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Information on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase and Organism(s) Zea mays and UniProt Accession P55241

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Word Map
The taxonomic range for the selected organisms is: Zea mays
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-glucose pyrophosphorylase
-
BT2
maize AGPase endosperm small subunit
SH2
maize AGPase endosperm large subunit
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
-
-
-
-
ADPGlc PPase
-
-
ADPglucose pyrophosphorylase
-
-
-
-
AGPase
Brittle-2
small subunit
SH2
large subunit
Shrunken-2
large subunit
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
nucleotidyl group transfer
SYSTEMATIC NAME
IUBMB Comments
ATP:alpha-D-glucose-1-phosphate adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-71-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
show the reaction diagram
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
-
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
show the reaction diagram
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by Mn2+, Zn2+, NH4+, Na+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
ADP-alpha-D-glucose
in wild-type, competitive with ATP, noncompetitive with glucose 1-phosphate. In chimeric mutant, competitive with ATP, mixed type inhibition with glucose 1-phosphate
ADP-glucose
-
in the presence of 3-phosphoglycerate, ADP-glucose is a competitve inhibitor with respect to ATP
Cl-
-
not at 5 mM, only at 10 mM
diphosphate
inorganic phosphate
NO3-
-
not at 5 mM, only at 10 mM
phosphate
phosphoenolpyruvate
-
-
pyruvate
-
-
Rabbit antiserum raised against spinach enzyme
-
-
-
SO42-
-
5 mM, weak
trehalose phosphate
-
-
UDP-glucose
-
-
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
3-PGA
1,6-Hexanediol bisphosphate
-
activation
2,3-diphosphoglycerate
-
no activation
2-keto-3-deoxy phosphogluconate
-
activation
2-oxobutyrate
-
slight activation, pyruvate analog
2-phospho-D-glycerate
-
no activation
3-phosphoglycerate
ADP
-
activation, less effective than 3-phosphoglycerate
ADP-glucose
-
in the absence of 3-phosphoglycerate, ADP-glucose stimulates catalytic acitvity, acting as a feedback product activator
AMP
-
activation, less effective than 3-phosphoglycerate
D-fructose
-
25 mM, 1.3fold stimulation, enzyme from maize endosperm
D-fructose 1,6-bisphosphate
D-fructose 6-phosphate
D-Glucose 1,6-bisphosphate
-
no activation
D-glucose 6-phosphate
D-ribose 5-phosphate
deoxyribose 5-phosphate
-
activation, D-fructose 6-phosphate analog
dihydroxyacetone phosphate
-
activation, less effective than 3-phosphoglycerate
fructose 6-phosphate
activation constant Ka is 0.53 for maize enzyme and 0.15 for the chimeric enzyme
fructose-6-phosphate
-
-
Fruf-beta-(2->1)-6-O-P-Glcp
-
-
glucose-6-phosphate
-
-
glyceraldehyde 3-phosphate
glycerol phosphate
-
-
Hydroxypyruvate
-
slight activation, pyruvate analog
NADPH
-
-
phosphate
-
enhances AGPase activity al low substrate concentations
phosphoenolpyruvate
pyridoxal 5'-phosphate
pyruvate
-
not
ribose-5-phosphate
-
-
sedoheptulose 1,7-diphosphate
-
activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.09
alpha-D-glucose 1-phosphate
0.09 - 0.42
ATP
0.07 - 0.48
ADP-D-glucose
0.62
ADP-glucose
-
pH 7.4, 37°C
0.017 - 11.9
alpha-D-glucose 1-phosphate
0.018 - 4
ATP
0.033 - 6.61
diphosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.17 - 59.86
alpha-D-glucose 1-phosphate
26.21 - 85
alpha-D-glucose 1-phosphate
2 - 98
ATP
additional information
additional information
-
turnover numbers for mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.83 - 20.43
phosphate
0.007 - 1.2
ADP-alpha-D-glucose
0.00038 - 0.9
diphosphate
0.44 - 9.8
phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.72
-
purified mutant Mos(1-198, 377-475) in absence of 3-phosphoglycerate
1.43
-
-
1.47
-
purified mutant Mos(1-376) in absence of 3-phosphoglycerate
1.68
-
purified mutant Mos(1-198, 430-475) in absence of 3-phosphoglycerate
1.78
-
purified mutant Mos(1-198, 377-429) in absence of 3-phosphoglycerate
1.8
-
purified mutant Mos(1-277) in absence of 3-phosphoglycerate
10.87
-
