2.7.7.27: glucose-1-phosphate adenylyltransferase
This is an abbreviated version!
For detailed information about glucose-1-phosphate adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.27
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2.7.7.27
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starch
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endosperm
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potato
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grain
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maize
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glycogen
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tuber
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wheat
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3-phosphoglycerate
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tuberosum
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sink
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amylose
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plastid
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solanum
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invertase
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granule-bound
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heterotetrameric
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kernel
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plastidial
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ppases
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amylopectin
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orthophosphate
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sh2
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phosphoglucomutase
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debranching
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amyloplasts
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grain-filling
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waxy
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starchless
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source-sink
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biotechnology
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anthesis
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agriculture
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endosperm-specific
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spikelets
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synthesis
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isoamylase
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pyrophosphorolysis
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fructose-1,6-bisphosphate
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photosynthate
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photoassimilate
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pullulanase
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starch-branching
- 2.7.7.27
- starch
- endosperm
- potato
- grain
- maize
- glycogen
- tuber
- wheat
- 3-phosphoglycerate
- tuberosum
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sink
- amylose
- plastid
- solanum
- invertase
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granule-bound
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heterotetrameric
- kernel
- plastidial
- ppases
- amylopectin
- orthophosphate
- sh2
- phosphoglucomutase
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debranching
- amyloplasts
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grain-filling
-
waxy
-
starchless
-
source-sink
- biotechnology
-
anthesis
- agriculture
-
endosperm-specific
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spikelets
- synthesis
- isoamylase
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pyrophosphorolysis
- fructose-1,6-bisphosphate
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photosynthate
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photoassimilate
- pullulanase
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starch-branching
Reaction
Synonyms
adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase, adenosine 5'-diphosphate glucose pyrophosphorylase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, adenosine-5'-diphosphoglucose pyrophosphorylase, adenylyltransferase, glucose 1-phosphate, ADG2, ADP glucose pyrophosphorylase, ADP-Glc PPase, ADP-Glc pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADPGlc PPase, ADPglucose pyrophosphorylase, AGP, AGP-S, AGP1, AGP2, AGPase, AGPL2, AGPS, AGPS1, AGPS2b, APS1, Brittle-2, BT2, GlgC, GlgD, OtaL, OtaS, SH2, Shrunken-2
ECTree
2.7.7.27 glucose-1-phosphate adenylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H379K
site-directed mutagenesis, kinetics compared to the wild-type enzyme
H379R
site-directed mutagenesis, kinetics compared to the wild-type enzyme
A33K
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mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
A33K/G96N
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mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates. Double mutant is less susceptible for inhibition by phosphate and shows increased sensitivity to 3-phosphoglycerate
C81S
mutation in small subunit APS1. Substitution of Cys81 by serine prevents small subunit APS1 dimerization. Cys81 is both necessary and sufficient for dimerization of APS1. Compared to control plants, the C81S lines have higher levels of ADP-glucose and maltose, and either increased rates of starch synthesis or a starch-excess phenotype, depending on the daylength. APS1 protein levels are five- to tenfold lower than in control plants
G96N
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mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
K267R
site-directed mutagenesis, co-expression of the wild-type APS1 subunit with mutated APL2K267R subunit produces enzymes with altered alpha-D-glucose-1-phosphate S0.5
K271R
site-directed mutagenesis, co-expression of the wild-type APS1 subunit with mutated APL1K71R subunit produces enzymes with altered alpha-D-glucose-1-phosphate S0.5
R22A
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about 15fold decrease in apparent affinity for fructose 6-phosphate compared to that of wild-type
R33A
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mutant enzyme is insensitive to activation by fructose 6-phosphate
R8A
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mutant enzyme exhibits reduced fold-activation by fructose 6-phosphate compared to that of wild-type but increased apparent affinity for ATP in the presence of fructose 6-phosphate
D142A
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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
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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
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
G336D
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a higher activity enzyme form, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
K195Q
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
