07
glycogen
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.1
glycogen
-
phosphorylase b
0.1
glycogen
-
phosphorolysis
0.15
glycogen
-
phosphorolysis
0.25
glycogen
-
stromal phosphorylase, synthesis
0.43
glycogen
-
phosphorylase a
0.5
glycogen
-
phosphorylase a and ab
0.55
glycogen
-
phosphorylase ab
0.62
glycogen
-
synthesis
0.67
glycogen
-
synthesis
0.94
glycogen
-
stromal phosphorylase, phosphorolysis
1.3
glycogen
-
fast isoenzyme, glycogen phosphorolysis
1.4
glycogen
-
kidney phosphophosphorylase
1.6
glycogen
-
pH 7.0, 30°C, recombinant wild-type enzyme and mutant H334A, phosphorolysis
1.7
glycogen
-
pH 7.0, 30°C, recombinant mutant H334Q, phosphorolysis
6.04
glycogen
-
phosphorylase b
6.5
glycogen
-
slow isoenzyme, glycogen phosphorolysis
16
glycogen
-
pH 7.0, 30°C, recombinant mutant H334N, phosphorolysis
22.2
glycogen
-
slow isoenzyme, glycogen synthesis
40
glycogen
-
fast isoenzyme, glycogen synthesis
0.27
glycogen DP14
-
phosphorolysis
4.32
glycogen DP14
-
synthesis
0.21
maltodecaheptaose
-
phosphorolysis
0.5
maltodecaheptaose
-
synthesis
0.08
maltoheptaose
-
stromal phosphorylase, synthesis
0.1
maltoheptaose
-
stromal phosphorylase, phosphorolysis
0.12
maltoheptaose
-
synthesis, isoenzyme P-2
0.18
maltoheptaose
-
synthesis, isoenzyme P-2
0.19
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.2
maltoheptaose
-
phosphorolysis
0.26
maltoheptaose
-
synthesis, isoenzyme P-1
0.38
maltoheptaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.59
maltoheptaose
-
synthesis, isoenzyme P-1
0.81
maltoheptaose
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
1.1
maltoheptaose
-
synthesis, isoenzyme P-1
1.22
maltoheptaose
-
phosphorolysis
1.7
maltoheptaose
-
phosphorolysis, at 30°C
1.7
maltoheptaose
-
degradation direction, cosubstrate: phosphate, pH 6.5, 30°C
2.2
maltoheptaose
-
synthesis
3.6
maltoheptaose
-
phosphorolysis, at 70°C
3.6
maltoheptaose
-
degradation direction, cosubstrate: phosphate, pH 6.5, 70°C
3.72
maltoheptaose
-
phosphorolysis
4.49
maltoheptaose
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
5.9
maltoheptaose
-
phosphorolysis
7.1
maltoheptaose
-
phosphorolysis
31
maltoheptaose
-
synthesis
33
maltoheptaose
-
synthesis
39.86
maltoheptaose
-
synthesis
0.16
maltohexaose
-
stromal phosphorylase, synthesis
0.18
maltohexaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.21
maltohexaose
-
stromal phosphorylase, phosphorolysis
0.3
maltohexaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.68
maltohexaose
-
phosphorolysis
2.5
maltohexaose
-
synthesis
2.65
maltohexaose
-
recombinant wild-type enzyme
3.15
maltohexaose
-
phosphorolysis
7.1
maltohexaose
-
phosphorolysis
8.3
maltohexaose
-
phosphorolysis
27
maltohexaose
-
synthesis
32
maltohexaose
-
synthesis
0.72
maltooctaose
-
phosphorolysis
2
maltooctaose
-
synthesis
2 - 8.3
maltooctaose
-
maltoheptaose, maltohexaose, maltopentaose, maltotetraose, synthesis
0.11
maltopentaose
-
-
0.17
maltopentaose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.23
maltopentaose
-
stromal phosphorylase, phosphorolysis
0.27
maltopentaose
-
stromal phosphorylase, synthesis
0.28
maltopentaose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.49
maltopentaose
-
synthesis, isoenzyme P-2
0.93
maltopentaose
-
phosphorolysis
1.7
maltopentaose
-
synthesis, isoenzyme P-1
2.73
maltopentaose
-
phosphorolysis
3
maltopentaose
-
synthesis
3.5
maltopentaose
-
pH 7.0, 30°C, recombinant mutant H334A, phosphorolysis
3.8
maltopentaose
-
pH 7.0, 30°C, recombinant wild-type enzyme, phosphorolysis
4.1
maltopentaose
-
pH 7.0, 30°C, recombinant mutant H334Q, phosphorolysis
8.8
maltopentaose
-
phosphorolysis
9.1
maltopentaose
-
phosphorolysis
38
maltopentaose
-
synthesis
42
maltopentaose
-
synthesis
103
maltopentaose
-
pH 7.0, 30°C, recombinant mutant H334N, phosphorolysis
0.28
maltotetraose
-
pH 6.2, 37°C, phosphorolytic direction, wild-type enzyme
0.3
maltotetraose
pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction
0.44
maltotetraose
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
0.478
maltotetraose
-
pH 6.2, 37°C, synthetic direction, wild-type enzyme
0.55
maltotetraose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
0.57
maltotetraose
-
stromal phosphorylase, synthesis
1.54
maltotetraose
-
mutant F39L/T706I, 37°C, pH 5.5
