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Information on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase and Organism(s) Solanum tuberosum and UniProt Accession P23509
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2.7.7.27 glucose-1-phosphate adenylyltransferaseSpecify your search results
Word Map
- 2.7.7.27
- starch
- endosperm
- potato
- grain
- maize
- glycogen
- tuber
- wheat
- 3-phosphoglycerate
- tuberosum
-
sink
- amylose
- plastid
- solanum
- invertase
-
granule-bound
-
heterotetrameric
- kernel
- plastidial
- ppases
- amylopectin
- orthophosphate
- sh2
- phosphoglucomutase
-
debranching
- amyloplasts
-
grain-filling
-
waxy
-
starchless
-
source-sink
- biotechnology
-
anthesis
- agriculture
-
endosperm-specific
-
spikelets
- synthesis
- isoamylase
-
pyrophosphorolysis
- fructose-1,6-bisphosphate
-
photosynthate
-
photoassimilate
- pullulanase
-
starch-branching
The taxonomic range for the selected organisms is: Solanum tuberosum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
adp-glucose pyrophosphorylase, agpase, adpglucose pyrophosphorylase, adp glucose pyrophosphorylase, shrunken-2, adp-glc ppase, adp-glc pyrophosphorylase, brittle-2, adp-glucose synthetase, adenosine diphosphate glucose pyrophosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-diphosphate glucose pyrophosphorylase
-
-
-
-
adenosine diphosphate glucose pyrophosphorylase
adenosine diphosphoglucose pyrophosphorylase
-
-
-
-
adenylyltransferase, glucose 1-phosphate
-
-
-
-
ADP glucose pyrophosphorylase
-
-
-
-
ADP-glucose pyrophosphorylase
ADP-glucose synthase
-
-
-
-
ADP-glucose synthetase
-
-
-
-
ADPG pyrophosphorylase
-
-
-
-
ADPglucose pyrophosphorylase
-
-
-
-
AGPase
adenosine diphosphate glucose pyrophosphorylase
-
-
-
-
ADP-glucose pyrophosphorylase
-
-
-
-
ADP-glucose pyrophosphorylase
-
-
AGPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-alpha-D-glucose
the small and large subunits of the enzyme define the catalytic and regulatory subunits
ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-alpha-D-glucose
the small and large subunits of the enzyme define the catalytic and regulatory subunits
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:alpha-D-glucose-1-phosphate adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9027-71-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
8-N3-ATP + alpha-D-glucose 1-phosphate
8-N3-ADP-D-glucose + diphosphate
-
both the large and small subunit in the heterotetrameric form are labeled at equivalent rates with 8-N3-ATP, an analog which can readily substitute for ATP in catalysis
-
-
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
ADP-D-glucose + diphosphate
-
-
-
-
r
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
ADP-D-glucose + diphosphate
-
the small subunit displays both catalytic and regulatory properties, the large subunit possesses catalytic and regulatory properties only when assembled with small subunit, the net properties of the heterotetrameric enzyme is a product of subunit synergy, 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
-
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
-
-
?
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
-
ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis
-
-
?
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
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch synthesis, both subunits are involved in the allosteric regulation of AGPase
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
enzyme consists of two regulatory large subunits and two catalytic small subunits. Allosterism and catalysis are the products of an interplay between the regulatory large subunits and the catalytic small subunits that result in a synergistic response to the allosteric effectors and substrates
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
additional information
?
-
-
presence of 3-phosphoglycerate increases the velocity and the affinity for glucose 1-phosphate for the potato enzymes. Redox state does not affect kcat of the two potato isoforms. Without 3-phosphoglycerate the oxidized potato enzyme exhibits a rapid equilibrium random bi-bi mechanism with a dead end ternary complex
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
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
-
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
-
-
?
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
-
ADP-glucose pyrophosphorylase catalyzes the first committed and rate-limiting step in starch biosynthesis
-
-
?