purified mutant Mos(1-198) in presence of 3-phosphoglycerate
13.1
large subunit mutant D161G, 37°C, pH 7.4
15.2
wild-type, 37°C, pH 7.4
2.45
-
purified wild-type enzyme, in absence of 3-phosphoglycerate
21.81
-
purified wild-type enzyme in presence of 3-phosphoglycerate
34
-
-
4.4
-
-
4.87
-
purified mutant Mos(1-198) in absence of 3-phosphoglycerate
41.1
-
recombinant enzyme from maize endosperm
6.14
-
purified mutant Mos(1-198, 430-475) in presence of 3-phosphoglycerate
6.81
-
purified mutant Mos(1-198, 377-429) in presence of 3-phosphoglycerate
7.29
-
purified mutant Mos(1-277) in presence of 3-phosphoglycerate
7.8
large subunit mutant D161G, 55°C, pH 7.4
8.59
-
purified mutant Mos(1-198, 377-475) in presence of 3-phosphoglycerate
9.38
-
purified mutant Mos(1-376) in presence of 3-phosphoglycerate
additional information
-
leaf metabolites of wild-type and transgenic wheat plants
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
activity assay
7 - 7.5
-
ADP-glucose synthesis, Tris buffer
7 - 8
-
ADP-glucose synthesis, HEPES buffer
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.3
-
about half-maximal activity at pH 6.0 and 8.3, Tris buffer
6.1 - 8.5
-
about half-maximal activity at pH 6.1 and about 80% of maximal activity at pH 8.5, HEPES buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.02
-
ADP-glucose pyrophosphorylase B
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Bt2a, transcript coding for the cytoplasmic isoform, almost exclusively expressed in the developing endosperm
Manually annotated by BRENDA team
of endosperm, enzyme small subunit Bt2
Manually annotated by BRENDA team
Bt2a, alternative transcript coding for a plastidial isoform
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
ADP-glucose pyrophosphorylase catalyzes the rate-limiting step in starch biosynthesis
malfunction
a 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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLGL1_MAIZE
516
0
57071
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
210000 - 240000
-
-
220000
-
gel filtration
230000
-
gel filtration
235000
-
enzyme B, gel filtration
237000 - 253000
-
sucrose density gradient centrifugation
375000
-
enzyme A, gel filtration
400000
-
enzyme A, PAGE
54000
-
4 * 54000 SDS-PAGE
96000
-
4 * 96000, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
consists of two small and two large subunits, BT2/SH2
heterotetramer
homotetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A508S
large subunit mutation
C114A
large subunit mutation
C382F
large subunit mutation
C424V
large subunit mutation
D368S
large subunit mutation
E438Q
large subunit mutation
H149S
large subunit mutation
M172T
large subunit mutation
P372A
large subunit mutation
Q213H
large subunit mutation
S163F
large subunit mutation
T361C
large subunit mutation
V227R
large subunit mutation
V502T
large subunit mutation
bt2-H2328
mutant, an insertion is located in exon 6 of the Bt2 gene generating a 9-bp duplication of bases TGATGTGAC, position 4,422 - 4,431, a comparative transcriptome analysis of wild-type and bt2-H2328 kernels at mid-development leads to the conclusion that the lack of Bt2-encoded AGPase triggers large-scale changes on the transcriptional level that concern mainly genes involved in carbohydrate or amino acid metabolic pathways
D161G
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme
F332S
-
site-directed mutagenesis in the potato part of the chimeric mutant
H333T
-
Sh2hs33, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 76% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2, enhanced subunit interaction in this mutant
H333T/T460I
-
Sh2hs40, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 72% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
H341Y
-
site-directed mutagenesis in the potato part of the chimeric mutant
I323V
-
site-directed mutagenesis in the potato part of the chimeric mutant
L38E
-
UpReg-1, this mutation greatly increases activation by 3-phosphoglycerate
L93Thr
-
Sh2-UR1, this mutation does not alter 3-phosphoglycerate activation and phosphate inhibition
N369H
-
site-directed mutagenesis in the potato part of the chimeric mutant