1.87
maltotetraose
-
mutant T706I, 37°C, pH 5.5
1.96
maltotetraose
-
mutant N135S, 37°C, pH 5.5
2
maltotetraose
-
mutant F39L, 37°C, pH 5.5
2
maltotetraose
-
mutant F39L/N135S, 37°C, pH 5.5
2.11
maltotetraose
-
wild-type, 37°C, pH 5.5
2.47
maltotetraose
-
mutant N135S/T706I, 37°C, pH 5.5
2.57
maltotetraose
-
mutant F39L/N135S/T706I, 37°C, pH 5.5
2.8
maltotetraose
-
phosphorolysis, at 30°C
2.8
maltotetraose
-
degradation direction, cosubstrate: phosphate, pH 6.5, 30°C
3.6
maltotetraose
-
synthesis
3.9
maltotetraose
-
phosphorolysis
4.8
maltotetraose
-
phosphorolysis, at 70°C
4.8
maltotetraose
-
degradation direction, cosubstrate: phosphate, pH 6.5, 70°C
8.3
maltotetraose
-
synthesis
12.7
maltotetraose
-
synthesis
12.7
maltotetraose
-
synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C
44
maltotetraose
-
synthesis
53
maltotetraose
-
synthesis
0.3
maltotriose
-
pH 6.2, 37°C, synthetic direction, mutant enzyme k308A
0.31
maltotriose
-
pH 6.2, 37°C, synthetic direction, wild-type enzyme
0.35
maltotriose
-
pH 6.2, 37°C, synthetic direction, mutant enzyme R303A
0.69
maltotriose
-
pH 6.2, 37°C, synthetic direction, mutant enzyme H185A
0.79
maltotriose
-
pH 6.2, 37°C, phosphorolytic direction, wild-type enzyme
0.88
maltotriose
-
synthesis, isoenzyme P-2
1.8
maltotriose
pH 6.5, 37°C, recombinant enzyme, synthesis reaction
13.4
maltotriose
-
synthesis
13.4
maltotriose
-
synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C
24.5
maltotriose
-
synthesis
70
maltotriose
80°C, pH 6.5, direction of glucose 1-phosphate synthesis
70
maltotriose
pH 6.8, 80°C
0.45
phosphate
-
phosphorolysis at pH 7.2
0.5
phosphate
-
phosphorolysis
0.9
phosphate
-
cytoplasmic phosphorylase, pH 7.0
1.15
phosphate
-
phosphorylase a
1.18
phosphate
-
dextrin DP9 phosphorolysis
1.2
phosphate
-
isoenzyme A
1.2
phosphate
-
chloroplast phosphorylase, pH 7.0
1.5
phosphate
-
isoenzyme b, in the presence of 3 mM 5'-AMP
1.5
phosphate
-
cytoplasmic phosphorylase, pH 8.0
1.5
phosphate
-
phosphorylase II
1.6
phosphate
pH 7.0, 30°C
1.8
phosphate
-
chloroplastphosphorylase, pH 8.0
1.9
phosphate
pH 7.0, 30°C
1.9
phosphate
-
phosphorylase I
1.9
phosphate
-
phosphorolysis, at 30°C
1.9
phosphate
-
degradation direction, cosubstrate: maltoheptaose, pH 6.5, 30°C
2.01
phosphate
-
phosphorylase a
2.2
phosphate
-
phosphorolysis of glucan
2.2
phosphate
-
phosphorolysis, at 70°C
2.2
phosphate
-
degradation direction, cosubstrate: maltoheptaose, pH 6.5, 70°C
2.26
phosphate
-
stromal phosphorylase
2.3
phosphate
-
kidney phosphophosphorylase, in the presence of 0.8 mg glycogen
2.4
phosphate
-
glucan phosphorolysis
2.6
phosphate
-
phosphorylase ab
2.6
phosphate
-
kidney phosphophosphorylase, in the presence of 0.4 mg glycogen
2.8
phosphate
-
kidney phosphophosphorylase, in the presence of 0.2 mg glycogen
2.9
phosphate
-
kidney phosphophosphorylase, in the presence of 0.1 mg glycogen
3.03
phosphate
-
phosphorylase ab
4
phosphate
-
70°C, pH 7.0
4.1
phosphate
-
chloroplast phosphorylase
5.3
phosphate
-
cytoplasmic phosphorylase
6
phosphate
-
recombinant wild-type enzyme
6.8
phosphate
-
pH 7.0, 30°C, recombinant wild-type enzyme, phosphorolysis
7.7
phosphate
-
pH 7.2, 50°C, degradation reaction
10.87
phosphate
-
starch phosphorolysis
11
phosphate
-
phosphorylase b
12
phosphate
-
pH 7.0, 30°C, recombinant mutants H334A and H334Q, phosphorolysis
13
phosphate
-
pH 7.0, 30°C, recombinant mutant H334N, phosphorolysis
17.89
phosphate
-
phosphorylase b
20
phosphate
-
isozyme ab
20
phosphate
-
glycogen, dephospho-phosphorylase
20
phosphate
-
phosphorylase b
20
phosphate
-
phosphorolysis of oyster glycogen
25
phosphate
-
phosphorolysis of corn dextrin
28
phosphate
-
phosphorylase ab
30
phosphate
-
kidney dephosphophosphorylase, in the presence of 1.6 mg glycogen
31
phosphate
80°C, pH 6.5
31
phosphate
pH 6.8, 80°C
55
phosphate
-
isoenzyme b, in the absence of 5'-AMP
70
phosphate
-
kidney dephosphophosphorylase, in the presence of 0.8 mg glycogen
100
phosphate
-
dephospho-phosphorylase
100
phosphate
-
kidney dephosphophosphorylase, in the presence of 0.2 mg glycogen
0.0106
soluble starch
-
pH 5.5, 37°C, synthesis reaction
-
0.0261
soluble starch
-
pH 5.5, 37°C, synthesis reaction
-
0.1
soluble starch
pH 7.5, 37°C, synthesis reaction, cytosolic isozyme
-
0.15
