Ligand ADP-glucose

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Basic Ligand Information

Molecular Structure
Picture of ADP-glucose (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C16H25N5O15P2
ADP-glucose
WFPZSXYXPSUOPY-ROYWQJLOSA-N
Synonyms:
ADP-alpha-D-glucose, ADP-D-glucose, ADP-Glc, ADPglucose


Show all pahtways known for Show all BRENDA pathways known for ADP-glucose

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
ADP-glucose + protein = ADP + alpha-D-glucosyl-protein
-
show the reaction diagram
ADP-glucose + D-fructose = ADP + sucrose
-
show the reaction diagram
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
-
show the reaction diagram
ADP-alpha-D-glucose + D-glucose = ADP + alpha,alpha-trehalose
-
show the reaction diagram
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate
-
show the reaction diagram
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
-
show the reaction diagram
ADP-glucose + H2O = AMP + alpha-D-glucose 1-phosphate
-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
ADP + sucrose = ADP-glucose + D-fructose
-

Substrate in Enzyme-catalyzed Reactions (85 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
ADP-glucose + protein = ADP + alpha-D-glucosyl-protein
-
show the reaction diagram
ADP-glucose + D-fructose 6-phosphate = ADP + sucrose 6-phosphate
-
show the reaction diagram
ADP-glucose + indoxyl = ADP + indican
-
show the reaction diagram
ADP-alpha-D-glucose + validoxylamine A = ADP + validamycin A
-
show the reaction diagram
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate
-
show the reaction diagram
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
-
show the reaction diagram
ADP-glucose + p-nitrophenol = ADP + p-nitrophenyl beta-D-glucoside
-
show the reaction diagram
ADP-glucose + glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
-
show the reaction diagram
ADP-alpha-D-glucose + 3-hydroxyflavone = ADP + 3-hydroxyflavone 3-O-beta-D-glucoside
-
show the reaction diagram
ADP-glucose + 7,8-dihydroxyflavone = ADP + 7-O-beta-D-glucosyl-7,8-dihydroxyflavone
-
show the reaction diagram
diphosphate + ADP-glucose = ATP + alpha-D-glucose 1-phosphate
show the reaction diagram
ADP-alpha-D-glucose + phosphate = ADP + alpha-D-glucose 1-phosphate
-
show the reaction diagram
ADP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + ADP
-
show the reaction diagram
ADP-glucose + H2O = ?
-
show the reaction diagram
ADP-glucose + H2O = IDP-glucose + NH3
-
show the reaction diagram
ADP-glucose + H2O = ?
-
show the reaction diagram
ADP-glucose + H2O = AMP + alpha-D-glucose 1-phosphate
-
show the reaction diagram
ADP-glucose + H2O = ?
-
show the reaction diagram
ADP-D-glucose = ?
-

Product in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (7 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (27 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
weak inhibition
-
strong inhibition
reversible by Mg2+
-
maximal inhibition achieved is 70%; maximal inhibition achieved is 95%
-
1.3 mM, 50% inhibition of phosphorylase II, glucan phosphorolysis; strong inhibition of phosphorolysis, isozyme I
-
2.5 mM, 80% inhibition of stromal phosphorylase
-
2fold inhibition at 4 mM
-
4 mM, 60% inhibition of chloroplast phosphorylase
-
5 mM, 30% inhibition
-
kinetics
-
competitive inhibition
-
competitive with UDPglucose
-
strong
-
competitive against UDP-N-acetyl-D-glucosamine
-
in the presence of 3-phosphoglycerate, ADP-glucose is a competitve inhibitor with respect to ATP
in wild-type, competitive with ATP, noncompetitive with glucose 1-phosphate. In chimeric mutant, competitive with ATP, mixed type inhibition with glucose 1-phosphate
competitive
-
0.5 mM, 77.8% of initial activity
-

