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Information on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A6V1
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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: Escherichia coli
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
ADP-glucose pyrophosphorylase
-
-
-
-
AGPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-alpha-D-glucose
mechanism
-
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
8-azaATP + alpha-D-glucose 1-phosphate
diphosphate + 8-azaADP-glucose
-
the photoaffinity labeling agent is used as a site specific probe of enzyme
reverse reaction is biphasic
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
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
-
substrate binding studies: 1 mol glucose 1-phosphate per mol subunit, 4 mol ADP-glucose per mol tetrameric enzyme
-
?, 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
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
?
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
-
-
?
additional information
?
-
-
identification of regions critically affecting kinetics and allosteric regulation of the ADP-glucose pyrophosphorylase, structure-function analysis, homology modelling, overview
-
-
?
additional information
?
-
-
enzyme displays a regulatory mechanism where the interaction with the allosteric activator triggers conformational changes at the level of loops containing residues Trp113 and Gln74
-
-
?
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
diphosphate + ADP-glucose
-
first unique reaction in synthesis of alpha-1,4-glucosidic linkage
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
major regulated step in the bacterial glycogen biosynthesis pathway
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-azaADP-glucose
-
photoinactivation, competitive inhibition, ADP-glucose and ATP protects
8-azaATP
-
photoinactivation, competitive inhibition, 0.5 mol/mol enzyme subunit for complete inactivation, ADP-glucose and ATP protects
additional information
-
activator/inhibitor interaction in vivo and in vitro
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6-diphosphate
50% of maximal activation at 0.059 for wild-type
1,6-Hexanediol bisphosphate
-
D-fructose 1,6-bisphosphate analog, most effective
2-keto-3-deoxy phosphogluconate
-
fructose 6-phosphate and pyruvate analog, less effective than fructose bisphosphate
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
mainly Escherichia coli and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme, C-terminus of Escherichia coli is relavant for the selectivity
D-fructose 1,6-bisphosphate
-
50% activation at 0.0364 mM for wild-type, at 0.0523 mM for mutant lacking N-terminal 3 amino acids, at 0.0887 mM for mutant lacking N-terminal 7 amino acids
D-fructose 6-phosphate
-
mainly Agrobacterium tumefaciens and chimeric enzyme AE containing the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, not chimeric enzyme EA containing the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
pyruvate
-
activation of chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme with higher affinity than activation of chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
pyruvate
-
pyruvate is a weak activator by itself, and synergically enhances the fructose-1,6-bisphosphate activation
additional information
-
activator/inhibitor interaction in vivo and in vitro
-
additional information
-
effector binding studies, structural requirements for an activator
-
additional information
-
ADP-glucose diphosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structural stability
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
alpha-D-glucose 1-phosphate
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.023
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.04
alpha-D-glucose 1-phosphate
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.12
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.12
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 1.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.143
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.17
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.2
alpha-D-glucose 1-phosphate
-
pH 7.0, 37°C, strain AC70R1, kinetic study
0.22
alpha-D-glucose 1-phosphate
-
mutant P103A, S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
0.23
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.25
alpha-D-glucose 1-phosphate
-
mutant Q106A, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C
0.26
alpha-D-glucose 1-phosphate
-
mutant R107A, S0.5 value, Hill coefficient 0.9, pH 8.0, 37°C
0.27
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.28
alpha-D-glucose 1-phosphate
-
mutant R115A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.34
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.37
alpha-D-glucose 1-phosphate
-
wild-type, S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C
0.39
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.41
alpha-D-glucose 1-phosphate
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.43
alpha-D-glucose 1-phosphate
-
mutant Y114A, S0.5 value, Hill coefficient 0.3, pH 8.0, 37°C
0.46
alpha-D-glucose 1-phosphate
-
mutant W113A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C
0.47
alpha-D-glucose 1-phosphate
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.57
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 25 mM pyruvate, pH 8.0, 37°C
