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ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
the enzyme is required for starch biosynthesis, while Tdy1 is not required, although tdy1-R mutant leaves retain large amounts of starch on prolonged dark treatment, consistent with a defect in starch catabolism, overview
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
substrate binding structure and kinetics, regulation of wild-type and mutant enzymes, mapping the polymorphic sites important in altered allosteric properties, overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
specific for ATP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
not: TTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate is UTP
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in seed starch biosynthesis
-
-
?
additional information
?
-
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms
-
-
?
additional information
?
-
-
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
AGPase, a key regulatory enzyme in starch biosynthesis, is highly regulated, effects of substrates, detailed overview
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
the enzyme is required for starch biosynthesis, while Tdy1 is not required, although tdy1-R mutant leaves retain large amounts of starch on prolonged dark treatment, consistent with a defect in starch catabolism, overview
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
one of the main regulatory steps in starch biosynthesis in plants
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis. The heat lability of maize endosperm AGPase contributes to yield loss caused by heat stress, overview
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in seed starch biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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1,6-Hexanediol bisphosphate
-
activation
2,3-diphosphoglycerate
-
no activation
2-keto-3-deoxy phosphogluconate
-
activation
2-oxobutyrate
-
slight activation, pyruvate analog
2-phospho-D-glycerate
-
no activation
ADP
-
activation, less effective than 3-phosphoglycerate
ADP-glucose
-
in the absence of 3-phosphoglycerate, ADP-glucose stimulates catalytic acitvity, acting as a feedback product activator
AMP
-
activation, less effective than 3-phosphoglycerate
D-fructose
-
25 mM, 1.3fold stimulation, enzyme from maize endosperm
D-fructose 1,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
no activation
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
dihydroxyacetone phosphate
-
activation, less effective than 3-phosphoglycerate
fructose 6-phosphate
activation constant Ka is 0.53 for maize enzyme and 0.15 for the chimeric enzyme
Fruf-beta-(2->1)-6-O-P-Glcp
-
-
glyceraldehyde 3-phosphate
Hydroxypyruvate
-
slight activation, pyruvate analog
phosphate
-
enhances AGPase activity al low substrate concentations
sedoheptulose 1,7-diphosphate
-
activation
3-phosphoglycerate
-
-
3-phosphoglycerate
-
allosteric activation
3-phosphoglycerate
-
activation
3-phosphoglycerate
-
pH-dependent
3-phosphoglycerate
-
the activities of recombinant maize and recombinant potato enzyme are comparable in the presence of 10 mM 3-phosphoglycerate, however in absence of 3-phosphoglycerate and phosphate the maize enzyme exhibits approximately 20fold more activity than does potato enzyme, in presence of both 3-phosphoglycerate and phosphate the maize enzyme is 47fold active than is the potato enzyme
3-phosphoglycerate
-
pH-dependent, endosperm
3-phosphoglycerate
-
strong
3-phosphoglycerate
-
10 mM, 16fold stimulation, enzyme from maize endosperm
3-phosphoglycerate
-
activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview
3-phosphoglycerate
in presence of 3-phosphoglycerate, enzyme follows a Theorell-Chance bi-bi mechanism with ATP binding first and ADP-Glc releasing last. 3-Phosphoglycerate increases the binding affinity for both substrates with little effect on velocity for the maize and chimeric maize/potato isoforms. Activation constant Ka is 0.06 for maize enzyme and 0.03 for the chimeric enzyme