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
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
rate-limiting step in starch synthesis, both subunits are involved in the allosteric regulation of AGPase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP-alpha-D-glucose
-
in wild-type, competitive with ATP, noncompetitive with glucose 1-phosphate. In chimeric mutant, competitive with ATP, mixed type inhibition with glucose 1-phosphate
diphosphate
-
in wild-type, mixed type inhibition with ATP, competitive with glucose 1-phosphate. In chimeric mutant, mixed type inhibition with ATP, competitive with glucose 1-phosphate
dithiothreitol
-
in presence of 3-phophoglycerate, decrease of acitivity for enzyme from tuber
phosphate
-
at 0.5 mM 3-phosphoglycerate, 50% inhibition of wild-type at 0.54 mM, of mutation P52L, large subunit, at 0.52 mM, of mutation P52L, large subunit, plus mutation L46F, small subunit at 0.61 mM, of mutation P52L, large subunit, plus mutation P112L, small subunit at 0.43 mM, of mutation P52L, large subunit, plus mutation P308L, small subunit at 2.5 mM, of mutation P52L, large subunit, plus mutation R350K, small subunit at 1.9 mM
phosphate
-
mutant Mos(1-198) is significantly inhibited in the absence of 3-phosphoglycerate even at low phosphate concentrations. Inhibition levels of wild-type and deletion mutants by phosphate, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP-D-glucose
-
activation of mutant Mos(1-198) is reduced compared to the wild-type enzyme, overview
dithiothreitol
-
in absence of 3-phosphoglycerate, increase of acitivity for enzyme from tuber, no effect on enzyme from leaf
fructose 1,6-bisphosphate
-
activation kinetics. 50% of the maximal velocity at 0.84 mM
glucose 6-phosphate
-
activation kinetics. 50% of the maximal velocity at 1.8 mM
3-phosphoglycerate
50% activation at 0.12 mM for wild-type, at 1.38 mM for mutant D157E, at 0.03 mM for mutant K41R of large subunit plus D143N of small subunit
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
-
the homotetrameric small subunit has much lower affinity for activator than the heterotetrameric enzyme
3-phosphoglycerate
-
50% activation of wild-type at 0.04 mM, of mutation P52L, large subunit, at 0.27 mM, of mutation P52L, large subunit, plus mutation L46F, small subunit at 0.1 mM, of mutation P52L, large subunit, plus mutation P112L, small subunit at 0.14 mM, of mutation P52L, large subunit, plus mutation P308L, small subunit at 0.006 mM, of mutation P52L, large subunit, plus mutation R350K, small subunit at 0.01 mM
3-phosphoglycerate
-
50% of maximal activation for wild-type at 0.11 mM, for mutant P17L at 0.08 mM, for mutant P26L at 0.15 mM, for mutant P44L at 0.25 mM, for mutant P52L at 0.77 mM, for mutant P55L at 0.26 mM, for mutant P66L at 0.03 mM
3-phosphoglycerate
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
3-phosphoglycerate
-
in leaves and tubers 1.4-3.8fold, DTT decreases the activation, overview
3-phosphoglycerate
-
activation kinetics. 50% of the maximal velocity at 0.054 mM
3-phosphoglycerate
A0.5 value for wild-type 0.28 mm, for large subunit E370G/small subunit wild-type 0.83 mM
3-phosphoglycerate
activation. A0.5 value and Hill coefficient for wild-type 0.076 mM and 1.0, large subunit mutant E38K 0.013 mM and 0.9, large subunit mutant G101N 0.023 mM and 1.0, large subunit mutant E38K/G101N 0.006 mM and 0.4
3-phosphoglycerate
-
presence of 3-phosphoglycerate increases the velocity and the affinity for glucose 1-phosphate for the potato enzymes. Redox state does not affect kcat of the two potato isoforms. Without 3-phosphoglycerate the oxidized potato enzyme exhibits a rapid equilibrium random bi-bi mechanism with a dead end ternary complex. Activation constant Ka is 0.52 for the oxidized and 0.20 for the reduced enzyme and 0.03 for the chimeric enzyme
fructose 6-phosphate
-
activation kinetics. 50% of the maximal velocity at 1.5 mM
fructose 6-phosphate
-
activation constant Ka is 9.8 for the oxidized and 20 for the reduced enzyme and 0.15 for the chimeric enzyme, respectively
additional information
-
mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
alpha-D-glucose 1-phosphate
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.25
alpha-D-glucose 1-phosphate
pH 7.5, 37°C, mutant TG-15, kinetic study
0.38
alpha-D-glucose 1-phosphate
mutation K41R, large subunit, plus D143N, small subunit
1.01
alpha-D-glucose 1-phosphate
mutation T51K, large subunit, plus D143N, small subunit
0.35
ATP
mutation K41R/T51K, large subunit, plus D143N, small subunit
0.017
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.05
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.074
alpha-D-glucose 1-phosphate
large subunit mutant G101N, pH 7.5, 37°C
0.081
alpha-D-glucose 1-phosphate
large subunit mutant E38K/G101N, pH 7.5, 37°C
0.1
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.13
alpha-D-glucose 1-phosphate
large subunit E370G/small subunit wild-type, pH 7.4, 37°C
0.158
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, presence of ATPgammaS, pH 7.4, 25°C
0.17
alpha-D-glucose 1-phosphate
large subunit mutant E38K, pH 7.5, 37°C
0.194
alpha-D-glucose 1-phosphate
heterodimer of small/large subunit, pH 7.4, 25°C
0.21
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.36
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.39
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.41