soluble starch
pH 7.5, 30°C, degradation reaction, cytosolic isozyme
-
0.013
starch
-
pH 6.2, 37°C, phosphorolytic direction, wild-type enzyme
0.04
starch
-
phosphorolysis
0.045
starch
-
pH 6.2, 37°C, synthetic direction, wild-type enzyme
0.23
starch
-
pH 7.0, 30°C, recombinant wild-type enzyme, phosphorolysis
0.25
starch
-
pH 7.0, 30°C, recombinant mutant H334A, phosphorolysis
0.3
starch
-
pH 7.2, 50°C, degradation reaction
0.32
starch
-
pH 7.0, 30°C, recombinant mutant H334Q, phosphorolysis
0.5
starch
-
fast isoenzyme, starch phosphorolysis
0.8
starch
-
slow isoenzyme, starch phosphorolysis
1
starch
-
pH 7.0, 30°C, recombinant mutant H334N, phosphorolysis
1.5
starch
-
pH 6.8, 50°C, synthesis reaction
4.4
starch
-
at 0.5 mM glucose 1-phosphate
5.6
starch
-
at 1.0 mM glucose 1-phosphate
6.7
starch
-
slow isoenzyme, starch synthesis
8
starch
-
fast isoenzyme, starch synthesis
15.5
starch
-
at 5 mM glucose 1-phosphate
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
Voandzeia subterranea
-
kinetic data
-
additional information
additional information
Indocibium guttattam
-
kinetic data
-
additional information
additional information
-
kinetic mechanism
-
additional information
additional information
-
kinetic parameters of 3 starch phosphorylases
-
additional information
additional information
-
1.21 mg/ml, starch, phosphorylase C
-
additional information
additional information
-
0.46% glycogen, with AMP, 0.67% glycogen, without AMP
-
additional information
additional information
-
1.26 mg/ml, glycogen
-
additional information
additional information
-
1.1 mg/ml, glycogen, phosphorylase A
-
additional information
additional information
-
20 mg/ml, oyster glycogen, phosphorolysis, 25 mg/ml, endogen glycogen, synthesis, 27 mg/ml, corn dextrin, phosphorolysis, 40 mg/ml, corn dextrin, synthesis
-
additional information
additional information
-
12 mg/ml maltodextrin
-
additional information
additional information
-
1.3 mg/ml, maltodextrin
-
additional information
additional information
-
amylopectin, 0.69 mg/ml and 0.68 mg/ml for phosphorolysis and synthesis, respectively
-
additional information
additional information
-
2.7 mg/ml, glycogen, isozyme a
-
additional information
additional information
-
42 mg/ml, oyster glycogen, synthesis
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
Gracilaria sordida
-
0.264 mg/ml, amylopectin, 0.277 mg/ml, glycogen, 0.285 mg/ml, amylose, 0.453 mg/ml, maltodextrin
-
additional information
additional information
-
0.36 mg/ml, glycogen
-
additional information
additional information
-
0.13 mg/ml, starch phosphorolysis
-
additional information
additional information
-
0.65 mg/ml, glycogen
-
additional information
additional information
-
0.24 mg/ml starch, phosphorylase A
-
additional information
additional information
-
0.19 mg/ml, starch synthesis
-
additional information
additional information
-
4.2 mg/ml, glycogen, isozyme b
-
additional information
additional information
-
0.13 mg/ml amylopectin, 0.45 mg/ml glycogen
-
additional information
additional information
-
5 mg/ml, oyster glycogen
-
additional information
additional information
kinetics, forward and reverse reaction, recombinant enzyme
-
additional information
additional information
-
stopped-flow and steady-state kinetics, wild-type and mutant enzymes
-
additional information
additional information
-
allosteric kinetics, overview
-
additional information
additional information
an allosteric enzyme existing as two interconvertible forms: phosphorylase a (active type) and phosphorylase b (inactive type)
-
additional information
additional information
-
an allosteric enzyme existing as two interconvertible forms: phosphorylase a (active type) and phosphorylase b (inactive type)
-
additional information
additional information
when maltohexaose is used as the substrate, typical Michaelis-Menten curves ar obtained
-
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0.000018 - 0.0015
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
0.00004 - 0.0012
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
0.000057
(2-[[(5-chloro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
(2-[[(5-chloro-1H-pyrrolo[2,3-c]pyridin-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000076