LP17L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP26L
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site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
LP44E
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44K
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44R
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44S
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP44Y
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP55L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
LP66L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
P103A
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mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
P295D
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extremely high activity in the absence of fructose 1,6-bisphosphate, 20fold decreased affinity for AMP than wild-type enzyme
P295D/G336D
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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
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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
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3.4fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
P295Q
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3.8fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme
Q106A
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mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R107A
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mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
R115A
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mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
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
W113A
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
Y114A
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mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate
Y216F
residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis
LP17L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
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LP26L
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site-directed mutagenesis, the mutant shows slightly reduced catalytic efficiency compared to the wild-type enzyme
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LP44L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
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LP55L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
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LP66L
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site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type enzyme
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A171V
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mutation in large subunit gene AGPL2. Seeds of mutant plants are severely shriveled and have seed weight and starch content comparable with the shriveled seeds from AGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme are significantly impaired, showing lower specific activities and affinities for the activator 3-phosphoglycerate
T139I
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mutation in large subunit gene AGPL2. Seeds of mutant plants are severely shriveled and have seed weight and starch content comparable with the shriveled seeds from AGPL2 null mutants. The catalytic and allosteric regulatory properties of the mutant enzyme are significantly impaired, showing lower specific activities and affinities for the activator 3-phosphoglycerate
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
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
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
H341Y
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site-directed mutagenesis in the potato part of the chimeric mutant
I323V
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site-directed mutagenesis in the potato part of the chimeric mutant
K41R
K41R/T51K
L46F
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mutation of small subunit, coexpression with mutation P52L of large subunit, partly restores sensitivity to 3-phosphoglycerate
L48F/V59I
TG-15, significant alteration in effector sensitivity of this homotetrameric enzyme in comparison to wild-type heterotetrameric enzyme
LSH342A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSH89A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI330K
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI335R
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSI339A/I330A
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large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSK334A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSK336A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN102A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSN87A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSP327A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR45A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSR88A
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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
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large subunit mutant, substitution of critical amino acids regarding the formation of the native heterotetrameric enzyme
LSW135A
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large subunit mutant, substitution of a critical amino acid regarding the formation of the native heterotetrameric enzyme
LSW135R
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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
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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
Q127M
mutation in ATP binding region of large subunit, kinetic analysis
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
T129V
mutation in ATP binding region of large subunit, kinetic analysis
T129V/A132V
mutation in ATP binding region of large subunit, kinetic analysis
T51K
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
L48F/V59I
-
TG-15, significant alteration in effector sensitivity of this homotetrameric enzyme in comparison to wild-type heterotetrameric enzyme
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H145G/A325V
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mutant shows UDP-N-acetylglucose pyrophosphorylase activity. Residue A325 is associated with sugar binding
H145G/A325V
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mutant shows UDP-N-acetylglucose pyrophosphorylase activity. Residue A325 is associated with sugar binding
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bt2-H2328
mutant, an insertion is located in exon 6 of the Bt2 gene generating a 9-bp duplication of bases TGATGTGAC, position 4,422 - 4,431, a comparative transcriptome analysis of wild-type and bt2-H2328 kernels at mid-development leads to the conclusion that the lack of Bt2-encoded AGPase triggers large-scale changes on the transcriptional level that concern mainly genes involved in carbohydrate or amino acid metabolic pathways
D161G
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme
H333T
-
