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Information on EC 2.7.9.4 - alpha-glucan, water dikinase
for references in articles please use BRENDA:EC2.7.9.4
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.9 Phosphotransferases with paired acceptors
2.7.9.4 alpha-glucan, water dikinase
IUBMB Comments
Requires Mg2+. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate . The protein phosphorylates glucans exclusively on O-6 of glucosyl residues . The protein phosphorylates itself with the β-phosphate of ATP, which is then transferred to the glucan .
The enzyme appears in viruses and cellular organisms
- 2.7.9.4
- glucans
- ribonucleotide
- deoxyribonucleotides
- alpha-glucans
- phosphoglucans
- amylopectin
- beta-amylase
-
allomorph
-
spirodela
-
beta-phosphate
- turions
-
starch-binding
- polyrhiza
- food industry
- biotechnology
showSynonyms
r1 protein, glucan water dikinase, alpha-glucan water dikinase, atgwd3, atgwd2, glucan water dikinase 3, starch-related r1 protein, glucan water dikinase 2, starch-related alpha-glucan/water dikinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glucan water dikinase
alpha-glucan water dikinase 1
alpha-glucan, water dikinase
alpha-glucan, water dikinase, GWD
-
-
-
-
At1g10760
At4g24450
AtGWD2
AtGWD3
glucan water dikinase
glucan, water dikinase
GWD
GWD1
GWD2
R1
SEX1
starch-related R1 protein
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate
ping-pong reaction mechanism
-
ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
starch degradation II
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SYSTEMATIC NAME
IUBMB Comments
ATP:alpha-glucan, water phosphotransferase
Requires Mg2+. ATP appears to be the only phosphate donor. No activity could be detected using GTP, UTP, phosphoenolpyruvate or diphosphate [1]. The protein phosphorylates glucans exclusively on O-6 of glucosyl residues [2]. The protein phosphorylates itself with the beta-phosphate of ATP, which is then transferred to the glucan [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 6-O-alpha-maltosyl-beta-cyclodextrin + H2O
AMP + phospho-6-O-alpha-maltosyl-beta-cyclodextrin + phosphate
Substrates: -
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ATP + alpha-cyclodextrin + H2O
AMP + phospho-alpha-cyclodextrin + phosphate
Substrates: -
Products: -
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?
ATP + amylopectin + H2O
?
-
Substrates: phosphorylation at the C3 position of glucose residues in amylopectin
Products: -
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ATP + amylose 18 + H2O
AMP + phosphorylated amylose 18 + phosphate
Substrates: -
Products: very poor substrate
Products: very poor substrate
?
ATP + amylose 24 + H2O
AMP + phosphorylated amylose 24 + phosphate
Substrates: -
Products: very poor substrate
Products: very poor substrate
?
ATP + amylose 53 + H2O
AMP + phosphorylated amylose 53 + phosphate
Substrates: -
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?
ATP + amylose 85 + H2O
AMP + phosphorylated amylose 85 + phosphate
Substrates: -
Products: -
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?
ATP + beta-cyclodextrin + H2O
AMP + phospho-beta-cyclodextrin + phosphate
Substrates: -
Products: -
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ATP + crystalline maltodextrin + H2O
AMP + phospho-alpha-glucosyl-maltodextrin + phosphate
Substrates: crystalline maltodextrin (MDcryst) is used as a model substrate for glucan phosphorylating enzyme activity that mimics features of native starches, such as allomorph and crystallinity but omitted branching. MDcryst has a higher degree of crystallinity and, therefore, recombinant GWD phosphorylates MDcryst with much higher rates than any other native starches tested so far. The incorporation of phosphate esters results in the release of phosphorylated (single, double, and triple phosphorylated glucan chains) as well as neutral maltodextrins from the water-insoluble MDcryst, indicating that the action of GWD disrupts the ordered arrangement of maltodextrins at the particle surface
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ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
ATP + elongated glucogen + H2O
AMP + elongated phosphoglucogen + phosphate
-
Substrates: -
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?