(2-[[(5-chloro-6-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000052
(2-[[(5-chloro-7-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00016
(2-[[(5-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0161
(2alpha)-3-hydroxyolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0133
(2alpha,3beta)-2,3-bis(acetyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0252
(2alpha,3beta)-2,3-bis(butanoyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0105
(2alpha,3beta)-2,3-bis(propanoyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0206
(2beta)-2-hydroxyurs-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0227
(2beta)-3-hydroxyolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00625
(2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0011
(2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000026 - 0.00043
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
0.000012 - 0.00045
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
0.000043 - 0.00042
(2E,2'E)-N,N'-butane-1,4-diylbis[3-(3,4-dichlorophenyl)-acrylamide]
0.000023 - 0.00026
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
0.00001
(2R)-2-cyclohexyl-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]propanoic acid
Homo sapiens
-
-
0.000009
(2S)-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]heptanoic acid
Homo sapiens
-
0.000006
(2S)-cyclohexyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
Homo sapiens
-
-
0.000014
(2S)-cyclopentyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
Homo sapiens
-
-
0.0131
(2Z)-2-(hydroxyimino)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0147
(2Z)-2-(hydroxyimino)urs-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00325
(3beta)-28-[(2-[[2-(acetylamino)ethyl]amino]ethyl)amino]-28-oxoolean-12-en-3-yl acetate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0152
(3beta)-28-[(3-aminopropyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
Oryctolagus cuniculus
-
-
0.0035
(3beta)-28-[(6-aminohexyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
Oryctolagus cuniculus
-
-
0.0309
(3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0102
(3beta)-N-(6-aminohexyl)-3,23-dihydroxylup-20(29)-en-28-amide
Oryctolagus cuniculus
-
-
0.0031
(3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00259 - 0.0026
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
0.0251
(4aS,6aS,6bR,8aR,14aR,14bR,16bS)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinoxaline-4a(2H)-carboxylic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.014
(6aS,6bR,8aR,16aR,16bR,18bS)-2,2,6a,6b,9,9,16a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,16,16a,16b,17,18b-hexadecahydrochryseno[1,2-b]phenazine-4a(2H)-carboxylic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0493
1'-(methylsulfonyl)pyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0538
1'-acetylpyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0372
1'-propanoylpyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000044 - 0.000059
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
0.026
1-(beta-D-glucopyranosyl)-4-hydroxymethyl-1,2,3-triazole
Oryctolagus cuniculus
-
-
0.036
1-(beta-D-glucopyranosyl)-4-phenyl-1,2,3-triazole
Oryctolagus cuniculus
-
-
0.000014 - 0.000024
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
0.0123
1-[6-(acetyloxy)hexyl] 4-(7-[[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]heptyl) (2R)-2-hydroxybutanedioate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000014
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclodecanecarboxylic acid
Homo sapiens
-
-
0.000005
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclooctanecarboxylic acid
Homo sapiens
-
-
0.0191
2,2',2''-tris[(2E)-4-hydroxybut-2-en-1-yl] 1,1',1''-(3b,5x,9x,13x,18x)-lup-20(29)-ene-3,23,28-triyl triethanedioate
Oryctolagus cuniculus
-
-
0.0186
2,3,4,6-tetra-O-acetyl-1-O-[(2alpha,3beta)-2,3-dihydroxy-28-oxoolean-12-en-28-yl]-beta-D-glucopyranose
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000017 - 0.00017
2-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)-4-methoxybutanoic acid
0.0256
2-(phenylamino)ethyl (3beta)-3-hydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0077
2-amino-3,4-dihydroxy-5-methoxybenzoic acid
Homo sapiens
-
-
0.00895
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