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
allosteric activator
D-fructose 1,6-bisphosphate
-
no activation
D-fructose 6-phosphate
-
-
D-fructose 6-phosphate
-
activation
D-fructose 6-phosphate
-
allosteric activator
D-fructose 6-phosphate
-
less effective than 3-phosphoglycerate
D-fructose 6-phosphate
-
25 mM, 15fold stimulation, enzyme from maize endosperm
D-glucose 6-phosphate
-
activation
D-glucose 6-phosphate
-
allosteric activator
D-glucose 6-phosphate
-
less effective than 3-phosphoglycerate
D-glucose 6-phosphate
-
25 mM, 12fold stimulation, enzyme from maize endosperm
D-ribose 5-phosphate
-
activation
D-ribose 5-phosphate
-
less effective than 3-phosphoglycerate
D-ribose 5-phosphate
-
D-fructose 6-phosphate analog
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
-
no activation
phosphoenolpyruvate
-
-
phosphoenolpyruvate
-
activation
phosphoenolpyruvate
-
less effective than 3-phosphoglycerate
pyridoxal 5'-phosphate
-
activation
pyridoxal 5'-phosphate
-
allosteric activator
additional information
-
-
-
additional information
-
-
-
additional information
-
not: fructose 2,6-bisphosphate, Ca2+/calmodulin
-
additional information
-
mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator
-
additional information
-
no activation by D-6-phosphogluconic acid, ribose 1,5-diphosphate, erythrose 4-phosphate, or methyl phosphate at 20 mM
-
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0.05 - 0.09
alpha-D-glucose 1-phosphate
0.07 - 0.48
ADP-D-glucose
0.62
ADP-glucose
-
pH 7.4, 37°C
0.017 - 11.9
alpha-D-glucose 1-phosphate
additional information
additional information
-
0.05
alpha-D-glucose 1-phosphate
mutant BT2/E438Q
0.05
alpha-D-glucose 1-phosphate
mutant BT2/P372A
0.06
alpha-D-glucose 1-phosphate
mutant BT2/A508S
0.06
alpha-D-glucose 1-phosphate
mutant BT2/M172T
0.06
alpha-D-glucose 1-phosphate
mutant BT2/T361C
0.06
alpha-D-glucose 1-phosphate
mutant BT2/V227R
0.06
alpha-D-glucose 1-phosphate
mutant BT2/V502T
0.07
alpha-D-glucose 1-phosphate
mutant BT2/C114A
0.07
alpha-D-glucose 1-phosphate
mutant BT2/D368S
0.07
alpha-D-glucose 1-phosphate
mutant BT2/H149S
0.07
alpha-D-glucose 1-phosphate
mutant BT2/Q213H
0.07
alpha-D-glucose 1-phosphate
wild type BT2/SH2
0.08
alpha-D-glucose 1-phosphate
mutant BT2/C382F
0.09
alpha-D-glucose 1-phosphate
mutant BT2/C424V
0.09
alpha-D-glucose 1-phosphate
mutant BT2/S163F
0.09
ATP
mutant BT2/A508S
0.09
ATP
mutant BT2/M172T
0.11
ATP
mutant BT2/D368S
0.12
ATP
wild type BT2/SH2
0.13
ATP
mutant BT2/E438Q
0.13
ATP
mutant BT2/T361C
0.14
ATP
mutant BT2/C114A
0.14
ATP
mutant BT2/C424V
0.14
ATP
mutant BT2/V227R
0.15
ATP
mutant BT2/C382F
0.15
ATP
mutant BT2/V502T
0.19
ATP
mutant BT2/H149S
0.19
ATP
mutant BT2/P372A
0.21
ATP
mutant BT2/Q213H
0.42
ATP
mutant BT2/S163F
0.07
ADP-D-glucose
-
pH 7.4, 37°C, mutant MP-TI
0.11
ADP-D-glucose
-
pH 7.4, 37°C, mutant MP
0.33
ADP-D-glucose
-
pH 7.4, 37°C, mutant BT2-TI
0.48
ADP-D-glucose
-
pH 7.4, 37°C, wild-type BT2
0.017
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.038
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C
0.038
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.039
alpha-D-glucose 1-phosphate
wild-type, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.04
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant BT2-TI
0.04
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.05
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, wild-type BT2
0.06
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
0.06
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP-TI
0.06
alpha-D-glucose 1-phosphate
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.08
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP
0.19
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C
1.81