0.77
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.0, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.92
alpha-D-glucose 1-phosphate
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.95
alpha-D-glucose 1-phosphate
-
S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C
0.155
ATP
-
pH 8.0, 37°C, chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
0.162
ATP
-
pH 8.0, 37°C, chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
0.17
ATP
-
wild-type, S0.5 value, Hill coefficient 2.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.26
ATP
-
pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes
0.32
ATP
-
wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.81
ATP
-
mutant P103A, S0.5 value, Hill coefficient 1.5, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
0.99
ATP
-
S0.5 value, Hill coefficient 3.6, presence of 25 mM pyruvate and 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.3
ATP
-
mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.63
ATP
-
mutant R107A, S0.5 value, Hill coefficient 2.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.67
ATP
-
S0.5 value, Hill coefficient 2.5, presence of 25 mM pyruvate, pH 8.0, 37°C
2.2
ATP
-
pH 7.0, 37°C, wild-type enzyme in the absence of fructose 1,6-bisphosphate, comparison of Km of wild-type and mutant enzymes in the presence and absence of fructose 1,6-bisphosphate
2.3
ATP
-
mutant Y114A, S0.5 value, Hill coefficient 1.9, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
2.5
ATP
-
mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
3.1
ATP
-
mutant W113A, S0.5 value, Hill coefficient 1.1, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
4.4
ATP
-
mutant Q106A, S0.5 value, Hill coefficient 1.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
5
ATP
-
S0.5 value, Hill coefficient 2.1, presence of 0.01 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
9.8
ATP
-
mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
additional information
additional information
-
effect of activators on substrate kinetic parameters of bacterial enzymes
-
additional information
additional information
-
kinetics wild-type and mutant enzymes, photoaffinity labeling of the AGPase heterotetramers, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki of AMP, effect of fructose 1,6-bisphosphate on wild-type and mutant enzymes
-
0.007
AMP
-
pH 8.0, 37°C, wild-type enzyme in presence of 0.1 mM fructose-1,6-bisphosphate
0.094
AMP
-
pH 7.0, 37°C, wild-type enzyme, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.3
AMP
-
pH 7.0, 37°C, mutant enzyme P295G, in the presence of a saturating concentration of fructose 1,6-bisphosphate,
0.34
AMP
-
pH 7.0, 37°C, mutant enzyme P295N, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.38
AMP
-
pH 7.0, 37°C, mutant enzyme P295Q, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.95
AMP
-
pH 7.0, 37°C, mutant enzyme G336D, in the presence of a saturating concentration of fructose 1,6-bisphosphate
0.96
AMP
-
pH 7.0, 37°C, mutant enzyme P295E, in the presence of a saturating concentration of fructose 1,6-bisphosphate
2
AMP
-
pH 7.0, 37°C, mutant enzyme P295D, in the presence of a saturating concentration of fructose 1,6-bisphosphate
9
AMP
-
pH 8.0, 37°C, the chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme is slightly activated by AMP in the range of 0.1-2 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.61
-
mutant W113A, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate , pH 8.0, 37°C
0.82
-
mutant Q74A, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.12
-
mutant W113A, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
1.6
-
mutant Q74A, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
27
-
chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme
3.6
-
wild-type, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
36
-
chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme
47.6
-
wild-type, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C
86
-
coexpression of mutant lacking N-terminal 15 amino acids and C-terminal 108 amino acids with C-terminal peptide of 108 amino acids, 37°C, pH 8.0
additional information
additional information
-
a radiometric assay for adenosine 5'-diphosphate (ADP)-glucose diphosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase
additional information
-
catalytic efficiency of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
bacterial glgC-TM gene, which codes for catalytically active, allosteric-insensitive enzyme, is introduced into seeds of Oryza sativa using an Agrobacterium tumefaciens-mediated transformation. The TM enzyme is expressed in the cytoplasm or amyloplast in Oryza sativa endosperm
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bacterial glgC-TM gene, which codes for catalytically active, allosteric-insensitive enzyme, is introduced into seeds of Oryza sativa using an Agrobacterium tumefaciens-mediated transformation. The TM enzyme is expressed in the cytoplasm or amyloplast in Oryza sativa endosperm
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
185000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
additional information
additional information
-
strain SG5, oligomer formation with several times the tetramer MW in the presence of 1 mM fructose 1,6-bisphosphate, not Escherichia coli B wild-type
additional information
-
structure-function analysis, homology modelling, overview
additional information
-