ATP + granular potato starch + H2O
AMP + phosphorylated granular potato starch + phosphate
Substrates: -
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?
ATP + maltodextrin + H2O
?
-
Substrates: crystallized maltodextrins, A- and B-type allomorphs
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ATP + postelongated glycogen + H2O
AMP + postelongated phospho-glycogen + phosphate
-
Substrates: -
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?
ATP + potato amylopektin + H2O
AMP + phosphorylated potato amylopektin + phosphate
Substrates: -
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ATP + potato amylose + H2O
AMP + phosphorylated potato amylose + phosphate
Substrates: -
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?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
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Substrates: essential step within starch metabolism. In Arabidopsis leaves starch turnover requires a close collaboration of alpha-glucan, water dikinase and phosphoglucan, water dikinase
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: the enzyme is involved in the cold-induced development of freezing tolerance in Arabidopsis
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
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Substrates: the endophytic fungus Piriformospora indica stimulates the expression of glucan-water dikinase Arabidopsis roots through a homeodomain transcription factor that binds to a conserved motif in the promoter
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: -
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
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Substrates: the endophytic fungus Piriformospora indica stimulates the expression of glucan-water dikinase in Nicotiana tabacum roots through a homeodomain transcription factor that binds to a conserved motif in the promoter
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: -
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amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
Substrates: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: exclusive phosphorylation of C-6 position, in vitro
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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Substrates: phosphorylation at C-6 position, crystallized maltodextrin, natural starch from maize, potato, Arabidopsis, A- and B-allomorph type
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: -
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP followingnucleotide binding and hydrolysis
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: -
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6 and 3, the gamma-phosphate group of ATP is transferred to water and the beta-phosphate group to an autocatalytical histidine residue via a phosphoramidate bond. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water. GWD-dependent incorporation of starch phosphate monoesters is higher after removing these surface-exposed glucans by amylolytic enzymes
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: GWD phosphorylates the hydroxyl group at carbon atom 6, the gamma-phosphate group of ATP is transferred to water and the beta-phosphate group to an autocatalytical histidine residue via a phosphoramidate bond
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: phosphorylation at C6
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: activity required for pollen tube germination in male tomato plants the impairment of which is linked to starch accumulation and reduction in level of soluble sugars
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: activity required for pollen tube germination
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: 4.5fold accumulation of starch and 1.8fold reduction in level of soluble sugars in absence of functional GWD
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: rescue of pollen germination in GWD-deficient mutant tomato plant
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: enzyme catalyzes the phophorylation of both C-6 and C-3 position of the glucose residues
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: -
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: room temperature, over night, agitating, pH 7.5, stimulated by beta-amylase activity, substrate: starch granules from Arabidopsis thaliana sex1-3 leaves
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: -
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: levels of starch phosphorylation at the C6 and C3 positions of the glucosyl residues are determined by mass spectrometry of hydrolyzed starch from tubers
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: the starch-binding R1 protein from potato catalyzes the glucan phosphorylation in a dikinase reaction type. Dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6 and 3, the gamma-phosphate group of ATP is transferred to water and the beta-phosphate group to an autocatalytical histidine residue via a phosphoramidate bond
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
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ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6 and 3
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ATP + amylopectin + H2O
AMP + phospho-amylopectin + phosphate
Substrates: 1 h, 30°C, pH 7, in presence of 10 mM NH4Cl, 10 mM MgCl2, 0.5 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, substrates: waxy maize amylopectin (unmodified (glycogen), elongated by phosphorylase a, pre-phosphorylated by potato glucan, water dikinase (GWD), or elongated and pre-phosphorylated) or soluble potato starch
Products: reaction stop by boiling
Products: reaction stop by boiling
?