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C, presence of phosphate
2.8
alpha-D-glucose 1-phosphate
wild-type, 37°C, pH 7.4
2.8
alpha-D-glucose 1-phosphate
wild-type, pH 7.4, 37°C
6.79
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
6.8
alpha-D-glucose 1-phosphate
large subunit mutant D161G, 37°C, pH 7.4
8.74
alpha-D-glucose 1-phosphate
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
11.9
alpha-D-glucose 1-phosphate
chimeric enzyme, pH 7.4, 37°C
0.018
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in absence of 3-phosphoglycerate
0.039
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 430-475), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-429), in absence of 3-phosphoglycerate
0.04
ATP
-
pH 7.4, 37°C, mutant Mos(1-376), in absence of 3-phosphoglycerate
0.043
ATP
large subunit mutant D161G, 37°C, pH 7.4
0.044
ATP
-
pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate
0.044
ATP
large subunit mutant D161G, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.051
ATP
-
pH 7.4, 37°C, mutant Mos(1-198), in presence of 3-phosphoglycerate
0.053
ATP
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
0.057
ATP
large subunit mutant Q96G/D161G/A443R, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.069
ATP
wild-type, presence of 3-phosphoglycerate, 37°C, pH 7.4
0.074
ATP
-
pH 7.4, 37°C, wild-type enzyme, in presence of 3-phosphoglycerate
0.075
ATP
-
pH 7.4, 37°C, wild-type enzyme, in absence of 3-phosphoglycerate
0.1
ATP
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
0.11
ATP
-
pH 7.4, 37°C, wild-type BT2 and mutant MP-TI
0.11
ATP
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.12
ATP
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
0.13
ATP
-
pH 7.4, 37°C, mutant MP
0.13
ATP
-
small subunit mutant R107A
0.15
ATP
-
pH 7.4, 37°C, mutant BT2-TI
0.19
ATP
-
large subunit mutant R116A
0.26
ATP
-
large subunit mutant R381A
0.3
ATP
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
0.36
ATP
-
small subunit mutant R340A
0.42
ATP
-
large subunit mutant R146A
0.58
ATP
wild-type, pH 7.4, 37°C, presence of phosphate
0.9
ATP
chimeric enzyme, pH 7.4, 37°C
1.1
ATP
-
small subunit mutant R77K
1.4
ATP
-
large subunit mutant R104A
4
ATP
wild-type, 37°C, pH 7.4
4
ATP
wild-type, pH 7.4, 37°C
0.033
diphosphate
-
pH 7.4, 37°C
2.32
diphosphate
-
pH 7.4, 37°C, wild-type BT2
4.07
diphosphate
-
pH 7.4, 37°C, mutant BT2-TI
5.87
diphosphate
-
pH 7.4, 37°C, mutant MP-TI
6.61
diphosphate
-
pH 7.4, 37°C, mutant MP
additional information
additional information
-
-
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
comparison of Km of proteolyzed and non-proteolyzed enzyme at pH 7.4 and pH 6.8
-
additional information
additional information
-
KM-values for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
additional information
additional information
-
ordered kinetic mechanism, regulation of AGPase by effectors, detailed overview
-
additional information
additional information
-
recombinant wild-type and mutant AGPase kinetic and allosteric properties for the forward and reverse reaction directions, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
16.17 - 59.86
alpha-D-glucose 1-phosphate
26.21 - 85
alpha-D-glucose 1-phosphate
additional information
additional information
-
turnover numbers for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
16.17
alpha-D-glucose 1-phosphate
mutant BT2/V227R
23.34
alpha-D-glucose 1-phosphate
mutant BT2/D368S
29.36
alpha-D-glucose 1-phosphate
mutant BT2/Q213H
32.87
alpha-D-glucose 1-phosphate
mutant BT2/E438Q
34.65
alpha-D-glucose 1-phosphate
mutant BT2/S163F
35.21
alpha-D-glucose 1-phosphate
mutant BT2/H149S
35.77
alpha-D-glucose 1-phosphate
mutant BT2/A508S
37.21
alpha-D-glucose 1-phosphate
mutant BT2/C114A
38.12
alpha-D-glucose 1-phosphate
mutant BT2/T361C
38.58
alpha-D-glucose 1-phosphate
mutant BT2/M172T
39.17
alpha-D-glucose 1-phosphate
wild type BT2/SH2