Sh2hs33, coexpression with wild-type Brittle2: 5 min 60ยฐC heat treatment, 76% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2, enhanced subunit interaction in this mutant
H333T/T460I
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Sh2hs40, coexpression with wild-type Brittle2: 5 min 60ยฐC heat treatment, 72% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
L93Thr
-
Sh2-UR1, this mutation does not alter 3-phosphoglycerate activation and phosphate inhibition
Q96G/D161G/A443R
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme. Mutant additionally shows an increase affinity for activator 3-phosphoglyceric acid
R104A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R104T
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Sh2hs16, coexpression with wild-type Brittle2: 5 min 60ยฐC heat treatment, 37% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R107A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R116A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R146A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R217P/H333T
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Sh2hs47, coexpression with wild-type Brittle2: 5min 60ยฐC heat treatment, about 65% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R340A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R381A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R77K
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
S34Q/Y36C
-
significant increase in heat stability as compared to wild-type enzyme. The ratio of turnover-number to KM-value for ATP is 2.1fold higher than wild-type ratio, the ratio of turnover-number to KM-value for alpha-D-glucose 1-phosphate is 2.6fold higher than wild-type ratio
T462I
-
random mutagenesis, small subunit mutant BT2-TI, BT2-TI exhibits enhanced heat stability compared to wildtype maize endosperm AGPase
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
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
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
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
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
site-directed mutagenesis of conserved glycines in this region, G20, G21, and G23, results in substantial loss of activity
additional information
-
site-directed mutagenesis of conserved glycines in this region, G20, G21, and G23, results in substantial loss of activity
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
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
additional information
-
coexpression of the small subunit APS1 with the different large subunits APL1, APL2, APL3 and APL4, results in heterotetramers with different regulatory and kinetic properties, APS1/APL1 shows the highest affinity for the substrates and the highest sensitivity to the allosteric effectors
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 T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
construction of a T-DNA mutant of APS1, aps1, that is starchless, lacks ADP-Glc PPase activity, APS1 mRNA, and APS1 protein, and is late flowering in long days. Transgenic lines of the aps1 mutant, expressing an inactivated form of APS1, recovered the wild-type phenotype, indicating that APL1 and APL2 have catalytic activity and may contribute to ADP-Glc synthesis in planta
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
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mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
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complementation of an aps1 null mutant with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues is replaced by serine. Substitution of Cys81 by serine prevents small subunit APS1 dimerization, whereas mutation of the other cysteines had no effect
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complementation of an aps1 null mutant with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues is replaced by serine. Substitution of Cys81 by serine prevents small subunit APS1 dimerization, whereas mutation of the other cysteines had no effect
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use of TILLING, i.e.Targeting Induced Local Lesions IN Genomes, of a chemically mutagenised population of plants to identify novel mutations in the APS1 gene, and high throughput measurements using a robotised cycling assay
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use of TILLING, i.e.Targeting Induced Local Lesions IN Genomes, of a chemically mutagenised population of plants to identify novel mutations in the APS1 gene, and high throughput measurements using a robotised cycling assay
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enzyme inactivation mutant results in complete loss of glycogen in all media tested and a distinct lag phase upon inoculation of cells in minimal medium containing 750 mM NaCl. Inactivation does not affect survival of cells in stationary phase or its glutamate and lysine production
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enzyme inactivation mutant results in complete loss of glycogen in all media tested and a distinct lag phase upon inoculation of cells in minimal medium containing 750 mM NaCl. Inactivation does not affect survival of cells in stationary phase or its glutamate and lysine production
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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
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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
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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
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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
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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
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Escherichia coli mutant glgC gene, glgC16, encodes a highly active and allosterically insensitive AGPase, developing seeds from transgenic maize plants show up to 2-4-fold higher levels of AGPase activity in the presence of phosphate, phenotype, overview
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Escherichia coli mutant glgC gene, glgC16, encodes a highly active and allosterically insensitive AGPase, developing seeds from transgenic maize plants show up to 2-4-fold higher levels of AGPase activity in the presence of phosphate, phenotype, overview
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generation of transgenic plants bearing antisense DNA of enzyme small subunit FagpS. Most transgenic fruit do not show differences in weight and hardness, but starch content in fruit is decreased to 27-47% and total soluble sugar content is increased to 16-37% compared to control. Sugar contents are particularly higher in the red stage of fruit. In other tissues, FagpS expression levle is similar to wild-type
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in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
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in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