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
0.42
alpha-D-glucose 1-phosphate
-
mutation P52L, large subunit, 37°C, pH 7.0
4.01
alpha-D-glucose 1-phosphate
-
oxidized wild-type, pH 7.4, 37°C, presence of phosphate
5.18
alpha-D-glucose 1-phosphate
-
reduced wild-type, pH 7.4, 37°C, presence of phosphate
6.79
alpha-D-glucose 1-phosphate
-
chimeric enzyme, pH 7.4, 37°C, presence of phosphate
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
0.044
ATP
-
pH 7.4, 37°C, mutant Mos(1-277), in absence of 3-phosphoglycerate
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 3-0.040 phosphoglycerate
0.056
ATP
-
pH 7.4, 37°C, mutant Mos(1-198, 377-475), in absence of 3-phosphoglycerate
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
0.13
ATP
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
0.22
ATP
-
mutation P52L, large subunit, plus mutation P112L, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation L46F, small subunit, 37°C, pH 7.0
0.24
ATP
-
mutation P52L, large subunit, plus mutation P308L, small subunit, 37°C, pH 7.0
0.29
ATP
-
mutation P52L, large subunit, plus mutation R350K, small subunit, 37°C, pH 7.0
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
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
-
kinetics of wild-type and mutant large subunits, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
0.002
alpha-D-glucose 1-phosphate
mutation D157L, large subunit, plus D143N, small subunit
0.07
alpha-D-glucose 1-phosphate
mutation K41R, large subunit, plus D143N, small subunit
4
alpha-D-glucose 1-phosphate
mutation T51K, large subunit, plus D143N, small subunit
9
alpha-D-glucose 1-phosphate
mutation K41R/T51K, large subunit, plus D143N, small subunit
11.9
ATP
mutation K41R/T51K, large subunit, plus D143N, small subunit
101
alpha-D-glucose 1-phosphate
large subunit mutant G101N, pH 7.5, 37°C
105
alpha-D-glucose 1-phosphate
large subunit mutant E38K/G101N, pH 7.5, 37°C
142
alpha-D-glucose 1-phosphate
large subunit mutant E38K, pH 7.5, 37°C
147.7
ATP
-
reduced wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
163.1
ATP
-
oxidized wild-type, pH 7.4, 37°C, presence of 3-phosphoglycerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
819
alpha-D-glucose 1-phosphate
large subunit mutant E38K, pH 7.5, 37°C
1300
alpha-D-glucose 1-phosphate
large subunit mutant E38K/G101N, pH 7.5, 37°C
1360
alpha-D-glucose 1-phosphate
large subunit mutant G101N, pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
ADP-alpha-D-glucose
-
oxidized wild-type, 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
0.11
ADP-alpha-D-glucose
-
oxidized wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.11
ADP-alpha-D-glucose
-
oxidized wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.13
ADP-alpha-D-glucose
-
oxidized wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.14
ADP-alpha-D-glucose
-
reduced wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.21
ADP-alpha-D-glucose
-
reduced wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.46
ADP-alpha-D-glucose
-
reduced wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.025
diphosphate
-
reduced wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
oxidized wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
oxidized wild-type, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.047
diphosphate
-
reduced wild-type, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.19
diphosphate
-
oxidized wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.35
diphosphate
-
chimeric mutant, substrate glucose 1-phosphate, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.35
diphosphate
-
reduced wild-type, substrate glucose 1-phosphate, pH 7.4, 37°C
0.44
diphosphate
-
chimeric mutant, substrate glucose 1-phosphate, pH 7.4, 37°C
0.55
diphosphate
-
chimeric mutant, substrate ATP, presence of 3-phosphoglycerate, pH 7.4, 37°C
0.04
phosphate
-
pH 8.0, 37°C, recombinant heterotetrameric enzyme, in absence of 3-phosphoglycerate
0.08
phosphate
-
pH 8.0, 37°C, the small subunit of enzyme, in presence of 3 mM 3-phosphoglycerate
0.63
phosphate
-
pH 8.0, 37°C, recombinant heterotetrameric enzyme, in presence of 3 mM 3-phosphoglycerate
1
phosphate
-
the phosphate inhibition pattern of Mos(1-198) is complex and biphasic. Inhibition at relatively high phopshate concentrations is less than predicted at low phosphate concentrations, the calculated Ki for phosphate is about 1 mM before 50% inhibition and 36 mM after 50% inhibition. Inhibition kinetics of mutants in presence and absence of 3-phosphoglycerate
additional information
additional information
comparison of Ki of phosphate
-
additional information
additional information
-
comparison of Ki of phosphate
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
phosphate
Solanum tuberosum
large subunit E370G/small subunit wild-type, presence of 1 mM 3-phosphoglycerate, pH 7.4, 37°C
0.38
phosphate
Solanum tuberosum
large subunit E370G/small subunit wild-type, presence of 2.5 mM 3-phosphoglycerate, pH 7.4, 37°C
0.44
phosphate
Solanum tuberosum
wild-type, presence of 1 mM 3-phosphoglycerate, pH 7.4, 37°C
0.67
phosphate
Solanum tuberosum
wild-type, presence of 2.5 mM 3-phosphoglycerate, pH 7.4, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
0.72
-
purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate
1.68
-
purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate
1.78
-
purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate
6.14
-
purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate
6.81
-
purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate
8.59
-
purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate
additional information
additional information
-
the small subunit alone is highly active but the large subunit alone has negligible catalytic activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 9.5
-
about half-maximal activity at pH 6.8 and about 70% of maximal activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
ADP-glucose pyrophosphorylase is a key allosteric enzyme involved in higher plants starch biosynthesis
physiological function
physiological function
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis
physiological function
-
ADP-glucose pyrophosphorylase is a key allosteric enzyme involved in higher plants starch biosynthesis
physiological function
-
catalyses the key regulatory step in starch synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLGS_SOLTU
521
0
57240
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
100000
-
AGPase subunit B, dimer, determined by SDS-PAGE and Western blot analysis
200000
50000
additional information
50000
-
AGPase subunit B, monomer, determined by SDS-PAGE and Western blot analysis
additional information
-
amino acid sequences of two novel enzymes AGP S2 and AGP S3 and comparison of the degree if identity with another
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
the enzyme is composed of pairs of large, LS, and small subunits, SS, 2 * 51000 + 2 * 50000 Da
heterotetramer
homotetramer
tetramer
-
AGPase is a heterotetramer comprised of two identical large and two identical small subunits in plants
additional information
heterotetramer
-
plant enzymes, composed of two large, 51000-60000 Da, and two small subunits, 50000-55000 Da
heterotetramer
-
the large subunit is 51000 Da, major function is to modulate the regulatory properties of the enzyme and the small subunit is 50000 Da, major function is catalysis, SDS-PAGE
heterotetramer
-
enzyme consists of two regulatory large subunits and two catalytic small subunits. Allosterism and catalysis are the products of an interplay between the regulatory large subunits and the catalytic small subunits that result in a synergistic response to the allosteric effectors and substrates
heterotetramer
-
consists of two small, AGPB, and two slightly larger, AGPS, subunits
heterotetramer
-
the enzyme is composed of pairs of large, LS, and small subunits, SS
additional information
-
chimeric enzyme containing N-terminus of Solanum tuberosum enzyme small subunit and C-terminus of Anabaena sp. small subunit and the inverse chimera. The N-terminus determines stability and regulatory redox-dependent properties. The interaction between the putative N- and C-domains determines the affinity for 3-phosphoglycerate. The large subunit functions mainly in modulating regulation of the enzyme by coordinate action of 3-phosphoglycerate and phosphate
additional information
-
higher plant ADP-glucose pyrophosphorylase is a heterotetramer consisting of two subunit types, which have evolved at different rates from a common ancestral gene. The potato tuber small subunit displays both catalytic and regulatory properties. The large subunit possesses catalytic and regulatory properties only when assembled with small subunit, the net properties of the heterotetrameric enzyme is a product of subunit synergy, modeling of AGPase structures, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
substitution of two lysine residues into maize enzyme to produce a variant containing the three lysines found in the large subunit of potato enzyme has no effect on 3-phosphoglycerate activation of the maize enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of alpha-subunit are grown in high concentrations of sulfate, resulting in the sulfate-bound, allosterically inhibited form of the enzyme. Structures of the enzyme in complex with ATP and ADP-glucose
-
isothermal titration calorimetry of substrate binding properties. The wild type heterotetramer possesses two distinct types of ATP binding sites, whereas the homotetrameric large/small subunit and small/small subunit variant forms only exhibit properties of one of the two binding sites. The wild type enzyme also exhibits significantly increased affinity to ATP compared to the homotetrameric enzyme forms. No stable binding is evident for glucose-1-phosphate, in the presence or absence of ATPgammaS supporting the Theorell-Chance bi-bi reaction mechanism
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A132D
mutation in ATP binding region of large subunit, kinetic analysis
A132F
mutation in ATP binding region of large subunit, kinetic analysis
A132N
mutation in ATP binding region of large subunit, kinetic analysis
A132V
mutation in ATP binding region of large subunit, kinetic analysis
D157E
mutation in ATP binding region of large subunit, kinetic analysis
D157L
D157N
mutation in ATP binding region of large subunit, kinetic analysis
G128A
mutation in ATP binding region of large subunit, kinetic analysis
G128L
mutation in ATP binding region of large subunit, kinetic analysis
G267L
mutation in ATP binding region of large subunit, kinetic analysis
G267S