ATP + amylopectin + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: -
Products: -
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?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
-
Substrates: -
Products: -
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?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
-
Substrates: -
Products: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
Products: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
Products: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
XM_015787980.2
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
XP_015579774.1
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: the enzyme is active in the wheat endosperm and contributes to the phosphorylation of wheat starch at the C-6 position
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
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Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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ATP + starch + H2O
AMP + phosphorylated starch + phosphate
Substrates: -
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phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
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Substrates: the enzyme is involved in degradation of transistory starch
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phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
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Substrates: AtGWD3 primarily catalyzes phosphorylation at the C-3 position of the glucose unit of preferably pre-phosphorylated amylopectin substrate with lon side chains
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starch + ATP + H2O
AMP + phospho-starch + phosphate
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Substrates: starch phosphorylation upon irradiation of dormant turions (1-2 days, 25°C) dependent on presence of nitrate (8 mM KNO3 and 1 mM Ca(NO3)2) or 10 mM NH4Cl (as nitrogen source) in nutrient medium
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starch + ATP + H2O
AMP + phospho-starch + phosphate
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Substrates: starch phosphorylation upon irradiation of dormant turions (1-2 days, 25°C) dependent on presence of nitrate (8 mM KNO3 and 1 mM Ca(NO3)2) or 10 mM NH4Cl (as nitrogen source) in nutrient medium
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additional information
?
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Substrates: not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
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additional information
?
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Substrates: not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
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additional information
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Substrates: phosphorylation of crystalline maltodextrin initiates solubilisation of both phosphorylated and neutral glucans
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additional information
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Substrates: substrate-specificity defined by physical arrangements of alpha glucans and by molecular order of glucan helices
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additional information
?
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Substrates: phosphorylation by GWD mediates phase transition from highly ordered to hydrated state glucans
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additional information
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Substrates: alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
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additional information
?
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Substrates: activity is independent of pre-phosphorylation of glucan substrate
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additional information
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Substrates: activity is independent of pre-phosphorylation of glucan substrate
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additional information
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Substrates: crystallized maltodextrin represents B-type starch allomorph, 30 min or 1 h, linear phosphorylation kinetics with respect to time and enzyme concentration (up to 1 h), phosphorylation at the surface of the crystalline maltodextrin, formation of a wide range of phosphoglucans (detection of mono-, di, and triphosphorylated alpha glucans), initiation of solubilisation of both phosphoglucans and neutral glucans from the crystalline maltodextrin
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additional information
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Substrates: GDW activity stimulates release of maltose from granular starch (by beta-amylase activity)
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additional information
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Substrates: GWD3-SBD shows strongest binding towards alpha-cyclodextrin and no detectable affinity for linear maltooligosaccharides or for phosphorylated beta-cyclodextrin
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additional information
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Substrates: the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
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additional information
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Substrates: the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
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additional information
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Substrates: no phosphorylation of the hydroxyl group at the C2 position
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additional information
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Substrates: no phosphorylation of the hydroxyl group at the C2 position
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additional information
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Substrates: enzyme binds reversibly to starch granules, depending upon the metabolic state of the leaf cells, properties of the starch granule surface change and these alterations are involved in the reversible binding of R1
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additional information
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Substrates: enzyme involved in phosphorylation and/or degradation of starch
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additional information
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Substrates: starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
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additional information
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Substrates: autocatalytic phosphorylation with beta not with gamma-phosphate
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additional information
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Substrates: enzyme binds reversibly to starch granules, depending upon the metabolic state of the leaf cells, properties of the starch granule surface change and these alterations are involved in the reversible binding of R1
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additional information
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Substrates: enzyme involved in phosphorylation and/or degradation of starch
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additional information
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Substrates: enzyme involved in phosphorylation and/or degradation of starch
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additional information
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Substrates: starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
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additional information
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Substrates: alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
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additional information
?