Q96G/D161G/A443R
large subunit mutant isolated by iterative saturation mutagenesis to improve heat stability of the enzyme. Mutant additionally shows an increase affinity for activator 3-phosphoglyceric acid
R104A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R104T
-
Sh2hs16, coexpression with wild-type Brittle2: 5 min 60°C heat treatment, 37% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R107A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R116A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R146A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R217P/H333T
-
Sh2hs47, coexpression with wild-type Brittle2: 5min 60°C heat treatment, about 65% remaining activity in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
R340A
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R381A
-
large subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
R77K
-
small subunit mutant, several arginine side chains contact the bound sulfate ions in the potato structure and likely play important roles in allosteric effector binding, mutagenesis is applied to the corresponding Arg residues of AGPase in maize
S34E/Y36C
-
significant increase in heat stability as compared to wild-type enzyme
S34Q/Y36C
-
significant increase in heat stability as compared to wild-type enzyme. The ratio of turnover-number to KM-value for ATP is 2.1fold higher than wild-type ratio, the ratio of turnover-number to KM-value for alpha-D-glucose 1-phosphate is 2.6fold higher than wild-type ratio
T462I
-
random mutagenesis, small subunit mutant BT2-TI, BT2-TI exhibits enhanced heat stability compared to wildtype maize endosperm AGPase
V347M
-
site-directed mutagenesis in the potato part of the chimeric mutant
Y36C
-
significant increase in heat stability as compared to wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53
-
half-lives of wild-type and mutant enzymes lay between 2 and 16 min, overview
55
wild-type, complete loss of activity
60
-
76% remaining activity of mutant enzyme Sh2hs33 in comparison to the 26% remaining activity of wild-type Shrunken2/Brittle2
additional information
-
ATP and ADP-Glc, but not Glc-1-P and diphosphate, protect AGPase from thermal inactivation, 3-PGA acts synergistically, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes the purified enzyme at 0.5 mg/ml
-
freeze-thawing reduces activity by 70%, high ionic strength, ATP and Mg2+ stabilize
-
phosphate, in the absence of 3-PGA, stabilizes endosperm AGPase
-
PMSF and chymostatin prevent proteolysis during purification, not p-aminobenzamidine, N-alpha-p-tosyl-L-lysine chloromethylketone, NEM, PCMB, benzamidine, leupeptin, pepstatin or EDTA
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 60% (NH4)2SO4, 15 weeks
-
-80°C, majority of activity is retained for several months, recombinant enzyme from maize and mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by protamine sulfate and ammonium sulfate fractionation, followed by anion-exchange and affinity chromatography
endosperm
-
isozyme A
-
recombinant enzyme
-
recombinant mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber
-
recombinant wild-type and mutant AGPases using protamine sulfate and ammonium sulfate fractionation, followed by ion exchange and hydroxyapatite chromatography
-
whole kernels
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for expression in Escherichia coli AC70R1-504 cells
altered AGP large subunit (Sh2r6hs) from maize containing two alterations relative to the wild-type maize Sh2 sequence is introduced into wheat. The rev6 alteration confers reduced phosphate inhibition and decreased heat stability in maize and the hs alteration increases AGP subunit interactions and enzyme stability in Escherichia coli. Low-level expression of Sh2r6hs under control of the maize Sh2 promoter increases yield in wheat
-
DNA and amino acid sequence determination and analyis, expression analysis, sequence comparison and phylogenetic analysis: two paralogous genes encoding small subunits of AGPase in maize, Bt2 and L2, replace the single alternatively spliced gene found in other cereal species, overview