40.75
alpha-D-glucose 1-phosphate
mutant BT2/C382F
41.91
alpha-D-glucose 1-phosphate
mutant BT2/V502T
42.32
alpha-D-glucose 1-phosphate
mutant BT2/P372A
59.86
alpha-D-glucose 1-phosphate
mutant BT2/C424V
26.21
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant BT2-TI
38.17
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, wild-type BT2
42.88
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP-TI
62.65
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, mutant MP
85
alpha-D-glucose 1-phosphate
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
2 - 3.7
ATP
wild-type, pH 7.4, 37°C, presence of phosphate
11
ATP
-
large subunit mutant R104A
11
ATP
-
large subunit mutant R146A
11
ATP
-
small subunit mutant R77K
16
ATP
-
small subunit mutant R340A
29.11
ATP
-
pH 7.4, 37°C, mutant BT2-TI
33
ATP
-
large subunit mutant R116A
35.2
ATP
wild-type, 37°C, pH 7.4
35.2
ATP
wild-type, pH 7.4, 37°C
42.6
ATP
wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
43.32
ATP
-
pH 7.4, 37°C, wild-type BT2
47.5
ATP
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
48.8
ATP
large subunit mutant D161G, 37°C, pH 7.4
49.03
ATP
-
pH 7.4, 37°C, mutant MP-TI
67.6
ATP
chimeric enzyme, pH 7.4, 37°C
69
ATP
-
large subunit mutant R381A
69.34
ATP
-
pH 7.4, 37°C, mutant MP
70
ATP
-
small subunit mutant R107A
70.6
ATP
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
72.4
ATP
large subunit mutant Q96G/D161G/A443R, 37°C, pH 7.4
98
ATP
-
pH 7.4, 37°C, enzyme from Zea mays endosperm
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.007 - 1.2
ADP-alpha-D-glucose
0.00038 - 0.9
diphosphate
1.83
phosphate
mutant BT2/S163F, 15 mM 3-phosphoglycerate
2.28
phosphate
mutant BT2/C382F, 15 mM 3-phosphoglycerate
3.21
phosphate
mutant BT2/Q213H, 15 mM 3-phosphoglycerate
3.72
phosphate
mutant BT2/P372A, 15 mM 3-phosphoglycerate
3.96
phosphate
mutant BT2/H149S, 15 mM 3-phosphoglycerate
4.26
phosphate
mutant BT2/D368S, 15 mM 3-phosphoglycerate
5.34
phosphate
mutant BT2/T361C, 15 mM 3-phosphoglycerate
13.23
phosphate
mutant BT2/C114A, 15 mM 3-phosphoglycerate
14.5
phosphate
mutant BT2/V227R, 15 mM 3-phosphoglycerate
15.22
phosphate
mutant BT2/E438Q, 15 mM 3-phosphoglycerate
16.8
phosphate
wild type BT2/SH2, 15 mM 3-phosphoglycerate
17.61
phosphate
mutant BT2/M172T, 15 mM 3-phosphoglycerate
17.93
phosphate
mutant BT2/V502T, 15 mM 3-phosphoglycerate
18.36
phosphate
mutant BT2/C424V, 15 mM 3-phosphoglycerate
20.43
phosphate
mutant BT2/A508S, 15 mM 3-phosphoglycerate
0.007
ADP-alpha-D-glucose
wild-type, substrate ATP, pH 7.4, 37°C
0.01
ADP-alpha-D-glucose
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.05
ADP-alpha-D-glucose
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.083
ADP-alpha-D-glucose
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.09
ADP-alpha-D-glucose
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.09
ADP-alpha-D-glucose
wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.12
ADP-alpha-D-glucose
wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
1.2
ADP-alpha-D-glucose
wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.00038
diphosphate
-
pH 7.4, 37°C
0.03
diphosphate
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.075
diphosphate
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.1
diphosphate
wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.11
diphosphate
wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.19
diphosphate
wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.36
diphosphate
chimeric mutant, substrate ATP, pH 7.4, 37°C
0.44
diphosphate
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.9
diphosphate
wild-type, substrate ATP, pH 7.4, 37°C
0.44
phosphate
-
pH 7.4, 37°C, in presence of 1 mM 3-phosphoglycerate
1
phosphate
-
the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phosphate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate
1.4
phosphate
-
wild-type enzyme, in presence of 3-phosphoglycerate