3D Structure of Enzyme-Ligand-Complex (PDB) (4 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (22 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
at pH 7.0 and 37°C
1.7
-
at pH 7.5 and 30°C
2.9
-
at pH 7.5 and 37°C
9.8
-
at pH 8.0 and 37°C
isoform SUS1, at pH 8.0 and 30°C
2.7
-
isoform SUS2, at pH 8.0 and 30°C
2.2
-
pH 8.0, 30°C, at 10 mg/ml glycogen
333
-
pH 8.0, 30°C, at 10 mg/ml amylopectin
235
-
pH 6.0, 60°C
with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
20
-
with 1.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
29.2
-
with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
19.8
-
with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
15.4
-
with phloretin as cosubstrate, at pH 7.5 and 30°C
58.67
-
with quercetin as cosubstrate, at pH 7.5 and 30°C
14.57
-
pH and temperature not specified in the publication
29
-
37°C, wild-type large subunit
139
-
25°C, pH 7.6, wild-type enzyme
9.1
-
pH 6.0, 37°C
214
-
pH 4.5, 37°C
130
-

KM Value (133 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
4.3
-
80°C, pH 5.0
4.1
-
high-mobility isoform
11.5
-
low-mobility isoform
46.9
-
pH 7.5, 35°C
8
-
-
0.9
-
at pH 7.0 and 37°C
0.03
-
at pH 7.3 and 26°C
1.8
-
at pH 7.5 and 30°C
at pH 7.5 and 37°C
6.7
-
at pH 8.0 and 37°C
isoform SUS1, at pH 8.0 and 30°C
0.17
-
isoform SUS2, at pH 8.0 and 30°C
0.78
-
isoform SUS3, at pH 8.5 and 25°C
0.67
-
pH 7.0, 37°C, recombinant enzyme
0.033
-
pH 7.0, 60°C
0.044
-
pH 8.0, enzyme expressed in Escherichia coli
2.7
-
pH 8.0, enzyme expressed in Nicotiana tabacum
2
-
37°C, pH 5.5
0.6
-
25°C
45°C
assay in water or 85% isopropanol
2.5
-
at pH 7.8, temperature not specified in the publication
0.058
-
catalytic domain
0.28
-
catalytic domain co-expressed with starch-binding domain 2 and part of starch-binding domain 3
0.81
-
catalytic domain co-expressed with starch-binding domain 3 and large part of starch-binding domain 2
0.59
-
catalytic domain co-expressed with starch-binding domains 123
0.95
-
catalytic domain co-expressed with starch-binding domains 23
0.62
-
free isoform SSI, at pH 8.0 and 30°C
0.39
-
free isoform SSIIa, at pH 8.0 and 30°C
0.84
-
free isoform SSIII, at pH 8.0 and 30°C
0.33
-
glycogen synthases I and II
0.035
-
granule bound starch synthase I, 5 mg/ml amylopectin
1.3
-
granule-bound isoenzyme I
0.14
-
granule-bound isoenzyme I from waxy maize
0.09
-
granule-bound isoenzyme II
0.11
-
granule-bound isoenzyme II from waxy maize
0.05
-
isoenzyme I
0.2
-
isoenzyme I, primed reaction
0.17
-
isoenzyme II
0.29
-
isoenzyme II, primed reaction
0.11
-
isoenzyme III
0.15
-
isoenzyme III, primed reaction
0.22
-
isoenzyme IV
0.25
-
isoenzyme IV, primed reaction
0.2
-
isoform GBSSI, with maltobiose as cosubstrate, at pH 8.5 and 30°C
0.09
-
isoform SSI with maltotriose as cosubstrate, at pH 8.5 and 30°C
0.63
-
isoform SSIIIb, with maltotriose as cosubstrate, at pH 8.5 and 30°C
0.44
-
isoform SSIV, with maltotriose as cosubstrate, at pH 8.5 and 30°C
0.31
-
mutant enzyme K193E, amylopectin as primer
0.22
-
mutant enzyme K193E, glycogen as primer
0.17
-
mutant enzyme K193Q, amylopectin as primer
0.14
-
mutant enzyme K193Q, glycogen as primer
0.1
-
mutant enzyme K193R, amylopectin as primer
0.15
-
mutant enzyme K193R, glycogen as primer
0.15
-
pH 8.0, 30°C, at 10 mg/ml amylopectin
0.22
-
pH 8.0, 30°C,at 10 mg/ml glycogen
0.32
-
recombinant starch synthase IIa
0.11
-
recombinant starch synthase IIb
0.12
-
soluble isoenzymes
0.1
0.12
starch synthase I, absence of citrate
0.24
-
starch synthase I, presence of 500 mM citrate
0.18
