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Information on EC 2.7.7.27 - glucose-1-phosphate adenylyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SIK1
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2.7.7.27 glucose-1-phosphate adenylyltransferaseSpecify your search results
Word Map
- 2.7.7.27
- starch
- endosperm
- potato
- grain
- maize
- glycogen
- tuber
- wheat
- 3-phosphoglycerate
- tuberosum
-
sink
- amylose
- plastid
- solanum
- invertase
-
granule-bound
-
heterotetrameric
- kernel
- plastidial
- ppases
- amylopectin
- orthophosphate
- sh2
- phosphoglucomutase
-
debranching
- amyloplasts
-
grain-filling
-
waxy
-
starchless
-
source-sink
- biotechnology
-
anthesis
- agriculture
-
endosperm-specific
-
spikelets
- synthesis
- isoamylase
-
pyrophosphorolysis
- fructose-1,6-bisphosphate
-
photosynthate
-
photoassimilate
- pullulanase
-
starch-branching
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
adp-glucose pyrophosphorylase, agpase, adpglucose pyrophosphorylase, adp glucose pyrophosphorylase, shrunken-2, adp-glc ppase, adp-glc pyrophosphorylase, brittle-2, adp-glucose synthetase, adenosine diphosphate glucose pyrophosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-diphosphate glucose pyrophosphorylase
-
-
-
-
adenosine diphosphate glucose pyrophosphorylase
-
-
-
-
adenosine diphosphoglucose pyrophosphorylase
-
-
-
-
adenylyltransferase, glucose 1-phosphate
-
-
-
-
ADP glucose pyrophosphorylase
-
-
-
-
ADP-glucose pyrophosphorylase
ADP-glucose synthase
-
-
-
-
ADP-glucose synthetase
-
-
-
-
ADPG pyrophosphorylase
-
-
-
-
ADPglucose pyrophosphorylase
-
-
-
-
AGPase
APS1
ADP-glucose pyrophosphorylase
-
-
-
-
AGPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:alpha-D-glucose-1-phosphate adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9027-71-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
diphosphate + ADP-glucose
-
-
?
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
ATP + alpha-D-glucose 1-phosphate
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-D-glucose 1-phosphate
ADP-D-glucose + diphosphate
-
-
-
r
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1
dithiothreitol
-
in presence of 3-phophoglycerate, decrease of acitivity
phosphate
kinetic study and comparison of activation of recombinant enzymes, the inhibition is more drastic for recombinant enzyme APS1/APL1
phosphate
-
wild-type, 50% inhibition at 0.044 mM, mutant A33K, 50% inhibition at 0.043 mM, mutant G96N, 50% inhibition at 0.054 mM, mutant A33K/G96N, 50% inhibition at 0.268 mM, all in presence of 3-phosphoglycerate in at concentration of halfmaximal activation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-phosphoglycerate
kinetic study and comparison of activation of recombinant enzymes, the activation is more drastic for recombinant enzyme APS1/APL1
3-phosphoglycerate
kinetic study and comparison of activation of recombinant enzymes, the activation is more drastic for recombinant enzyme APS1/APL1
3-phosphoglycerate
-
generation of hybrid enzymes using Solanum tuberosum large subunit and Arabidopsis thaliana small subunit. Hybrid potato small subunit with Arabidopsis large subunit APL1 is extremely sensitive against 3-phosphoglycerate and phosphate, while hybrid potato small subunit with Arabidosis large subunit APL2 is rather insensitive to both
3-phosphoglycerate
-
wild-type, half-maximal activation at 0.016 mM, mutant A33K, at 0.0055 mM, mutant G96N, at 0.0064 mM, mutant A33K/G96N, at 0.0066 mM
3-phosphoglycerate
-
in leaves 2fold, DTT abolishes the activation at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.118
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
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
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16
recombinant enzyme, homotetramer APS1
17
recombinant enzyme APS1 plus APL4
2.5
recombinant enzyme APS2 plus APL3
3.7
recombinant enzyme APS2 plus APL1
5
recombinant enzyme APS1 plus APL2
0.0021
wild-type APS1, forward reaction
16
recombinant enzyme, homotetramer APS1
17
recombinant enzyme APS1 plus APL4
2.5
recombinant enzyme APS2 plus APL3
3.7
recombinant enzyme APS2 plus APL1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
APL4; two genes encode small subunits APS1 and APS2, and four large subunits APL1-APL4
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
ApL1, ApL2 and ApL3 transcripts are localized in the mesophyll and vasular companion cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
adjustment of starch synthesis to daylength was compromised in plants expressing a deregulated bacterial AGPase in place of the endogenous AGPase and in plants containing mutant forms of the endogenous AGPase with altered allosteric regulatory properties. If growth at night is low, as in short days, there is a delay before growth recovers during the next day, leading to accumulation of sucrose and stimulation of starch synthesis via activation of AGPase. If growth at night is fast, photosynthate is used for growth at the start of the day, sucrose does not accumulate, and starch synthesis is not upregulated
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLGL4_ARATH
523
0
58205
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
heterotetramer alpha2beta2 consisting of two small and two large subunits, APL1 and APL2, besides their regulatory role, have catalytic activity
heterotetramer
tetramer
additional information
tetramer
-
AGPase is a heterotetramer comprised of two identical large and two identical small subunits in plants
tetramer
heterotetramer alpha2beta2 consisting of two small and two large subunits, APL1 and APL2, besides their regulatory role, have catalytic activity
additional information
-
the presence of functional small subunits is required for large subunit stability
additional information
-
six Arabidopsis thaliana ADP-glucose pyrophosphorylase-encoding genes (two small subunits, ApS1 and ApS2, and four large subunits, ApL1ApL4) studied. Based on mRNA expression, ApS1 is the main small subunit or catalytic isoform responsible for ADP-glucose diphosphorylase activity in all tissues of the plant. Large subunits play a regulatory role. ApL1 is the main large subunit in source tissues, whereas ApL3 and, to a lesser extent, ApL4 are the main isoforms present in sink tissues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