mutation in ATP binding region of large subunit, kinetic analysis
G36A
mutation in ATP binding region of large subunit, kinetic analysis
G37A
mutation in ATP binding region of large subunit, kinetic analysis
K41R
K41R/T51K
L48F/V59I
TG-15, significant alteration in effector sensitivity of this homotetrameric enzyme in comparison to wild-type heterotetrameric enzyme
Q127M
mutation in ATP binding region of large subunit, kinetic analysis
T129V
mutation in ATP binding region of large subunit, kinetic analysis
T129V/A132V
mutation in ATP binding region of large subunit, kinetic analysis
T51K
E370G
mutation in the large subunit alters the heterotetrameric stability along with the binding properties of substrate and effectors of the enzyme. The affinity of the large subunit E370G/small subunit wild-type AGPase for glucose-1-phosphate is 3fold less than for wild type AGPase. The mutant enzyme complex requires 3fold more 3-phosphogyceric acid to be activated and lis less heat stable
E38K
the enzyme activities of large subunit mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
E38K/G101N
in an Escherichia coli mutant defective in the synthesis of ADP-glucose, expression of large subunit mutant E38K/G101N mediates higher glycogen production than wild-type potato AGPase and the single mutant enzymes, E38K and G101N, individually. Purified large subunit mutant E38K/G101N shows higher sensitivity to 3-phosphoglycerate activation and tolerance to phosphate inhibition than mutants E38K or G101N. The enzyme activities of mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
F332S
-
site-directed mutagenesis in the potato part of the chimeric mutant
G101N
the enzyme activities of large subunit mutants E38K, G101N, and E38K/G101N are more readily stimulated by phosphate-ester metabolites, such as fructose 6-phosphate, fructose 2,6-bisphosphate, and ribose 5-phosphate, than that of wild-type
H341Y
-
site-directed mutagenesis in the potato part of the chimeric mutant
I323V
-
site-directed mutagenesis in the potato part of the chimeric mutant
L46F
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
LSH342A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSH89A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI330K
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI335R
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI339A/I330A
-
large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSK334A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSK336A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN102A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN87A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSP327A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR45A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR88A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR92A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LST328A/I330A
-
large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSW135A
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSW135R
-
large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
N369H
-
site-directed mutagenesis in the potato part of the chimeric mutant
P112L
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
P17L
-
mutation in large enzyme subunit, moderate effect on catalytic properties
P26L
-
mutation in large enzyme subunit, moderate effect on catalytic properties but severely impaired catalytic rates
P308L
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
P44L
-
mutation in large enzyme subunit, moderate changes in properties toward 3-phosphoglycerate
P52L
P55L
-
mutation in large enzyme subunit, moderate effect on catalytic properties
P66L
-
mutation in large enzyme subunit, up-regulatory properties toward 3-phosphoglycerate
R350K
-
mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
S302N
-
site-directed mutagenesis, the mutant shows increased solubility of the recombinant potato tuber large subunit and, in turn, enabling it to form a homotetrameric structure. The LS302N homotetramer possesses very little enzyme activity at a level 100fold less than that seen for the unactivated small subunit homotetramer. Unlike the small subunit enzyme, the LS302N homotetramer enzyme is neither activated by the effector 3-phosphoglycerate nor inhibited by phosphate. The mutation significantly enhances glycogen production in bacterial host cells
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
additional information
D157L
mutation in ATP binding region of large subunit, kinetic analysis
D157L
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
K41R
mutation in ATP binding region of large subunit plus mutation D143N in small subunit, kinetic analysis
K41R
mutation in ATP binding region of large subunit, kinetic analysis
K41R/T51K
mutation in ATP binding region of large subunit, kinetic analysis
K41R/T51K
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
T51K
mutation in ATP binding region of large subunit, kinetic analysis
T51K
mutation in ATP binding region of large subunit, plus mutation D143N in small subunit, kinetic analysis
P52L
-
mutation in large enzyme subunit, down-regulatory properties toward 3-phosphoglycerate
P52L
-
mutation in large subunit, mutant is 5fold less sensitive to activation by 3-phosphoglycerate
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
-