DNA and amino acid sequence determination and analyis, expression analysis, sequence comparison and phylogenetic analysis: two paralogous genes encoding small subunits of AGPase in maize, Bt2 and L2, replace the single alternatively spliced gene found in other cereal species, overview, Bt2 has arised as a result of the tetraploidization of the maize genome
DNA and amino acid sequence determination and analyis, expression analysis, sequence comparison and phylogenetic analysis: two paralogous genes encoding small subunits of AGPase in maize, Bt2 and L2, replace the single alternatively spliced gene found in other cereal species, overview, L2 has arised as a result of the tetraploidization of the maize genome
expression in Escherichia coli
expression in Escherichia coli AC70R1-504
-
expression of maize large subunit mutant Sh2r6hs in Triticum aestivum endosperm under control of the maize Sh2 promoter, plants are grown from F2 derived F3 seeds of crosses between Sh2r6hs expressing lines 161-12 or GS8 and their parent variety Hi-Line
-
expression of the wild-type and mutant enzymes in Escherichia coli, Shrunken2, Sh2 encodes the large subunit and Brittle2, Bt2 encodes the small subunit, cloning and expression of the heat-stable variant Sh2hs33 and Bt2 in the yeast two-hybrid expression system
-
expression of wild-type and mutant AGPases in Escherichia coli strain AC70R1-504, wild-type BT2 and mutant BT2-TI show very low expression levels, overview
-
for expression in Escherichia coli AC70R1-504 cells
-
mosaic AGPases derived from protein motifs normally expressed in the Zea mays endosperm and the Solanum tuberosum tuber, expression in Escherichia coli
-
survey of plant species and tissues from which cDNA sequences encoding the small and large subunit of ADPG pyrophosphorylase are available
-
the flanking sequences of the mutant bt2-H2328 are cloned and sequenced
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Amir, J.; Cherry, J.H.
Purification and properties of adenosine diphosphoglucose pyrophosphorylase from sweet corn
Plant Physiol.
49
893-897
1972
Zea mays
Manually annotated by BRENDA team
Plaxton, W.C.; Preiss, J.
Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm
Plant Physiol.
83
105-112
1987
Zea mays
Manually annotated by BRENDA team
Fuchs, R.L.; Smith, J.D.
The purification and characterization of ADP-glucose pyrophosphorylase A from developing maize seeds
Biochim. Biophys. Acta
566
40-48
1979
Zea mays
Manually annotated by BRENDA team
Hannah, L.C.; Nelson, O.E.
Characterization of adenosine diphosphate glucose pyrophosphorylases from developing maize seeds
Plant Physiol.
55
297-302
1975
Zea mays
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Greene, T.W.; Hannah, L.C.
Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
Proc. Natl. Acad. Sci. USA
95
13342-13347
1998
Zea mays
Manually annotated by BRENDA team
Salamone, P.R.; Greene, T.W.; Kavakli, I.H.; Okita, T.W.
Isolation and characterization of a higher plant ADP-glucose pyrophosphorylase small subunit homotetramer
FEBS Lett.
482
113-118
2000
Zea mays, Escherichia coli (P0A6V1), Escherichia coli, Solanum tuberosum (P23509), Solanum tuberosum, Anabaena sp. (P30521), Synechocystis sp. (P52415), Solanum tuberosum SS (P23509)
Manually annotated by BRENDA team
Burger, B.T.; Cross, J.M.; Shaw, J.R.; Caren, J.R.; Greene, T.W.; Okita, T.W.; Hannah, L.C.
Relative turnover numbers of maize endosperm and potato tuber ADP-glucose pyrophosphorylases in the absence and presence of 3-phosphoglyceric acid
Planta
217
449-456
2003
Oryza sativa, Solanum tuberosum, Zea mays
Manually annotated by BRENDA team
Smidansky, E.D.; Martin, J.M.; Hannah, L.C.; Fischer, A.M.; Giroux, M.J.
Seed yield and plant biomass increases in rice are conferred by deregulation of endosperm ADP-glucose pyrophosphorylase
Planta
216
656-664
2003
Oryza sativa, Zea mays
Manually annotated by BRENDA team
Johnson, P.E.; Patron, N.J.; Bottrill, A.R.; Dinges, J.R.; Fahy, B.F.; Parker, M.L.; Waite, D.N.; Denyer, K.
A low-starch barley mutant, riso 16, lacking the cytosolic small subunit of ADP-glucose pyrophosphorylase, reveals the importance of the cytosolic isoform and the identity of the plastidial small subunit
Plant Physiol.