G96N
-
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
additional information
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
purification of heterotetramers formed by small subunit APS1 with any of the large subunits APL1, APL2, APL3, or APL4 involves a 5 min/65°C heat treatment step
65
purification of heterotetramers formed by small subunit APS1 with any of the large subunits APL1, APL2, APL3, or APL4 involves a 5 min/65°C heat treatment step
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least 3 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial, recombinant enzymes, heat treatment step of heterotetramers formed by small subunit APS1 with any of the large subunits APL1, APL2, APL3 or APL4 at 65°C and of homotetramer APS1 at 70°C, only fractions that show activity at two concentrations of activator 3-phosphoglycerate, 0.5 and 10 mM are pooled
partial, recombinant enzymes, heat treatment step of heterotetramers formed by small subunit APS1 with any of the large subunits APL1, APL2, APL3 or APL4 at 65°C and of homotetramer APS1 at 70°C, only fractions that show activity at two concentrations of activator 3-phosphoglycerate, 0.5 and 10 mM are pooled
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
apl4, DNA and amino acid determination and analysis, expression in Escherichia coli
six genes coding for enzyme isoforms, two small and four large subunits are cloned and expressed in Escherichia coli
apl1, DNA and amino acid determination and analysis, expression in Escherichia coli
apl2, DNA and amino acid determination and analysis, expression in Escherichia coli
apl3, DNA and amino acid determination and analysis, expression in Escherichia coli
aps1, DNA and amino acid determination and analysis, expression in Escherichia coli
DNA and amino acid sequence determination and analysis, phylogenetic analysis, and determination and analysis of rates of evolution, the number of duplications in both large and small subunit genes and document changes in the patterns of AGPase evolution over time. The AGPase large subunit family occurs early in the history of land plants, while the earliest small subunit duplication occurs after the divergence of monocots and eudicots. The large subunit also has a larger number of gene duplications than does the small subunit, overview
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
inhibition of enzyme by dithiothreitol is prevented by pre- or by coincubation with 3-phophoglycerate, but incubation of already inhibited enzyme with 3-phophoglycerate may not reverse the inhibition
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
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raising sugar levels in plants is accompanied by increases in the level of trehalose 6-phosphate, redox activation of glucose 1-phosphate adenylyltransferase and the stimulation of starch synthesis in vivo. trehalose 6-phopshate acts as a signalling metabolite of sugar status
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, L.; Preiss, J.
Characterization of ADPglucose pyrophosphorylase from a starch-deficient mutant of Arabidopsis thaliana
Carbohydr. Res.
227
227-239
1992
Arabidopsis thaliana
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Zabawinski, C.; Van Den Koornhuyse, N.; D'Hulst, C.; Schlichting, R.; Giersch, C.; Delrue, B.; Lacroix, J.M.; Preiss, J.; Ball, S.
Starchless mutants of Chlamydomonas reinhardtii lack the small subunit of a heterotetrameric ADP-glucose pyrophosphorylase
J. Bacteriol.
183
1069-1077
2001
Salmonella enterica subsp. enterica serovar Typhimurium (P05415), Oryza sativa (P15280), Oryza sativa (P93430), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Anabaena sp. (P30521), Synechocystis sp. (P52415), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Chlamydomonas reinhardtii (Q42702), Chlamydomonas reinhardtii (Q9LLL6), Chlamydomonas reinhardtii, Solanum tuberosum LS2 (P55242)
Crevillen, P.; Ballicora, M.A.; Merida, A.; Preiss, J.; Romero, J.M.
The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme
J. Biol. Chem.
278
28508-28515
2003
Anabaena sp. (P30521), Arabidopsis thaliana (P55228), Arabidopsis thaliana (P55229), Arabidopsis thaliana (P55230), Arabidopsis thaliana (P55231), Arabidopsis thaliana (Q9SIK1), Arabidopsis thaliana, Beta vulgaris (P55232), Beta vulgaris (P55233), Hordeum vulgare (O04896), Hordeum vulgare (P30524), Hordeum vulgare (P55238), Ipomoea batatas (O81274), Ipomoea batatas (Q42859), no activity in Arabidopsis thaliana, Oryza sativa (O23809), Oryza sativa (P15280), Oryza sativa (P93430), Oryza sativa (Q9ARH9), Pisum sativum (Q43815), Pisum sativum (Q43816), Pisum sativum (Q43819), Solanum lycopersicum (O04924), Solanum lycopersicum (P93229), Solanum lycopersicum (P93230), Solanum lycopersicum (Q42882), Solanum tuberosum (P23509), Solanum tuberosum (P55242), Solanum tuberosum (P55243), Solanum tuberosum (Q00081), Solanum tuberosum LS1 (Q00081), Solanum tuberosum LS3 (P55243), Synechocystis sp. (P52415), Triticum aestivum (P12299), Triticum aestivum (P30523), Vicia faba (P52416), Vicia faba (P52417), Vicia faba SS1 (P52416), Vicia faba SS2 (P52417), Zea mays (Q941P2), Zea mays (Q947B9), Zea mays (Q947C0)
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
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
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
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
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
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
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
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
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)
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
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
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)
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