Oryctolagus cuniculus
-
0.0309
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.0239
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.00268
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.00987
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.0254
2-bromoethyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.01025
2-bromoethyl (3beta)-3-hydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0225
2-ethoxy-2-oxoethyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.029
2-oxours-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00153
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (1S,2R,4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-1,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00223
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-2,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0063
2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]-N-(3'',4''-dichlorobenzyl)acetamide
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0011
2beta,3alpha-dihydroxyurs-12-en-28-oic acid
Oryctolagus cuniculus
-
-
0.000056
3-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.08
3-(beta-D-glucopyranosyl)-1-(2-naphthyl)-1H-1,2,4-triazol-5(4H)-one
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.35
3-(beta-D-glucopyranosyl)-1-phenyl-1H-1,2,4-triazol-5(4H)-one
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.26
3-methoxypterolactone
Homo sapiens
-
-
0.00114
3-O-[1-(methyl 6-deoxy-alpha-D-glucopyranosid-6-yl)-1H-1,2,3-triazol-4-yl]methyl 3b-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
pH 6.0, 37°C
0.000056
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)amino]-3-oxopropanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000059
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
1.6
4-((E)-azobenzene)-beta-D-glucoside
Rattus norvegicus
untreated enzyme, pH 7.0, 30°C
0.032
4-((Z)-azobenzene)-beta-D-glucoside
Rattus norvegicus
enzyme after irradiation and subsequent conversion to the (Z)-form, pH 7.0, 30°C
0.000054
4-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)butanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00043 - 0.000915
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
0.091
4-hydroxy-3-methoxybenzoic acid
Homo sapiens
-
-
0.0247
4-oxo-4-[(pyrazolo[4,3-b]olean-12-en-28-yl)oxy]butanoic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000042
4-[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfonyl]butanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
5-chloro-N-(1,3,6,6-tetrafluoro-(R)-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000048
5-chloro-N-(1,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00044
5-chloro-N-(1-hydroxy-2,3-dihydro-1H-inden-5-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000063
5-chloro-N-(3,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00032
5-chloro-N-(5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000068
5-chloro-N-(6,6-difluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00042
5-chloro-N-[2-chloro-4-(1,2-dihydroxyethyl)-phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00034
5-chloro-N-[4-(1,2-dihydroxyethyl)-3-(trifluoromethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.0009
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.0012
5-chloro-N-[4-(2-hydroxyethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00044
5-chloro-N-[5-(1,2-dihydroxyethyl)pyrazin-2-yl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00025
5-chloro-N-[5-(1,2-dihydroxyethyl)pyridin-2-yl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.0126
6-(butylamino)hexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0141
6-aminohexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0116
6-hydroxyluteolin
Rattus norvegicus
-
pH 6.8, 25°C
0.0281
6-[(4-methylphenyl)amino]hexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0116
6-[4-(methyl 2,3,4-tri-O-benzyl-alpha-D-glucopyranosiduronylmethyl)-1H-1,2,3-triazol-1-yl]hexyl 3beta-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
pH 6.0, 37°C
0.037
alpha-boswellic acid
Homo sapiens
-
-
0.0042
benzyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0223
benzyl (2beta)-2-hydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00669