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in mutant Riso 16, the Hv.AGP.S.1. gene is substantially deleted and therefore inactive and lacks the cytosolic small subunit of enzyme in the endosperm and cytosolic enzyme activity, the Hv.AGP.S.2. gene is not affected in Riso and it has a normal plastidial enzyme activity
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AGP-antisense plants show flowers with abnormal petal limbs due to the early termination of the expansion growth of the petal limbs between the corolla lobes, the cell expansion is limited in NtAGP-antisense plants but cell numbers remained unchanged. Enzyme mRNA levels and starch content in the sepal tissues of AGP-antisense plants are reduced, resulting in significantly lower levels of sugars, sucrose, glucose, and fructose, in the petal limbs. The feeding of these sugars to flower buds of the AGP-antisense plants restores the expansion growth in the limb area between the corolla lobes, which is severely arrested in ยXanthiย flowers from which sepals are removed
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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lesions in the cytosolic enzyme isoforms small subunit OsAGPS2b, or large subunit OsAGPL2, cause a shrunken endosperm due to a remarkable reduction in starch synthesis. During vegetative growth, the osagps2 mutant is indstinguishable from wild-type
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagpl2 mutants, subcellular localization, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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isolation of osagps2 mutants, subcellular localization, expression analysis in different tissues, the mutant plants show reduced starch content, phenotypes, overview
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mutant apl1 of rice with a Tos17 insertion and lacking the leaf large subunit of ADP-glucose pyrophosphorylase has drastically reduced leaf starch content but grows normally, phenotype, overview
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tomato plants harboring the gene AgpL1 for ADP-glucose pyrophosphorylase large subunit from wild species Solanum habrochaites show an increase in enzyme activity correlating with a prolonged expression of the L1 protein. The small subunit also remains for an extended period of fruit development due to prolonged stability of the heterotetramer in presence of the L1 protein. Mature fruit show an increased starch content and higher soluble solids
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expression of the large subunit isoforms L1 to L3 in Escherichia coli, in conjunction with small subunit S and individually and kinetic characterisation of the L1/S and L3/S heterotetramers. The recombinant L3 subunit is also active when expressed alone
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expression of the large subunit isoforms L1 to L3 in Escherichia coli, in conjunction with small subunit S and individually and kinetic characterisation of the L1/S and L3/S heterotetramers. The recombinant L3 subunit is also active when expressed alone
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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
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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
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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
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construction of a LRKNSWT heterotetramer, the LS mutant homotetramer LRKN is catalytically very inefficient, binds ATP less efficiently, and is less heat-stable, overview
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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
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construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
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the modified maize AGP large subunit sequence Sh2r6hs encodes a subunit with increased AGP activity leading to plants with increased seed yield, and plant size, phenotypes of transgenic plants, overview
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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
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expression of maize Sh2r6hs transgene, a modified maize Sh2 cDNA coding sequence with alterations conferring reduced sensitivity to phosphate inhibition and greater heat stability, in Triticum aestivum results in increased photosynthetic rates under high light but not low light conditions, peaking at 7 days after flowering. Transgenic plants show increases in levels of fructose, glucose, and sucrose in flag leaves at 7 and 14 days after flowering
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expression of the maize/potato small subunit mosaic mutant MP, Mos(1-198), containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, Mos(1-198) and its derivatives are expressed exclusively with the wild-type maize large subunit, SH2. In the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglycerate, enzymatic activity in the absence of 3-phosphoglycerate is substantially 2-5fold higher than that of wild-type enzyme, while in presence of 3-phosphoglycerate, Mos(1-198) AGPase activity is actually less than that of wild-type enzyme, phenotype, mutant Mos(1-198) naturally occurs in a semiactivated state in the absence of an activator, overview. Mutational exchange of carboxylterminal region containing 15 polymorphic amino acids from 377 to 475 to create Mos(1-198, 430-475) and Mos(1-198, 377-429) leading to reduced enzyme activity independent of 3-phosphoglycerate. Constructed mutant Mos(1-277) exhibits 3-phosphoglycerate-independent activity that is less than mutant Mos(1-198) and wild-type activity. Mutant Mos(1-321) has no detectible activity in the absence of 3-phosphoglycerate. In the presence of 3-phosphoglycerate however, Mos(1-321) activity in the reverse direction is identical to that of Mos(1-277), overview
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heat-stable small subunit variant MP is composed of sequences from the maize endosperm and the potato tuber small subunit, construction of a double mutant MP-TI, which may lead to increased starch yield when expressed in monocot endosperms
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identification of a mutant allele of the leaf-expressed small subunit of ADP-glucose pyrophosphorylase agps-m1, the AGPase mutant is unable to synthesize transitory starch and lacks leaf starch, phenotype, overview
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mutant Sh2r6hs, expressed in transgenic wheat plants, shows increases in ADP-glucose, UDP-glucose, and fructose at maturity , phenotype, overview
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construction of a hybrid AGPase composed of portions from the maize endosperm and the potato tuber AGPases in the small subunit paired with a wild-type maize large subunit. The chimeric maize/potato heat stable enzyme lacks the cysteine responsible for redox changes
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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