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Substrates: GDW activity stimulates beta-amylase1 activity, starch breakdown (in presence of beta-amylase1 and isoamylase3 and ATP), release of maltose from granular starch (by beta-amylase 1 and 3)
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additional information
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-
-
Substrates: suppression of GWD affects starch structure: reduction in glucose-6-phosphate content (2.3 nmol/mg starch compared to 14.1 nmol/mg), slight increase in amylose content (36% compared to 31%) along with decrease in diffraction maximum (Imax: 2.5, due to decrease in molecular density of crystalline lamellae through accumulation of amylose tie-chains in crystalline lamellae or of transversely oriented amylose chains in amorphous lamellae), higher ordered starch structures and elongated double helical chain compared to wild-type plant, increased melting temperature, disordered ends of double helix being excluded from crystal, but no destabilization of molecular packing of amylopectin A-chains and change in size of crystalline lamellae
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?
additional information
?
-
Substrates: no phosphorylation of the hydroxyl group at the C2 position
Products: -
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?
additional information
?
-
-
Substrates: starch degradation
Products: -
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?
additional information
?
-
-
Substrates: enzyme binds to starch granules
Products: -
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?
additional information
?
-
-
Substrates: enzyme involved in phosphorylation and/or degradation of starch
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + amylopectin + H2O
?
-
Substrates: phosphorylation at the C3 position of glucose residues in amylopectin
Products: -
Products: -
?
phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: the enzyme is involved in degradation of transistory starch
Products: -
Products: -
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: essential step within starch metabolism. In Arabidopsis leaves starch turnover requires a close collaboration of alpha-glucan, water dikinase and phosphoglucan, water dikinase
Products: -
Products: -
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: the enzyme is involved in the cold-induced development of freezing tolerance in Arabidopsis
Products: -
Products: -
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: the endophytic fungus Piriformospora indica stimulates the expression of glucan-water dikinase Arabidopsis roots through a homeodomain transcription factor that binds to a conserved motif in the promoter
Products: -
Products: -
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: the endophytic fungus Piriformospora indica stimulates the expression of glucan-water dikinase in Nicotiana tabacum roots through a homeodomain transcription factor that binds to a conserved motif in the promoter
Products: -
Products: -
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: exclusive phosphorylation of C-6 position, in vitro
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP followingnucleotide binding and hydrolysis
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: -
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: phosphorylation at C6
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: activity required for pollen tube germination in male tomato plants the impairment of which is linked to starch accumulation and reduction in level of soluble sugars
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: activity required for pollen tube germination
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: dikinases use ATP as a dual phosphate donor and transfer the beta- and gamma-phosphate groups to two distinct acceptor molecules, a glucan and water. A conserved histidine residue within this domain is capable of accepting the beta-phosphate group of ATP following nucleotide binding and hydrolysis
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
Substrates: levels of starch phosphorylation at the C6 and C3 positions of the glucosyl residues are determined by mass spectrometry of hydrolyzed starch from tubers
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
Products: -
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?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
Products: -
Products: -
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
Substrates: GWD phosphorylates the hydroxyl group at carbon atoms 6 and 3
Products: -
Products: -
?
additional information
?
-
Substrates: not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphorylation of crystalline maltodextrin initiates solubilisation of both phosphorylated and neutral glucans
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate-specificity defined by physical arrangements of alpha glucans and by molecular order of glucan helices
Products: -
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?
additional information
?
-
-
Substrates: phosphorylation by GWD mediates phase transition from highly ordered to hydrated state glucans
Products: -
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?
additional information
?
-
-
Substrates: alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
Products: -
Products: -
?
additional information
?
-
-
Substrates: GWD3-SBD shows strongest binding towards alpha-cyclodextrin and no detectable affinity for linear maltooligosaccharides or for phosphorylated beta-cyclodextrin
Products: -
Products: -
?
additional information
?
-
Substrates: the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
Products: -
Products: -
?
additional information
?
-
-
Substrates: the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme involved in phosphorylation and/or degradation of starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme involved in phosphorylation and/or degradation of starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme involved in phosphorylation and/or degradation of starch
Products: -
Products: -
?
additional information
?