-
starch synthase I, primer amylopectin
0.053
-
starch synthase I, primer amylopectin, 500 mM citrate
0.11
-
starch synthase II, 5 mg/ml amylopectin
0.07
-
starch synthase II, primer amylopectin, 500 mM citrate
0.3
-
synthase I, absence of citrate
0.29
-
synthase I, presence of citrate
0.97
-
synthase II, absence of citrate
0.48
-
synthase II, presence of citrate
0.51
-
truncated protein lacking starch binding domain 1 and large part of starch binding domain 2
1.68
-
truncated protein lacking starch binding domain 1 and medium part of starch binding domain 2
1.77
-
truncated protein lacking starch binding domain 1 and small part of starch binding domain 2
2.39
-
truncated protein lacking starch-binding domain 1
2.56
-
truncated protein lacking starch-binding domains 12
1.74
-
wild-type
4.08
-
wild-type enzyme, amylopectin as primer
0.11
-
wild-type enzyme, glycogen as primer
0.13
-
pH 8.0, 30°C
0.48
-
-
4.1
-
55°C, pH 6.5
2.7
-
enzyme monomer, pH not specified in the publication, temperature not specified in the publication
0.03
-
enzyme oligomer, pH not specified in the publication, temperature not specified in the publication
0.027
-
90°C, pH 6.5
1.14
-
pH 6.0, 60°C
recombinant enzyme, at 60°C
0.8
-
pH 7.5, 25°C
0.7
-
pH 7.5, 30°C
pH 7.5, 37°C
pH 6.5, 70°C
1.5
-
pH 6.7, 60°C, native enzyme
2.9
-
pH 6.7, 60°C, recombinant enzyme
9.3
-
pH 6.7, 70°C, native enzyme
2
-
with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.145
-
with 1.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.121
-
with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.063
-
with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.046
-
37°C, pH 5.5
0.6
-
with phloretin as cosubstrate, at pH 7.5 and 30°C
0.05867
-
with quercetin as cosubstrate, at pH 7.5 and 30°C
0.01457
-
pH and temperature not specified in the publication
0.44
-
-
0.24
-
pH 7.4, 37°C
0.62
-
pH 7.4, 37°C, mutant BT2-TI
0.33
-
pH 7.4, 37°C, mutant MP
0.11
-
pH 7.4, 37°C, mutant MP-TI
0.07
-
pH 7.4, 37°C, wild-type BT2
0.48
-
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L1 and small subunit S
0.45
-
pH 7.8, 37°C, heterotetramer comprised of large subunit isoform L3 and small subunit S
0.72
-
pH 7.8, 37°C, large subunit isoform L3
1.57
-
pH 8.0, 37°C
25°C, pH 7.6, wild-type enzyme
3.16
-
pH 7.5
0.167
-
AGPPase2
0.8
-
pH 4.5, 37°C
0.7
-
pH 6.0, 37°C
0.8
-

Ki Value (24 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
-
0.7
-
synthesis
0.033
-
presence of 1 mM orthophosphate, pH 7.0, 30°C
phosphorolysis
0.11
-
recombinant enzyme
0.75
-
wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
1.2
-
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.05
-
wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.09
-
wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.12
-
wild-type, substrate ATP, pH 7.4, 37°C
0.007
-
reduced wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.21
-
reduced wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.46
-
reduced wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.14
-
chimeric mutant, substrate ATP, pH 7.4, 37°C
oxidized wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.11
-
oxidized wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.11
-
oxidized wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.13
-
oxidized wild-type, substrate ATP, pH 7.4, 37°C
0.045
-
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.083
-
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.09
-

References & Links

Links to other databases for ADP-glucose

ChEBI
PubChem
-
PubChem