chimeric enzyme containing N-terminus of Solanum tuberosum enzyme small subunit and C-terminus of Anabaena sp. small subunit and the inverse chimera. The N-terminus determines stability and regulatory redox-dependent properties. The interaction between the putative N- and C-domains determines the affinity for 3-phosphoglycerate
additional information
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit and vice versa using different arabidospsis large subunit isoforms. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
additional information
-
construction of a LRKNSWT heterotetramer, the LS mutant homotetramer LRKN is catalytically very inefficient, binds ATP less efficiently, and is less heat-stable, overview
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 wt maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with ADP-D-glucose, 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
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
purification of small subunit enzyme TG-15 involves a 7 min/55°C heat shock step
42
-
wild-type AGPAse in the absence of 3-phosphoglycerate has a half-life of 1 min, whereas mutant Mos(1-198) has a half-life of 5.5 min, when 3-phosphoglycerate is added to the wid-type enzyme, the half-life increases to 5.5 min and the half-life of the mutant is incrwased to 9.4 min
60
65
-
large and truncated small subunits: 1.4% remaining activity, large and small subunits: 83% remaining activity, the small subunit: 102% remainig activity after heat treatment
60
-
large and truncated small subunits: 24% remaining activity, large and small subunits: 89% remaining activity, the small subunit: 98% remainig activity after heat treatment
60
-
5 min, the recombinant LRKNSWT heterotetrameric mutant retains 92% of wild-type AGPase activity, the recombinant SWT homotetrameric mutant has an intermediate level of 68%, whereas the recombinant homotetrameric mutant LRKN shows only below 7% of wild-type activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, majority of activity is retained for several months, mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
4°C, in 50 mM HEPES buffer, pH 7.5, 20% sucrose, 1 mM EDTA, 2 mM GSH, at least 6 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, homotetrameric small subunit enzyme TG-15, heat shock step at 55°C
recombinant mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography
-
the heterotetrameric plant enzyme can efficiently be purified by attachment of polyhistidine tag to the amino-terminus of the large subunit or small subunit. Polyhistidine tags do no alter enzymatic properties of the enzyme. The use of the polyhistidine-tagged large subunit will enable the facile purification of preparative amounts of the enzyme, free of potentially formed small-subunit homotetramer, for future biochemical studies
-
the recombinant enzyme containing the large subunit and the truncated small subunit, the recombinant enzyme containing the small subunit and the large subunit and the small subunit alone
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the cDNAs of potato AGPase LS and SS are cloned into pGADT7 and pGBKT7 vectors, respectively
wild-type gene pML10 is mutated by hydroxylamine, the mutated SS gene TG-15 is expressed in Escherichia coli AC70R1-504
DNA and amino acid sequence determination and analysis, phylogenetic analysis, and determination and analysis of rates of evolution, the number of duplications in both large and small subunit genes and document changes in the patterns of AGPase evolution over time. The AGPase large subunit family occurs early in the history of land plants, while the earliest small subunit duplication occurs after the divergence of monocots and eudicots. The large subunit also has a larger number of gene duplications than does the small subunit, overview
-
expression in Escherichia coli. Different combinations of wild-type regulatory large subunit and variant forms L(UpREg1) and L(M345) are cowxpressed with wild-type catalytic small subunit and variant forms S(TG-15) and S(devo330)
-
expression of mosaic AGPases composed of Solanum tuberosum tuber and Zea mays endosperm subunit fragments in Escherichia coli
-
mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber, expression in Escherichia coli
-
survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available
-
the cDNAs of potato AGPase LS and SS are PCR amplified using pML7 and pML10 plasmids as template, respectively, and ligated into pGADT7 and pGBKT7 vectors for the yeast two-hybrid assay
-
The genes of both subunits of enzyme are cloned, expression in Escherichia coli strain AC70R1-504, the one cloned small subunit lacks 10 amino acids of the N-terminus, and is defined as the truncated small subunit. A new cDNA clone of the small subunit encodes a polypeptide that has 10 amino acids more at the N-terminus than the truncated small subunits
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition of enzyme by dithiothreitol is prevented by pre- or by coincubation with 3-phophoglycerate, but incubation of already inhibited enzyme with 3-phophoglycerate may not reverse the inhibition
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the results suggest that the sweetpotato ibAGP1 promoter and its transit peptide are a strong foreign gene expression system that can be used for molecular farming in potato plants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sowokinos, J.R.; Preiss, J.