benzyl (2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00125
benzyl (2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0163
benzyl (2Z)-2-(hydroxyimino)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0202
benzyl (2Z)-2-(hydroxyimino)urs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00539
benzyl (3beta)-3-[(pyridinium-1-ylacetyl)oxy]olean-12-en-28-oate chloride
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0175
benzyl (3beta)-3-[([4-[(4-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl]phenoxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0078
benzyl (3beta)-3-[([4-[(dodecanoyloxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0277
benzyl (3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0065
benzyl (3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00535
benzyl (3beta,12beta,13xi)-3,12-dihydroxyoleanan-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.132
benzyl 1'-(2,4-dichlorobenzyl)pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.057
benzyl 1'-(carboxymethyl)pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.063
benzyl 1'-benzylpyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0999
benzyl 1'-methylpyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.111
benzyl 1'-[(ethoxycarbonyl)methyl]pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0032
benzyl 2-oxoolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0242
benzyl 2-oxours-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0265
benzyl 3-O-propargyl-3beta-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
pH 6.0, 37°C
0.0201
benzyl 3beta-(2-(diethylamino)acetoxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0127
benzyl 3beta-(2-azidoacetoxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0126
benzyl 3beta-(2-chloroacetoxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00213
benzyl 3beta-(4-aminobenzoyloxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0161
benzyl 3beta-(4-nitrobenzoyloxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0456
benzyl pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.047
beta-amyrin
Homo sapiens
-
-
0.06
beta-amyrone
Homo sapiens
-
-
0.026
beta-boswellic acid
Homo sapiens
-
-
0.044
beta-O-trans-caffeoyl-morolic acid
Homo sapiens
-
-
0.0123
bis(6-([(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy)hexyl) (2R)-2-hydroxybutanedioate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00625
bredemolic acid
Oryctolagus cuniculus
-
-
0.0138
butyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00092
CP-320626
Homo sapiens
pH 6.8, 22C
0.0153
ethyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0003
FR258900
Oryctolagus cuniculus
-
0.0068
gallic acid
Homo sapiens
-
-
0.0207
hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyl) (3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate)
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0157
hypolaetin
Rattus norvegicus
-
pH 6.8, 25°C
0.00325
iminobis[ethane-2,1-diylimino(3beta)-28-oxoolean-12-ene-28,3-diyl]diacetate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0461
isoscullarein
Rattus norvegicus
-
pH 6.8, 25°C
0.0297
luteolin
Rattus norvegicus
-
pH 6.8, 25°C
0.0281
methyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0112
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](4-hydroxyphenyl)ethanoate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0239
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](phenyl)ethanoate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00114
methyl 6-deoxy-6-[4-([[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]methyl)-1H-1,2,3-triazol-1-yl]-alpha-D-glucopyranoside
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0125
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
Oryctolagus cuniculus
-
0.0187
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
Oryctolagus cuniculus
-
524.3
N-([(2E)-2-[4-(trifluoromethyl)benzylidene]hydrazinyl]carbonothioyl)-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
0.0342
N-benzyl-2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]acetamide
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000023
N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-norleucine
Homo sapiens
-
370
N-[[(2E)-2-(2-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