a Pro103-Arg115 loop is part of an activation path. It has strongly correlated movements with regions of the enzyme associated with regulation and ATP binding, and the optimal network pathways linking ATP and the activator binding Lys39 mainly involve residues of this loop. The loop is a distinct insertional element present only in allosterically regulated sugar nucleotide diphosphorylases
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
covalent modification with 8-azaATP and 8-azaADP-glucose accompanies irreversible loss of the enzyme catalytic activity, in the presence of light
side-chain modification
-
pyridoxal phosphate can covalently modify two distinct lysine residues by reduction with NaBH4, modification increases specific activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of enzyme. Binding of ATP correlates with conformational changes of a loop facing the ATP substrate, going from an open to a closed substrate-bound form
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D239A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D239E
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D239N
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276E
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D276N
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194D
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
E194Q
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
F240A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
F240M
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
K195Q
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212T
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212V
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
S212Y
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274A
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274F
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
W274L
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
Y216F
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
D142A
-
Km values are not significantly different in comparison to the wild-type enzyme, no significant changes for fructose 1,6-bisphosphate activation, Ki value of AMP 3fold increases in comparison to the wild-type enzyme
D142E
-
47fold increase of Km value of glucose 1-phosphate and 11.5fold increase of Km value of ATP in comparison to the wild-type enzyme, activation by fructose 1,6-bisphosphate increases, no significant changes for AMP-inhibition in comparison to the wild-type enzyme
D142N
-
Km values are not significantly different in comparison to the wild-type enzyme, Ki value of AMP 25fold increases in comparison to the wild-type enzyme
G336D
-
a higher activity enzyme form, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
LP17L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP26L
-
site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
LP44E
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44K
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44R
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44S
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44Y
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP55L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP66L
-
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P103A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
P295D
-
extremely high activity in the absence of fructose 1,6-bisphosphate, 20fold decreased affinity for AMP than wild-type enzyme
P295D/G336D
-
the double mutant enzyme is more active in the absence of fructose 1,6-bisphosphate, with a higher affinity for fructose 1,6-bisphosphate and a lower apparent affinity for AMP than either single mutated enzyme
P295E
-
extremely high activity in the absence of fructose 1,6-bisphosphate, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
P295G
P295N
-
3.4fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
P295Q
-
3.8fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
Q106A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R107A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R115A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
W113A
Y114A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
additional information
P295G
-
activity in the absence of fructose 1,6-bisphosphate is similar to wild-type enzyme
P295G
-
3fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
W113A
-
mutation does not change apparent affinities for the substrates, but mutant becomes insensitive to activation by fructose-1,6-bisphosphate. The mutant enzymes still binds fructose-1,6-bisphosphate, with similar affinity as the wild type enzyme
W113A
-
mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
additional information
-
construction of two chimeric enzymes, AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme and EA is the inverse construction, chimeric enzyme AE is activated by D-fructose 1,6-bisphosphate, D-fructose 6-phosphate and pyruvate, chimeric enzyme AE is only activated by pyruvate
additional information
-
deletion of 3,7,11, and 15 amino acids from N-terminus results in specific activites of mutants comparable to wild-type. Deletion of N-terminal 19 amino acids decreases the catalytic activity by two orders of magnitude. Coexpression of a mutant lacking N-terminal 15 amino acids and C-terminal 108 amino acids with C-terminal peptide of 108 amino acids recovers the sensitivity for allosteric effectors that is lost in the N-terminal deletion mutants that lack more than 7 amino acids