2.96
phosphate
-
pH 7.4, 37°C, enzyme from maize endosperm
8.7
phosphate
-
mutant Mos(1-198), in presence of 3-phosphoglycerate
9.8
phosphate
-
pH 7.4, 37°C, in presence of 10 mM 3-phosphoglycerate
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A508S
large subunit mutation
C114A
large subunit mutation
C382F
large subunit mutation
C424V
large subunit mutation
D368S
large subunit mutation
E438Q
large subunit mutation
H149S
large subunit mutation
M172T
large subunit mutation
P372A
large subunit mutation
Q213H
large subunit mutation
S163F
large subunit mutation
T361C
large subunit mutation
V227R
large subunit mutation
V502T
large subunit mutation
bt2-H2328
mutant, an insertion is located in exon 6 of the Bt2 gene generating a 9-bp duplication of bases TGATGTGAC, position 4,422 - 4,431, a comparative transcriptome analysis of wild-type and bt2-H2328 kernels at mid-development leads to the conclusion that the lack of Bt2-encoded AGPase triggers large-scale changes on the transcriptional level that concern mainly genes involved in carbohydrate or amino acid metabolic pathways
D161G
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme
F332S
-
site-directed mutagenesis in the potato part of the chimeric mutant
H333T
-
Sh2hs33, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 76% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2, enhanced subunit interaction in this mutant
H333T/T460I
-
Sh2hs40, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 72% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
H341Y
-
site-directed mutagenesis in the potato part of the chimeric mutant
I323V
-
site-directed mutagenesis in the potato part of the chimeric mutant
L38E
-
UpReg-1, this mutation greatly increases activation by 3-phosphoglycerate
L93Thr
-
Sh2-UR1, this mutation does not alter 3-phosphoglycerate activation and phosphate inhibition
N369H
-
site-directed mutagenesis in the potato part of the chimeric mutant
Q96G/D161G/A443R
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme. Mutant additionally shows an increase affinity for activator 3-phosphoglyceric acid
R104A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R104T
-
Sh2hs16, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 37% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R107A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R116A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R146A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R217P/H333T
-
Sh2hs47, coexpression with wild-type Brittle2: 5min 60°C heat treatment, about 65% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R340A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R381A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R77K
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
S34E/Y36C
-
significant increase in heat stability as compared to wild-type enzyme
S34Q/Y36C
-
significant increase in heat stability as compared to wild-type enzyme. The ratio of turnover-number to KM-value for ATP is 2.1fold higher than wild-type ratio, the ratio of turnover-number to KM-value for alpha-D-glucose 1-phosphate is 2.6fold higher than wild-type ratio
T462I
-
random mutagenesis, small subunit mutant BT2-TI, BT2-TI exhibits enhanced heat stability compared to wildtype maize endosperm AGPase
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
Y36C
-
significant increase in heat stability as compared to wild-type enzyme
additional information
-
mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber. Km for ATP and alpha-D-glucose 1-phosphate do not differ significantly for the mosaic enzymes in the presence of 3-phosphoglycerate. 2fold increase in Km for ATP when the potato small subunit is combined with the maize large subunit (Pss/Mls). Interestingly, the turnover number is increased for all mosaics
additional information
-