Pyrophphosphorylases in Solanum tuberosum, III. Purification, physical, and catalytic properties of ADPglucose pyrophophorylase in potatoes
Plant Physiol.
69
1459-1466
1982
Solanum tuberosum
Sowokinos, J.R.
Pyrophphosphorylases in Solanum tuberosum, II. Catalytic properties an reguation of ADP-glucose and UDP-glucose pyrophosphorylase activities in potatoes
Plant Physiol.
68
924-929
1981
Solanum tuberosum
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
-
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
La Cognata, U.; Willmitzer, L.; Mller-Rber, B.
Molecular cloning and characterization of novel isoforms of potato ADP-glucose pyrophosphorylase
Mol. Gen. Genet.
246
538-548
1995
Solanum tuberosum
Ballicora, M.A.; Laughlin, M.J.; Fu, Y.; Okita, T.W.; Barry, G.F.; Preiss, J.
Adenosine 5'-diphosphate-glucose pyrophosphorylase from potato tuber. Significance of the N terminus of the small subunit for catalytic properties and heat stability
Plant Physiol.
109
245-251
1995
Solanum tuberosum
Zabawinski, C.; Van Den Koornhuyse, N.; D'Hulst, C.; Schlichting, R.; Giersch, C.; Delrue, B.; Lacroix, J.M.; Preiss, J.; Ball, S.
Starchless mutants of Chlamydomonas reinhardtii lack the small subunit of a heterotetrameric ADP-glucose pyrophosphorylase
J. Bacteriol.
183
1069-1077
2001
Salmonella enterica subsp. enterica serovar Typhimurium (P05415), Oryza sativa (P15280), Oryza sativa (P93430), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Anabaena sp. (P30521), Synechocystis sp. (P52415), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Chlamydomonas reinhardtii (Q42702), Chlamydomonas reinhardtii (Q9LLL6), Chlamydomonas reinhardtii, Solanum tuberosum LS2 (P55242)
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)
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)
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
Jin, X.; Ballicora, M.A.; Preiss, J.; Geiger, J.H.
Crystal structure of potato tuber ADP-glucose pyrophosphorylase
EMBO J.
24
694-704
2005
Solanum tuberosum
Hwang, S.K.; Salamone, P.R.; Okita, T.W.
Allosteric regulation of the higher plant ADP-glucose pyrophosphorylase is a product of synergy between the two subunits
FEBS Lett.
579
983-990
2005
Solanum tuberosum
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
Cross, J.M.; Clancy, M.; Shaw, J.R.; Greene, T.W.; Schmidt, R.R.; Okita, T.W.; Hannah, L.C.
Both subunits of ADP-glucose pyrophosphorylase are regulatory
Plant Physiol.
135
137-144
2004
Solanum tuberosum
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.
138
1552-1562
2005
Solanum tuberosum, Zea mays
Hwang, S.K.; Salamone, P.R.; Kavakli, H.; Slattery, C.J.; Okita, T.W.
Rapid purification of the potato ADP-glucose pyrophosphorylase by polyhistidine-mediated chromatography
Protein Expr. Purif.
38
99-107
2004
Solanum tuberosum
Kim, D.; Hwang, S.K.; Okita, T.W.
Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
Biochem. Biophys. Res. Commun.
362
301-306
2007
Solanum tuberosum
Hwang, S.K.; Hamada, S.; Okita, T.W.
ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
FEBS Lett.