additional information
-
expression of gene in maize under control of an endosperm-specific promoter. Developing seeds show 2-4fold higher levels of enzyme activity in the presence of 5 mM phosphate. Under phosphate-inhibitory conditions, transgenic plants show increases in seed weight over the control. In transgenic plants, the seeds are fully filled, and the seed number has no significant difference from untransformed control
additional information
-
generation of pentapeptide insertions at different positions of the enzyme and analysis of proteins with homology model. Region around L102P103 is critical for allosteric regulation of the enzyme
additional information
-
mutational analysis using random mutagenesis for creation of diverse insertion, deletion and point mutations, structure-function analysis, overview, the mutant enzyme with a pentapeptide insertion between Leu102 and Pro103 is catalytically competent but insensitive to activation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
87% remaining activity of the chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, 75% remaining activity of the chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme and 60% remaining activity of wild-type enzymes
55
60
55
-
5 min 80% remaining activity of the wild-type enzyme, 98% remaining activity of the mutant enzyme D142A, 96% remaining activity of the mutant enzyme D142E, 52% remaining activity of the mutant enzyme D142N
55
-
65% remaining activity of the chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, 70% remaining activity of the chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme and 90% remaining activity of wild-type enzymes
60
-
purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, the heat treatment step of the double mutant enzyme results in 20% loss of activity
60
-
37% remaining activity of the chimeric enzyme AE contains the N-terminus of Agrobacterium tumefaciens enzyme and the C-terminus of Escherichia coli enzyme, 45% remaining activity of the chimeric enzyme EA contains the N-terminus of Escherichia coli enzyme and the C-terminus of Agrobacterium tumefaciens enzyme and 70% remaining activity of wild-type enzymes
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the irradiation of enzyme in the presence of 8-N3ATP, fructose 1,6-phosphate and Mg2+ result in the covalent modification accompanying the loss of the enzyme activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50 mM HEPES buffer, pH 8.0, 10% sucrose, 5mM MgCl2, 0.1 mM EDTA, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant enzymes, purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, but the heat treatment step of the double mutant enzyme results in 20% loss of activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bacterial glgC-TM gene, which codes for catalytically active, allosteric-insensitive enzyme, is introduced into seeds of Oryza sativa using an Agrobacterium tumefaciens-mediated transformation. The TM enzyme is expressed in the cytoplasm or amyloplast in Oryza sativa endosperm. Starch synthesis and consequently seed weight can be increased by manipulation of the cytoplasmic AGPase catalytic activity in transgenic rice
-
expression of wild-type and D142E plasmids in Escherichia coli strain BL21(DE3), expression of D142N and D142A plasmids in Escherichia coli strain AC70R1-504
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
expression of gene in maize under control of an endosperm-specific promoter. Developing seeds show 2-4fold higher levels of enzyme activity in the presence of 5 mM phosphate. Under phosphate-inhibitory conditions, transgenic plants show increases in seed weight over the control. In transgenic plants, the seeds are fully filled, and the seed number has no significant difference from untransformed control
REF.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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1989
Escherichia coli, Oryza sativa (P15280), Oryza sativa
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1984
Escherichia coli, Escherichia coli B / ATCC 11303
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1976
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1974
Escherichia coli
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263
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1988
Escherichia coli
Yung, S.G.; Preiss, J.
Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase
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151
742-749
1982
Blastochloris viridis, Escherichia coli, Rhodobacter capsulatus, Cereibacter sphaeroides, Rubrivivax gelatinosus, Rhodomicrobium vannielii, Rhodoblastus acidophilus, Rhodopila globiformis, Rhodopseudomonas palustris, Magnetospirillum fulvum, Magnetospirillum molischianum, Rhodospirillum rubrum, Rhodocyclus tenuis, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea
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147
101-109
1981
Blastochloris viridis, Escherichia coli, Rhodobacter capsulatus, Cereibacter sphaeroides, Rubrivivax gelatinosus, Rhodomicrobium vannielii, Rhodoblastus acidophilus, Rhodopila globiformis, Rhodopseudomonas palustris, Magnetospirillum fulvum, Magnetospirillum molischianum, Rhodospirillum rubrum, Rhodocyclus tenuis, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea
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
Lee, Y.M.; Mukherjee, S.; Preiss, J.