expression of maize Sh2r6hs transgene, a modified maize Sh2 cDNA coding sequence with alterations conferring reduced sensitivity to phosphate inhibition and greater heat stability, in Triticum aestivum results in increased photosynthetic rates under high light but not low light conditions, peaking at 7 days after flowering. Transgenic plants show increases in levels of fructose, glucose, and sucrose in flag leaves at 7 and 14 days after flowering
additional information
-
expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wild-type maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglycerate, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview
additional information
-
heat-stable small subunit variant MP is composed of sequences from the maize endosperm and the potato tuber small subunit, construction of a double mutant MP-TI, which may lead to increased starch yield when expressed in monocot endosperms
additional information
-
identification of a mutant allele of the leaf-expressed small subunit of ADP-glucose pyrophosphorylase agps-m1, the AGPase mutant is unable to synthesize transitory starch and lacks leaf starch, phenotype, overview
additional information
-
mutant Sh2r6hs, expressed in transgenic wheat plants, shows increases in ADP-glucose, UDP-glucose, and fructose at maturity , phenotype, overview
additional information
construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
additional information
-
construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
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Amir, J.; Cherry, J.H.
Purification and properties of adenosine diphosphoglucose pyrophosphorylase from sweet corn
Plant Physiol.
49
893-897
1972
Zea mays
brenda
Plaxton, W.C.; Preiss, J.
Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm
Plant Physiol.
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1987
Zea mays
brenda
Fuchs, R.L.; Smith, J.D.
The purification and characterization of ADP-glucose pyrophosphorylase A from developing maize seeds
Biochim. Biophys. Acta
566
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1979
Zea mays
brenda
Hannah, L.C.; Nelson, O.E.
Characterization of adenosine diphosphate glucose pyrophosphorylases from developing maize seeds
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55
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1975
Zea mays
brenda
Kleczkowski, L.A.; Villand, P.; Lnneborg, A.; Olsen O.A.; Lthi, E.
Plant ADP-glucose pyrophosphoylase - recent advances and biotechnological perspectives
Z. Naturforsch. C
46c
605-612
1991
Escherichia coli, Hordeum vulgare, Oryza sativa, Solanum tuberosum, Spinacia oleracea, Zea mays
-
brenda
Preiss, J.
Regulation of adenosine diphosphate glucose pyrophosphorylase
Adv. Enzymol. Relat. Areas Mol. Biol.
46
317-381
1978
Aeromonas caviae, Aeromonas hydrophila, Agrobacterium tumefaciens, Allochromatium vinosum, Arachis hypogaea, Auxenochlorella pyrenoidosa, Beta vulgaris, Cereibacter sphaeroides, Chlamydomonas reinhardtii, Chlorella vulgaris, Chlorobaculum thiosulfatiphilum, Citrobacter freundii, Clostridium pasteurianum, Daucus carota, Enterobacter cloacae, Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli SG14, Hordeum vulgare, Klebsiella aerogenes, Lactuca sativa, Magnetospirillum molischianum, Micrococcus luteus, Mycolicibacterium smegmatis, Nicotiana tabacum, Oryza sativa, Persea americana, Phaseolus vulgaris, Pisum sativum, Rhizobium viscosum, Rhodobacter capsulatus, Rhodocyclus tenuis, Rhodomicrobium vannielii, Rhodopseudomonas palustris, Rhodospirillum rubrum, Rubrivivax gelatinosus, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia liquefaciens, Serratia marcescens, Shigella dysenteriae, Solanum lycopersicum, Solanum tuberosum, Sorghum sp., Spinacia oleracea, Synechococcus sp., Synechocystis sp., Tetradesmus obliquus, Triticum aestivum, Vigna radiata var. radiata, Zea mays
brenda
Crevillen, P.; Ballicora, M.A.; Merida, A.; Preiss, J.; Romero, J.M.