580
6741-6748
2006
Solanum tuberosum (P23509), Solanum tuberosum
Chen, L.S.; Qi, Y.P.
Dithiothreitol decreases in vitro activity of ADP-glucose pyrophosphorylase from leaves of apple (Malus domestica Borkh.) and many other plant species
Phytochem. Anal.
18
300-305
2007
Arabidopsis thaliana, Glycine max, Hordeum vulgare, Malus domestica, Solanum lycopersicum, Solanum tuberosum, Sorghum sp., Spinacia oleracea, Triticum aestivum
Hwang, S.K.; Hamada, S.; Okita, T.W.
Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit
Phytochemistry
68
464-477
2007
Escherichia coli, Solanum tuberosum, Escherichia coli ER2566
Iglesias, A.A.; Ballicora, M.A.; Sesma, J.I.; Preiss, J.
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase
Plant Cell Physiol.
47
523-530
2006
Anabaena sp., Solanum tuberosum
Ventriglia, T.; Ballicora, M.A.; Crevillen, P.; Preiss, J.; Romero, J.M.
Regulatory properties of potato-Arabidopsis hybrid ADP-glucose pyrophosphorylase
Plant Cell Physiol.
48
875-880
2007
Arabidopsis thaliana, Solanum tuberosum
Georgelis, N.; Braun, E.L.; Hannah, L.C.
Duplications and functional divergence of ADP-glucose pyrophosphorylase genes in plants
BMC Evol. Biol.
8
232
2008
Arabidopsis thaliana, Chlamydomonas reinhardtii, Hordeum vulgare, Solanum lycopersicum, Oryza sativa, Physcomitrium patens, Solanum tuberosum
Hwang, S.K.; Nagai, Y.; Kim, D.; Okita, T.W.
Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form
J. Biol. Chem.
283
6640-6647
2008
Solanum tuberosum
Oliver, S.N.; Tiessen, A.; Fernie, A.R.; Geigenberger, P.
Decreased expression of plastidial adenylate kinase in potato tubers results in an enhanced rate of respiration and a stimulation of starch synthesis that is attributable to post-translational redox-activation of ADP-glucose pyrophosphorylase
J. Exp. Bot.
59
315-325
2008
Solanum tuberosum
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
Tuncel, A.; Kavakli, I.H.; Keskin, O.
Insights into subunit interactions in the heterotetrameric structure of potato ADP-glucose pyrophosphorylase
Biophys. J.
95
3628-3639
2008
Solanum tuberosum (P23509), Solanum tuberosum
Kim, T.W.; Goo, Y.M.; Lee, C.H.; Lee, B.H.; Bae, J.M.; Lee, S.W.
The sweet potato ADP-glucose pyrophosphorylase gene (ibAGP1) promoter confers high-level expression of the GUS reporter gene in the potato tuber
C. R. Biol.
332
876-885
2009
Solanum tuberosum
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
Plant Physiol.
151
67-77
2009
Solanum tuberosum (Q00081), Zea mays (P55241), Zea mays
Baris, I.; Tuncel, A.; Ozber, N.; Keskin, O.; Kavakli, I.H.
Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase
PLoS Comput. Biol.
5
e1000546
2009
Solanum tuberosum
Kuhn, M.; Figueroa, C.; Iglesias, A.; Ballicora, M.
The ancestral activation promiscuity of ADP-glucose pyrophosphorylases from oxygenic photosynthetic organisms
BMC Evol. Biol.
13
51
2013
Solanum tuberosum, Ostreococcus tauri, Nostoc sp. (P30521), Nostoc sp. PCC 7120 (P30521)
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
Arch. Biochem. Biophys.
535
215-226
2013
Solanum tuberosum, Zea mays (Q947C0 and P55241), Zea mays
Wakuta, S.; Shibata, Y.; Yoshizaki, Y.; Saburi, W.; Hamada, S.; Ito, H.; Hwang, S.K.; Okita, T.W.; Matsui, H.
Modulation of allosteric regulation by E38K and G101N mutations in the potato tuber ADP-glucose pyrophosphorylase
Biosci. Biotechnol. Biochem.
77
1854-1859
2013
Solanum tuberosum (Q00081), Solanum tuberosum
Cakir, B.; Tuncel, A.; Green, A.R.; Koper, K.; Hwang, S.K.; Okita, T.W.; Kang, C.
Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry
FEBS Lett.
589
1444-1449
2015
Solanum tuberosum (Q00081 and P23509), Solanum tuberosum
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