131
684-696
2003
Triticum aestivum (P30523), Hordeum vulgare (P55238), Hordeum vulgare (Q8HS72), Hordeum vulgare, Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0), Oryza sativa (Q9ARH9)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Boehlein, S.K.; Sewell, A.K.; Cross, J.; Stewart, J.D.; Hannah, L.C.
Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics
Plant Physiol.
138
1552-1562
2005
Solanum tuberosum, Zea mays
Manually annotated by BRENDA team
Linebarger, C.R.; Boehlein, S.K.; Sewell, A.K.; Shaw, J.; Hannah, L.C.
Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N-terminus of the small subunit
Plant Physiol.
139
1625-1634
2005
Zea mays
Manually annotated by BRENDA team
Meyer, F.D.; Smidansky, E.D.; Beecher, B.; Greene, T.W.; Giroux, M.J.
The maize Sh2r6hs ADP-glucose pyrophosphorylase (AGP) large subunit confers enhanced AGP properties in transgenic wheat (Triticum aestivum)
Plant Sci.
167
899-911
2004
Zea mays
Manually annotated by BRENDA team
Roesti, S.; Denyer, K.
Two paralogous genes encoding small subunits of ADP-glucose pyrophosphorylase in maize, Bt2 and L2, replace the single alternatively spliced gene found in other cereal species
J. Mol. Evol.
65
316-327
2007
Zea mays, Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0)
Manually annotated by BRENDA team
Smidansky, E.D.; Meyer, F.D.; Blakeslee, B.; Weglarz, T.E.; Greene, T.W.; Giroux, M.J.
Expression of a modified ADP-glucose pyrophosphorylase large subunit in wheat seeds stimulates photosynthesis and carbon metabolism
Planta
225
965-976
2007
Zea mays
Manually annotated by BRENDA team
Slewinski, T.L.; Ma, Y.; Baker, R.F.; Huang, M.; Meeley, R.; Braun, D.M.
Determining the role of Tie-dyed1 in starch metabolism: epistasis analysis with a maize ADP-glucose pyrophosphorylase mutant lacking leaf starch
J. Hered.
99
661-666
2008
Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined
Plant Physiol.
146
289-299
2008
Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase
Plant Physiol.
149
318-326
2008
Solanum tuberosum, Zea mays
Manually annotated by BRENDA team
Georgelis, N.; Hannah, L.C.
Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant
Plant Sci.
175
247-254
2008
Zea mays
Manually annotated by BRENDA team
Cossegal, M.; Chambrier, P.; Mbelo, S.; Balzergue, S.; Martin-Magniette, M.L.; Moing, A.; Deborde, C.; Guyon, V.; Perez, P.; Rogowsky, P.
Transcriptional and metabolic adjustments in ADP-glucose pyrophosphorylase-deficient bt2 maize kernels
Plant Physiol.
146
1553-1570
2008
Zea mays (Q947C0), Zea mays
Manually annotated by BRENDA team
Georgelis, N.; Shaw, J.R.; Hannah, L.C.
Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme
Plant Physiol.
151
67-77
2009
Solanum tuberosum (Q00081), Zea mays (P55241), Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Hannah, L.C.
Studies of the kinetic mechanism of maize endosperm ADP-glucose pyrophosphorylase uncovered complex regulatory properties
Plant Physiol.
152
1056-1064
2010
Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Hannah, L.C.; Stewart, J.D.
Probing allosteric binding sites of the maize endosperm ADP-glucose pyrophosphorylase
Plant Physiol.
152
85-95
2010
Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Hwang, S.K.; Stewart, J.D.; Curtis Hannah, L.
Deciphering the kinetic mechanisms controlling selected plant ADP-glucose pyrophosphorylases
Arch. Biochem. Biophys.
535
215-226
2013
Solanum tuberosum, Zea mays (Q947C0 and P55241), Zea mays
Manually annotated by BRENDA team
Boehlein, S.K.; Shaw, J.R.; Stewart, J.D.; Sullivan, B.; Hannah, L.C.
Enhancing the heat stability and kinetic parameters of the maize endosperm ADP-glucose pyrophosphorylase using iterative saturation mutagenesis
Arch. Biochem. Biophys.
568
28-37
2015
Zea mays (Q947C0 and P55241), Zea mays
Manually annotated by BRENDA team