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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
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
ATP + alpha-D-glucose-1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
no substrate are alpha-D-mannose 1-phosphate or alpha-D-galactose 1-phosphate
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
different large subunit isoforms allow the enzyme to be efficiently regulated according to the metabolic situation and the starch necessities of a tissue. In source tissues, ADP-glucose diphosphorylase would be finely regulated by the 3-phosphoglycerate/phosphate ratio, whereas in sink tissues, the enzyme would be dependent on the availability of substrates for starch synthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
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ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
additional information
?
-
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
key regulatory enzyme of starch biosynthesis
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
different large subunit isoforms allow the enzyme to be efficiently regulated according to the metabolic situation and the starch necessities of a tissue. In source tissues, ADP-glucose diphosphorylase would be finely regulated by the 3-phosphoglycerate/phosphate ratio, whereas in sink tissues, the enzyme would be dependent on the availability of substrates for starch synthesis
-
-
?
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
first committed step in synthesis of ADP-glucose
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
ADP-Glc PPase catalyzes the first committed step in starch biosynthesis
-
-
?
additional information
?
-
-
ADP-glucose pyrophosphorylase catalyzes a rate-limiting step in starch synthesis
-
-
?
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0.019 - 0.085
alpha-D-glucose 1-phosphate
0.019 - 0.085
alpha-D-glucose 1-phosphate
0.041 - 0.083
alpha-D-glucose-1-phosphate
additional information
additional information
-
0.019
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.052
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.06
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.076
alpha-D-glucose 1-phosphate
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.085
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.067
ATP
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.094
ATP
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.42
ATP
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.57
ATP
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.019
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.052
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.06
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.076
alpha-D-glucose 1-phosphate
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.085
alpha-D-glucose 1-phosphate
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
0.041
alpha-D-glucose-1-phosphate
-
mutant A33K, pH 7.5
0.055
alpha-D-glucose-1-phosphate
-
mutant G96N, pH 7.5
0.063
alpha-D-glucose-1-phosphate
-
mutant A33K/G96N, pH 7.5
0.083
alpha-D-glucose-1-phosphate
-
wild-type, pH 7.5
0.052
ATP
-
mutant G96N, pH 7.5
0.055
ATP
-
mutant A33K/G96N, pH 7.5
0.056
ATP
-
mutant A33K, pH 7.5
0.067
ATP
pH 7.9, APS1/APL1 in presence of 0.1 mM 3-phosphoglycerate
0.073
ATP
-
wild-type, pH 7.5
0.094
ATP
pH 7.9, APS1/APL3 in presence of 2 mM 3-phosphoglycerate
0.118
ATP
pH 7.9, APS1/APL4 in presence of 1 mM 3-phosphoglycerate
0.42
ATP
pH 7.9, homotetramer APS1 in presence of 20 mM 3-phosphoglycerate
0.57
ATP
pH 7.9, APS1/APL2 in presence of 4 mM 3-phosphoglycerate
additional information
additional information
-
kinetic study
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
additional information
additional information
wild-type and mutant kinetics, forward and reverse reaction directions
-
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A114T
14% of wild-type activity
A33K
-
mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
A33K/G96N
-
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
D349N
49% of wild-type activity
G118D
43% of wild-type activity
G284D
82% of wild-type activity
G284S
109% of wild-type activity
G96N
-
mutation in leaf-specific large subunit ApL1, little effect on affinity of holoenzyme for substrates
G98E
30% of wild-type activity
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
L106F
68% of wild-type activity
L142F
83% of wild-type activity
P105S
33% of wild-type activity
R102H
30% of wild-type activity
R246Q
106% of wild-type activity
R260H
118% of wild-type activity
R306K
90% of wild-type activity
V52I
93% of wild-type activity
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
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
additional information
mutation of alpha-D-glucose 1-phosphate binding site affects APL1- and APL2-dependent activity
additional information
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
additional information
-
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
additional information
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
additional information
-
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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Li, L.; Preiss, J.