-
-
Substrates: starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
Products: -
Products: -
?
additional information
?
-
-
Substrates: alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme involved in phosphorylation and/or degradation of starch
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EARLY STARVATION1
i.e. ESV1, a 50000 Da starch-binding protein. Decreases action of glucan, water dikinase. ESV1 does not affect the autophosphorylation of glucan, water dikinase
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioredoxin
-
starch granule-bound enzyme, isolated from dark-adapted plants exists in the inactive, oxidized form, which is capable of reactivation upon treatment with reduced thioredoxin
additional information
-
presence of beta-amylase BAM1 or BAM3 strongly stimulates enzyme-catalyzed phosphorylation
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Herpes Simplex
Modified adenovirus penton base protein (UTARVE) as a non-replicating vector for delivery of antisense oligonucleotides with antiviral and/or antineoplastic activity.
Herpes Simplex
The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway.
Herpes Simplex
The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) functions as a dominant regulator of apoptosis in hippocampal neurons involving activation of the ERK survival pathway and upregulation of the antiapoptotic protein Bag-1.
Herpes Simplex
The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase.
Neoplasms
Overexpression of the R2 subunit of ribonucleotide reductase in human nasopharyngeal cancer cells reduces radiosensitivity.
Vaccinia
Allosteric regulation of vaccinia virus ribonucleotide reductase, analyzed by simultaneous monitoring of its four activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
amylopectin, mean chain length: 23.5, nmol glucose-6-phosphate/mg: 0.1
0.04
amylopectin, pre-phosphorylated, mean chain length: 24.8, nmol glucose-6-phosphate/mg: 0.5
0.49
amylopectin, elongated, mean chain length: 29.7, nmol glucose-6-phosphate/mg: 0.1
0.65
amylopectin, elongated and pre-phosphorylated, mean chain length: 30.8, nmol glucose-6-phosphate/mg: 39.4
additional information
-
conversion of heat solubilized maltodextrin below 1 nmol/min/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
20°C: about 75% of maximal activity, 40°C: about 85% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
ecotype Columbia-0, wild-type or mutant lacking AtGWD2
UniProt
brenda
AtGWD1, AtGWD2 and AtGWD3 ORFs, nucleotide-binding domain; genotype TMS 4(2)1425
D7RA57; D7RA56
UniProt
brenda
wild-type or legwd::Ds mutant plants with different genetic backgrounds: cv. Micro-Tom, cv. Ailsa Craig, cv. M82, cv. VF36
-
-
brenda
cv. Daniella background, wild-type and GWD-suppressed lines H926-28.4 and H924-14.3
-
-
brenda
grown in field trials at Lincoln, Canterbury, New Zealand, during two consecutive seasons, 2011 and 2012, tubers are planted in October and harvested in March
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
floral organ, strong expression in vascular tissue just before onset of senescence (promoter activity)
brenda
phloem, high expression just before onset of senescence (promoter activity)
brenda
strong expression in mature flower parts (microarray)
brenda
in vitro germination at 25°C for 8 h (to 50% impaired in absence of functional GWD, starch accumulation and reduction in level of soluble sugars)
brenda
strong expression in vascular tissue just before onset of senescence (promoter activity)
brenda
-
70% of the total R1 protein found in the soluble fraction, strong increase of soluble enzyme activity during continuous red light
brenda
strong expression in vascular tissue just before onset of senescence (promoter activity)
brenda
leaf, stem, root, flower, silique only just before onset of senescence (promoter activity)
brenda
additional information
strong expression in vascular tissue (abaxial side of primary vascular bundle, phloem) just before onset of senescence (promoter activity), senescent leaves (microarray)
brenda
-
enzyme is isolated from illuminated or darkened leaves, in a granule-bound and a soluble state, but in darkened leaves at least 80% of total R1 was recovered in the soluble state
brenda
-
predominantly located at the surface of the particle of starch granule
brenda
-
enzyme is isolated from illuminated or darkened leaves, in a granule-bound and a soluble state, but in darkened leaves at least 80% of total R1 was recovered in the soluble state