Covalent modification of Escherichia coli ADPglucose synthetase with 8-azido substrate analogs
Arch. Biochem. Biophys.
244
585-595
1986
Escherichia coli
Meyer, C.R.; Yirsa, J.; Gott, B.; Preiss, J.
A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation
Arch. Biochem. Biophys.
352
247-254
1998
Escherichia coli
Frueauf, J.B.; Ballicora, M.A.; Preiss, J.
Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli
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276
46319-46325
2001
Escherichia coli
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Characterization of Chimeric ADPglucose Pyrophosphorylases of Escherichia coli and Agrobacterium tumefaciens. Importance of the C-Terminus on the Selectivity for Allosteric Regulators
Biochemistry
41
9431-9437
2002
Agrobacterium tumefaciens, Escherichia coli
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
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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)
Meyer, C.R.; Borra, M.; Igarashi, R.; Lin, Y.S.; Springsteel, M.
Characterization of ADP-glucose pyrophosphorylase from Rhodobacter sphaeroides 2.4.1: evidence for the involvement of arginine in allosteric regulation
Arch. Biochem. Biophys.
372
179-188
1999
Anabaena sp., Escherichia coli, Cereibacter sphaeroides, Cereibacter sphaeroides (Q9RNH7)
Ko, J.H.; Kim, C.H.; Lee, D.S.; Kim, Y.S.
Purification and characterization of a thermostable ADP-glucose pyrophosphorylase from Thermus caldophilus GK-24
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319
977-983
1996
Anabaena sp., Escherichia coli, Cereibacter sphaeroides, Rhodospirillum rubrum, Thermus caldophilus, Thermus caldophilus GK-24
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An assay for adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase
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324
52-59
2004
Escherichia coli
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The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
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573
99-104
2004
Escherichia coli
Ballicora, M.A.; Iglesias, A.A.; Preiss, J.
ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
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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
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Escherichia coli
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ADPglucose pyrophosphorylases N-terminus: structural role in allosteric regulation
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343
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Escherichia coli
Ballicora, M.A.; Erben, E.D.; Yazaki, T.; Bertolo, A.L.; Demonte, A.M.; Schmidt, J.R.; Aleanzi, M.; Bejar, C.M.; Figueroa, C.M.; Fusari, C.M.; Iglesias, A.A.; Preiss, J.
Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis
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189
5325-5333
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Escherichia coli
Bejar, C.M.; Jin, X.; Ballicora, M.A.; Preiss, J.
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281
40473-40484
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Escherichia coli (P0A6V1), Escherichia coli
Hwang, S.K.; Hamada, S.; Okita, T.W.
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68
464-477
2007
Escherichia coli, Solanum tuberosum, Escherichia coli ER2566
Wang, Z.; Chen, X.; Wang, J.; Liu, T.; Liu, Y.; Zhao, L.; Wang, G.
Increasing maize seed weight by enhancing the cytoplasmic ADP-glucose pyrophosphorylase activity in transgenic maize plants
Plant Cell Tissue Organ Cult.
88
83-92
2007
Escherichia coli
-
Nagai, Y.S.; Sakulsingharoj, C.; Edwards, G.E.; Satoh, H.; Greene, T.W.; Blakeslee, B.; Okita, T.W.
Control of starch synthesis in cereals: metabolite analysis of transgenic rice expressing an up-regulated cytoplasmic ADP-glucose pyrophosphorylase in developing seeds
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50
635-643
2009
Escherichia coli, Oryza sativa
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Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli
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93
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2011
Escherichia coli
Asencion Diez, M.D.; Aleanzi, M.C.; Iglesias, A.A.; Ballicora, M.A.
A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvate
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9
e103888
2014
Escherichia coli
Hill, B.L.; Wong, J.; May, B.M.; Huerta, F.B.; Manley, T.E.; Sullivan, P.R.; Olsen, K.W.; Ballicora, M.A.
Conserved residues of the Pro103-Arg115 loop are involved in triggering the allosteric response of the Escherichia coli ADP-glucose pyrophosphorylase
Protein Sci.
24
714-728
2015
Escherichia coli
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