The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme
J. Biol. Chem.
278
28508-28515
2003
Anabaena sp. (P30521), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Arabidopsis thaliana (P55230), Arabidopsis thaliana (P55231), Arabidopsis thaliana (Q9SIK1), Arabidopsis thaliana, Beta vulgaris (P55232), Beta vulgaris (P55233), Hordeum vulgare (O04896), Hordeum vulgare (P30524), Hordeum vulgare (P55238), Ipomoea batatas (O81274), Ipomoea batatas (Q42859), no activity in Arabidopsis thaliana, Oryza sativa (O23809), Oryza sativa (P15280), Oryza sativa (P93430), Oryza sativa (Q9ARH9), Pisum sativum (Q43815), Pisum sativum (Q43816), Pisum sativum (Q43819), Solanum lycopersicum (O04924), Solanum lycopersicum (P93229), Solanum lycopersicum (P93230), Solanum lycopersicum (Q42882), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Solanum tuberosum (P55243), Solanum tuberosum (Q00081), Solanum tuberosum LS1 (Q00081), Solanum tuberosum LS3 (P55243), Synechocystis sp. (P52415), Triticum aestivum (P12299), Triticum aestivum (P30523), Vicia faba (P52416), Vicia faba (P52417), Vicia faba SS1 (P52416), Vicia faba SS2 (P52417), Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0)
brenda
Greene, T.W.; Hannah, L.C.
Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
Proc. Natl. Acad. Sci. USA
95
13342-13347
1998
Zea mays
brenda
Salamone, P.R.; Greene, T.W.; Kavakli, I.H.; Okita, T.W.
Isolation and characterization of a higher plant ADP-glucose pyrophosphorylase small subunit homotetramer
FEBS Lett.
482
113-118
2000
Zea mays, Escherichia coli (P0A6V1), Escherichia coli, Solanum tuberosum (P23509), Solanum tuberosum, Anabaena sp. (P30521), Synechocystis sp. (P52415), Solanum tuberosum SS (P23509)
brenda
Burger, B.T.; Cross, J.M.; Shaw, J.R.; Caren, J.R.; Greene, T.W.; Okita, T.W.; Hannah, L.C.
Relative turnover numbers of maize endosperm and potato tuber ADP-glucose pyrophosphorylases in the absence and presence of 3-phosphoglyceric acid
Planta
217
449-456
2003
Oryza sativa, Solanum tuberosum, Zea mays
brenda
Smidansky, E.D.; Martin, J.M.; Hannah, L.C.; Fischer, A.M.; Giroux, M.J.
Seed yield and plant biomass increases in rice are conferred by deregulation of endosperm ADP-glucose pyrophosphorylase
Planta
216
656-664
2003
Oryza sativa, Zea mays
brenda
Johnson, P.E.; Patron, N.J.; Bottrill, A.R.; Dinges, J.R.; Fahy, B.F.; Parker, M.L.; Waite, D.N.; Denyer, K.
A low-starch barley mutant, riso 16, lacking the cytosolic small subunit of ADP-glucose pyrophosphorylase, reveals the importance of the cytosolic isoform and the identity of the plastidial small subunit
Plant Physiol.
131
684-696
2003
Triticum aestivum (P30523), Hordeum vulgare (P55238), Hordeum vulgare (Q8HS72), Hordeum vulgare, Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0), Oryza sativa (Q9ARH9)
brenda
Ballicora, M.A.; Iglesias, A.A.; Preiss, J.
ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
Photosynth. Res.