brenda
-
starch granule-bound enzyme, isolated from dark-adapted plants exists in the inactive, oxidized form, which is capable of reactivation upon treatment with reduced thioredoxin
brenda
strong expression in vascular tissue just before onset of senescence (promoter activity)
brenda
strong expression in vascular tissue (floral organ abscission zone, dehiscence zone between silique walls, vascular tissue of silique walls) just before onset of senescence (promoter activity, microarray)
brenda
strong expression in vascular tissue just before onset of senescence (promoter activity)
brenda
additional information
-
enzyme is expressed in all starch-synthesizing tissues
brenda
additional information
spatially (vascular) and temporarily (age-dependent) restricted expression pattern (promoter activity)
brenda
additional information
-
spatially (vascular) and temporarily (age-dependent) restricted expression pattern (promoter activity)
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
along the cell wall, N-terminal 158 and 61 amino acids (revealed by confocal laser scanning microscopy)
brenda
the expression of AtGWD2 is in a relatively late stage of plant development
brenda
N-terminal 158 and 61 amino acids (revealed by confocal laser scanning microscopy)
brenda
-
starch granule-bound enzyme, isolated from dark-adapted plants exists in the inactive, oxidized form, which is capable of reactivation upon treatment with reduced thioredoxin
brenda
additional information
the enzyme acts significantly on the surface of native starch granules
-
brenda
altered GWD expression levels influence the surface properties of starch granules, determination of granule morphologies in different transgenic lines, which affects the starch synthesis by enzyme AtSS1, overview
-
brenda
nonamylolytic, starch granule-associated protein in potato. Phosphorylated glucans are more abundant at the granule surface of potato leaf starch during the beginning of starch mobilization
-
brenda
additional information
extra-plastidial localisation of full-length enzyme (in vitro chloroplast import assay), lack of chloroplast transit peptide
-
brenda
additional information
-
extra-plastidial localisation of full-length enzyme (in vitro chloroplast import assay), lack of chloroplast transit peptide
-
brenda
additional information
no fluorescence signal detected for full-length enzyme or its 610 N-terminal residues fused to eYFP or eGFP
-
brenda
additional information
-
no fluorescence signal detected for full-length enzyme or its 610 N-terminal residues fused to eYFP or eGFP
-
brenda
additional information
the GWD full-length protein binds to native starch granules in vivo and in vitro. Binding of GWD in vivo is dependent on the metabolic status of the cells. A significantly higher proportion of the dikinases is associated with native leaf starch granules isolated during the dark period than in the light phase of the photoperiod
-
brenda
additional information
the GWD full-length protein binds to native starch granules in vivo and in vitro. Binding of GWD in vivo is dependent on the metabolic status of the cells. A significantly higher proportion of the dikinases is associated with native leaf starch granules isolated during the dark period than in the light phase of the photoperiod
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
D7RA57; D7RA56
phylogenetic analysis of the cassava GWD sequences with other plant GWDs reveal that the cassava GWD belongs to the same group as that of Ricinus communis, Solanum tuberosum, Solanum lycopersicum, and Nicotiana sanderae
evolution
the largest differences in the amino acid sequence of GWD, EC 2.7.9.4, and PWD, EC 2.7.9.5, span the non-catalytic N-terminal region. In case of PWD, the N-terminus contains a single starch-binding domain (SBD) that belongs to the well-characterized carbohydrate-binding module (CBM) family CBM20. In contrast to PWD, the identity of the N-terminal starch-binding domain of GWD is less pronounced but might be assigned to the recently identified CBM45 family
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
XP_015579774.1
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
XM_015787980.2
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
evolution
-