Characterization of ADPglucose pyrophosphorylase from a starch-deficient mutant of Arabidopsis thaliana
Carbohydr. Res.
227
227-239
1992
Arabidopsis thaliana
-
brenda
Zabawinski, C.; Van Den Koornhuyse, N.; D'Hulst, C.; Schlichting, R.; Giersch, C.; Delrue, B.; Lacroix, J.M.; Preiss, J.; Ball, S.
Starchless mutants of Chlamydomonas reinhardtii lack the small subunit of a heterotetrameric ADP-glucose pyrophosphorylase
J. Bacteriol.
183
1069-1077
2001
Salmonella enterica subsp. enterica serovar Typhimurium (P05415), Oryza sativa (P15280), Oryza sativa (P93430), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Anabaena sp. (P30521), Synechocystis sp. (P52415), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Chlamydomonas reinhardtii (Q42702), Chlamydomonas reinhardtii (Q9LLL6), Chlamydomonas reinhardtii, Solanum tuberosum LS2 (P55242)
brenda
Crevillen, P.; Ballicora, M.A.; Merida, A.; Preiss, J.; Romero, J.M.
The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme
J. Biol. Chem.
278
28508-28515
2003
Anabaena sp. (P30521), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Arabidopsis thaliana (P55230), Arabidopsis thaliana (P55231), Arabidopsis thaliana (Q9SIK1), Arabidopsis thaliana, Beta vulgaris (P55232), Beta vulgaris (P55233), Hordeum vulgare (O04896), Hordeum vulgare (P30524), Hordeum vulgare (P55238), Ipomoea batatas (O81274), Ipomoea batatas (Q42859), no activity in Arabidopsis thaliana, Oryza sativa (O23809), Oryza sativa (P15280), Oryza sativa (P93430), Oryza sativa (Q9ARH9), Pisum sativum (Q43815), Pisum sativum (Q43816), Pisum sativum (Q43819), Solanum lycopersicum (O04924), Solanum lycopersicum (P93229), Solanum lycopersicum (P93230), Solanum lycopersicum (Q42882), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Solanum tuberosum (P55243), Solanum tuberosum (Q00081), Solanum tuberosum LS1 (Q00081), Solanum tuberosum LS3 (P55243), Synechocystis sp. (P52415), Triticum aestivum (P12299), Triticum aestivum (P30523), Vicia faba (P52416), Vicia faba (P52417), Vicia faba SS1 (P52416), Vicia faba SS2 (P52417), Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0)
brenda
Wang, S.M.; Lue, W.L.; Yu, T.S.; Long, J.H.; Wang, C.N.; Eimert, K.; Chen, J.
Characterization of ADG1, an Arabidopsis locus encoding for ADPG pyrophosphorylase small subunit, demonstrates that the presence of the small subunit is required for large subunit stability
Plant J.
13
63-70
1998
Arabidopsis thaliana
brenda
Crevillen, P.; Ventriglia, T.; Pinto, F.; Orea, A.; Merida, A.; Romero, J.M.
Differential pattern of expression and sugar regulation of Arabidopsis thaliana ADP-glucose pyrophosphorylase-encoding genes
J. Biol. Chem.
280
8143-8149
2005
Arabidopsis thaliana
brenda
Ballicora, M.A.; Iglesias, A.A.; Preiss, J.
ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
Photosynth. Res.
79
1-24
2004
Aeromonas caviae, Agrobacterium tumefaciens, Allochromatium vinosum, Synechocystis sp., Arabidopsis thaliana, Geobacillus stearothermophilus, Bacillus subtilis, Chlamydomonas reinhardtii, [Chlorella] fusca, Chlorella vulgaris, Escherichia coli, Nostoc sp., Oryza sativa, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodocyclus purpureus, Rhodospirillum rubrum, Rhodocyclus tenuis, Serratia marcescens, Solanum tuberosum, Spinacia oleracea, Synechococcus sp., Triticum aestivum, Zea mays, Rhodobacter gelatinosa, Rhodobacter globiformis, Synechococcus sp. PCC6301
brenda
Lunn, J.E.; Feil, R.; Hendriks, J.H.; Gibon, Y.; Morcuende, R.; Osuna, D.; Scheible, W.R.; Carillo, P.; Hajirezaei, M.R.; Stitt, M.
Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana
Biochem. J.
397
139-148
2006
Arabidopsis thaliana
brenda
Chen, L.S.; Qi, Y.P.
Dithiothreitol decreases in vitro activity of ADP-glucose pyrophosphorylase from leaves of apple (Malus domestica Borkh.) and many other plant species
Phytochem. Anal.
18
300-305
2007
Arabidopsis thaliana, Glycine max, Hordeum vulgare, Malus domestica, Solanum lycopersicum, Solanum tuberosum, Sorghum sp., Spinacia oleracea, Triticum aestivum
brenda
Ventriglia, T.; Ballicora, M.A.; Crevillen, P.; Preiss, J.; Romero, J.M.
Regulatory properties of potato-Arabidopsis hybrid ADP-glucose pyrophosphorylase
Plant Cell Physiol.
48
875-880
2007
Arabidopsis thaliana, Solanum tuberosum
brenda
Obana, Y.; Omoto, D.; Kato, C.; Matsumoto, K.; Nagai, Y.; Kavakli, I.H.; Hamada, S.; Edwards, G.E.; Okita, T.W.; Matsui, H.; Ito, H.
Enhanced turnover of transitory starch by expression of up-regulated ADP-glucose pyrophosphorylases in Arabidopsis thaliana
Plant Sci.
170
1-11
2006
Arabidopsis thaliana
brenda
Georgelis, N.; Braun, E.L.; Hannah, L.C.
Duplications and functional divergence of ADP-glucose pyrophosphorylase genes in plants
BMC Evol. Biol.
8
232
2008
Arabidopsis thaliana, Chlamydomonas reinhardtii, Hordeum vulgare, Solanum lycopersicum, Oryza sativa, Physcomitrium patens, Solanum tuberosum
brenda
Ventriglia, T.; Kuhn, M.L.; Ruiz, M.T.; Ribeiro-Pedro, M.; Valverde, F.; Ballicora, M.A.; Preiss, J.; Romero, J.M.
Two Arabidopsis ADP-glucose pyrophosphorylase large subunits (APL1 and APL2) are catalytic
Plant Physiol.
148
65-76
2008
Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Arabidopsis thaliana (P55230), Arabidopsis thaliana (P55231), Arabidopsis thaliana (Q9SIK1)
brenda
Haedrich, N.; Gibon, Y.; Schudoma, C.; Altmann, T.; Lunn, J.E.; Stitt, M.
Use of TILLING and robotised enzyme assays to generate an allelic series of Arabidopsis thaliana mutants with altered ADP-glucose pyrophosphorylase activity
J. Plant Physiol.
168
1395-1405
2011
Arabidopsis thaliana (P55228), Arabidopsis thaliana
brenda
Haedrich, N.; Hendriks, J.H.; Koetting, O.; Arrivault, S.; Feil, R.; Zeeman, S.C.; Gibon, Y.; Schulze, W.X.; Stitt, M.; Lunn, J.E.
Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves
Plant J.
70
231-242
2012
Arabidopsis thaliana (P55228), Arabidopsis thaliana
brenda
Mugford, S.T.; Fernandez, O.; Brinton, J.; Flis, A.; Krohn, N.; Encke, B.; Feil, R.; Sulpice, R.; Lunn, J.E.; Stitt, M.; Smith, A.M.
Regulatory properties of ADP glucose pyrophosphorylase are required for adjustment of leaf starch synthesis in different photoperiods
Plant Physiol.
166
1733-1747
2014
Arabidopsis thaliana (P55228 and P55229)
brenda