79
1-24
2004
Aeromonas caviae, Agrobacterium tumefaciens, Allochromatium vinosum, Synechocystis sp., Arabidopsis thaliana, Geobacillus stearothermophilus, Bacillus subtilis, Chlamydomonas reinhardtii, [Chlorella] fusca, Chlorella vulgaris, Escherichia coli, Nostoc sp., Oryza sativa, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodocyclus purpureus, Rhodospirillum rubrum, Rhodocyclus tenuis, Serratia marcescens, Solanum tuberosum, Spinacia oleracea, Synechococcus sp., Triticum aestivum, Zea mays, Rhodobacter gelatinosa, Rhodobacter globiformis, Synechococcus sp. PCC6301
brenda
Boehlein, S.K.; Sewell, A.K.; Cross, J.; Stewart, J.D.; Hannah, L.C.
Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics
Plant Physiol.
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Solanum tuberosum, Zea mays
brenda
Linebarger, C.R.; Boehlein, S.K.; Sewell, A.K.; Shaw, J.; Hannah, L.C.
Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N-terminus of the small subunit
Plant Physiol.
139
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2005
Zea mays
brenda
Meyer, F.D.; Smidansky, E.D.; Beecher, B.; Greene, T.W.; Giroux, M.J.
The maize Sh2r6hs ADP-glucose pyrophosphorylase (AGP) large subunit confers enhanced AGP properties in transgenic wheat (Triticum aestivum)
Plant Sci.
167
899-911
2004
Zea mays
brenda
Roesti, S.; Denyer, K.
Two paralogous genes encoding small subunits of ADP-glucose pyrophosphorylase in maize, Bt2 and L2, replace the single alternatively spliced gene found in other cereal species
J. Mol. Evol.
65
316-327
2007
Zea mays, Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0)
brenda
Smidansky, E.D.; Meyer, F.D.; Blakeslee, B.; Weglarz, T.E.; Greene, T.W.; Giroux, M.J.
Expression of a modified ADP-glucose pyrophosphorylase large subunit in wheat seeds stimulates photosynthesis and carbon metabolism
Planta
225
965-976
2007
Zea mays
brenda
Slewinski, T.L.; Ma, Y.; Baker, R.F.; Huang, M.; Meeley, R.; Braun, D.M.
Determining the role of Tie-dyed1 in starch metabolism: epistasis analysis with a maize ADP-glucose pyrophosphorylase mutant lacking leaf starch
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99
661-666
2008
Zea mays
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Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined
Plant Physiol.
146
289-299
2008
Zea mays
brenda
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase
Plant Physiol.
149
318-326
2008
Solanum tuberosum, Zea mays
brenda
Georgelis, N.; Hannah, L.C.
Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant
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175
247-254
2008
Zea mays
brenda
Cossegal, M.; Chambrier, P.; Mbelo, S.; Balzergue, S.; Martin-Magniette, M.L.; Moing, A.; Deborde, C.; Guyon, V.; Perez, P.; Rogowsky, P.
Transcriptional and metabolic adjustments in ADP-glucose pyrophosphorylase-deficient bt2 maize kernels
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146
1553-1570
2008
Zea mays (Q947C0), Zea mays
brenda
Georgelis, N.; Shaw, J.R.; Hannah, L.C.
Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme
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151
67-77
2009
Solanum tuberosum (Q00081), Zea mays (P55241), Zea mays
brenda
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Studies of the kinetic mechanism of maize endosperm ADP-glucose pyrophosphorylase uncovered complex regulatory properties
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Zea mays
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Boehlein, S.K.; Shaw, J.R.; Hannah, L.C.; Stewart, J.D.
Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
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2010
Zea mays
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Boehlein, S.K.; Shaw, J.R.; Hwang, S.K.; Stewart, J.D.; Curtis Hannah, L.
Deciphering the kinetic mechanisms controlling selected plant ADP-glucose pyrophosphorylases
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535
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2013
Solanum tuberosum, Zea mays (Q947C0 and P55241), Zea mays
brenda
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Sullivan, B.; Hannah, L.C.
Enhancing the heat stability and kinetic parameters of the maize endosperm ADP-glucose pyrophosphorylase using iterative saturation mutagenesis
Arch. Biochem. Biophys.
568
28-37
2015
Zea mays (Q947C0 and P55241), Zea mays
brenda