significant diversity in the evolution of alpha-glucan, water dikinase enzymes across plant species may be evolutionarily advantageous according to the varying needs for phosphorylated stored starch between plants and environments. Computational approaches to compare the enzyme sequences of 48 plant species provide an insight into the evolutionary variation in catalytic activity of alpha-glucan, water dikinase among plants. Deleterious mutations are identified for some plants at various positions of the five aromatic amino acids, which are highly conserved in tandems of CBM45 and vital for binding of the enzymes to starch. These mutations may be responsible for altered carbohydrate binding activity of alpha-glucan, water dikinase in plants, thereby affecting phosphorylation of transit and stored starch
malfunction
in glasshouse pot trials, enzyme down-regulation leads to a 29% increase in grain yield while in glasshouse tub trials simulating field row spacing and canopy development, enzyme down-regulation results in a grain yield increase of 26%. Decreased activity of the enzyme is correlated with an increase in alpha-amylase activity
malfunction
mutants lacking the enzyme reveal a starch excess phenotype as well as growth retardation. The lack of GWD causes a reduction of G6P and G3P. The lack of GWD in mature Arabidopsis thaliana plants as observed in the null mutant sex1-8 results in a fivefold increased leaf starch content compared to wild-type plants. Although the internal structure of sex1-8 starch granules is similar to wild-type, the length as well as the abundance of glucan chains exposed on the granule surface differs in the mutant. The lack of GWD in mature sex1-8 plants results in a shift of the chain length distribution towards shorter glucan chains at the granule surface, the abundance of glucan chains at the granule surface is increased in the mutant compared to wild-type. Similar to the Arabidopsis GWD null mutant, the altered surface properties are also present in two partially complemented sex1-8 mutants which have compared to WT an approx. 79% and 93% lowered GWD protein level, respectively. Reduced expression of GWD impair the elongation of existing glucan chains catalyzed by starch synthase 1 (AtSS1), one of the dominate starch synthesizing activity in Arabidopsis. Impaired starch degradation caused by GWD deficiency may lead to lowered export of sugars to heterotrophic tissue and an overall reduction of biomass
malfunction
AtGWD2 knockout mutants do not accumulate high amounts of starch nor have a visible growth phenotype compared to wild-type plants
malfunction
melting enthalpy and crystallinity of purified starches are higher if GWD-mediated starch phosphorylation is suppressed. R1 reduction results in a starch excess phenotype in leaves, e.g., the accumulation of high amounts of starch at the end of a normal dark phase because of the decreased rates of leaf starch degradation. In addition, the lowered expression of R1 in these plants is accompanied by a reduction in cold-induced sweeting in tubers. Transgenic potato plants with reduced StGWD expression, show impeded starch degradation and an overall reduction in starch phosphate content. In transgenic potato lines with reduced expression of StGWD, small alteration in storage starch metabolism is reported
malfunction
GWD-deficient Arabidopsis thaliana mutants have a starch excess phenotype (sex1). The internal structure of granules isolated from GWD mutant plants, having reduced or no GWD activity, is unaffected, as thermal stability, allomorph, chain length distribution and density of starch granules are similar to wild-type, but short glucan chain residues located at the granule surface dominate in starches of transgenic plants and impede GWD activity. A similarly reduced rate of phosphorylation by GWD is also observed in potato tuber starch fractions that differ in the proportion of accessible glucan chain residues at the granule surface. A model is proposed to explain the characteristic morphology of starch granules observed in GWD transgenic plants. The model postulates that the occupancy rate of single glucan chains at the granule surface limits accessibility to starch-related enzymes
malfunction
-
downregulation of the enzyme causes phenotypic alteration in grain and growth. Coleoptile length is increased in these transgenic lines independently of grain size increases. The GWD-depleted wheat lines exhibit unexpected increases in grain size, early vigour and plant biomass. No changes in starch degradation rates during germination are identified, or any major alteration in soluble sugar levels that may explain the coleoptile growth modification. There is no evidence that the increased growth of coleoptiles in these lines is connected to starch conformation or degradation or soluble sugar content. Phenotype, overview