26.6
N-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
484.2
N-[[(2E)-2-(2-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
50.4
N-[[(2E)-2-(3-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
23.2
N-[[(2E)-2-(3-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
180
N-[[(2E)-2-(3-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
93.2
N-[[(2E)-2-(4-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
28.3
N-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
5.7
N-[[(2E)-2-(4-fluorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
340.5
N-[[(2E)-2-(4-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
406.5
N-[[(2E)-2-(4-methoxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
192.4
N-[[(2E)-2-(4-methylbenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
25.7
N-[[(2E)-2-(4-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
200
N-[[(2E)-2-(pyridin-4-ylmethylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
0.000006
O-(1-methylcyclopentyl)-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
Homo sapiens
-
0.000007
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
Homo sapiens
-
0.000044
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-serine
Homo sapiens
-
0.008 - 0.014
oleanolic acid
0.0231
prop-2-en-1-yl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0273
propyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.232
pterolactone
Homo sapiens
-
-
0.0099
pyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0097
quercetagetin
Rattus norvegicus
-
pH 6.8, 25°C
0.0335
quercetin
Rattus norvegicus
-
pH 6.8, 25°C
0.00003
[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0207
[1-(6-[4-[(acetyloxy)methyl]-1H-1,2,3-triazol-1-yl]hexyl)-1H-1,2,3-triazol-4-yl]methyl (3b)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00004
[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfanyl]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
additional information
additional information
Oryctolagus cuniculus
-
kinetics of inhibition of the forward reaction
-
0.000018
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0015
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0012
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000026
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C, presence of glucose
0.00043
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C
0.000012
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C, presence of glucose
0.00045
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C
0.000043
(2E,2'E)-N,N'-butane-1,4-diylbis[3-(3,4-dichlorophenyl)-acrylamide]
Homo sapiens
pH 6.8, 22°C, presence of glucose
0.00042
(2E,2'E)-N,N'-butane-1,4-diylbis[3-(3,4-dichlorophenyl)-acrylamide]
Homo sapiens
pH 6.8, 22°C
0.000023
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C, presence of glucose
0.00026
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
Homo sapiens
pH 6.8, 22°C
0.00259
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0026
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000044
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000059
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
0.000014
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000024
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
0.000017
2-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)-4-methoxybutanoic acid
Homo sapiens
-
The configuration of the asymmetric centre in the alpha-position of the carboxylic acid is not known. pH and temperature not specified in the publication
0.00017
2-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)-4-methoxybutanoic acid
Homo sapiens
-
The configuration of the asymmetric centre in the alpha-position of the carboxylic acid is not known. pH and temperature not specified in the publication
0.00043
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000915
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
0.0066
Caffeine
Homo sapiens
-
-
0.1023
Caffeine
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.114
Caffeine
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.114
Caffeine
Oryctolagus cuniculus
pH 7.2, 22°C
0.008
oleanolic acid
Homo sapiens
-
-
0.014
oleanolic acid
Oryctolagus cuniculus
-
-
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