malfunction
analysis of changes in GWD protein abundance in relation to starch levels in wild-type plants, in transgenic plants in which GWD transcripts are strongly reduced by induction of RNA interference, and in transgenic plants overexpressing GWD, overview. Overexpression of GWD does not accelerate starch degradation in leaves, and starch degradation is not inhibited until GWD levels are reduced by 70%. GWD protein levels do not vary over the diel cycle and the protein has a half-life of 2 days. Plants expressing redox-insensitive GWD have normal starch turnover
malfunction
gwd2 mutants are shrunken, with the epidermal cells of the seed coat irregularly shaped. gwd2 seeds contain a lower lipid to protein ratio and are impaired in germination
metabolism
-
GWD1 phosphorylates highly ordered, insoluble starch, and glucan phosphorylation at the C-6 position results in a transition state of the phosphoglucans,´which is less ordered but still insoluble. This specific state of the starch granule is an appropriate substrate for phosphoglucan, water dikinase GWD3 catalysis (C-3 phosphorylation) after which the phosphoglucan finally becomes soluble
metabolism
during starch metabolism, the phosphorylation of glucosyl residues of amylopectin is a repeatedly observed process. The phosphorylation is mediated by dikinases, the glucan, water dikinase (GWD, EC 2.7.9.4) and the phosphoglucan, water dikinase (PWD, EC 2.7.9.5). By the collaborative action of both enzymes, the initiation of a transition of alpha-glucans from highly ordered, water-insoluble state to a less order state is realized and thus the initial process of starch degradation
metabolism
starch phosphorylation in potato tubers is influenced by allelic variation in the genes encoding glucan water dikinase, starch branching enzymes I and II, and starch synthase III. Starch phosphorylation is a complex trait, usage of association mapping approach to discover genetic markers associated with the degree of starch phosphorylation
metabolism
glucan, water dikinase is a key enzyme of starch metabolism
metabolism
-
Glucan, water dikinase (GWD; EC 2.7.9.4) and its sister enzyme phosphoglucan, water dikinase (PWD; EC 2.7.9.5), are responsible for the phosphorylation of starch during synthesis. These dikinases phosphorylate C6 and C3 residues of alpha-D-glucan chains, respectively, with PWD activity dependent on that of GWD
metabolism
the first step on the pathway of starch degradation in Arabidopsis thaliana leaves at night is the phosphorylation of starch polymers, catalyzed by glucan, water dikinase, GWD. The enzyme exerts only a low level of control over starch degradation in Arabidopsis leaves. The starch-phosphorylating enzymes are attractive candidates for the control of flux through starch degradation. Daily control of starch degradation is likely to be at a posttranslational level
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
XP_015579774.1
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
XM_015787980.2
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
-
the enzyme catalyzes starch phosphorylation, an integral step in transitory starch degradation
metabolism
the enzyme is involved in starch metabolism by adding phosphate groups to amylopectin
metabolism
the enzyme is involved in starch phosphorylation, a key step in starch degradation
physiological function
enzyme GWD catalyzes starch phosphorylation both in leaves and different plant storage organs
physiological function
D7RA57; D7RA56
enzyme GWD mediates starch breakdown through glucan phosphorylation
physiological function
the enzyme is involved in starch degradation
physiological function
the starch-related dikinase utilizes ATP as dual phosphate donor transferring the terminal gamma-phosphate group to water selectively to C6 position of a glucosyl residue within amylopectin. The action of the dikinase is restricted to the granule surface and glucan chains exposed at the surface account only for a minor proportion of the entire granule. Glucan chains that are phosphorylated by the dikinase remain covalently linked to the insoluble starch particle. In Arabidopsis leaf starch about 0.1% of the glucosyl residues are phosphorylated, respectively. GWD is responsible for C3 and C6 phosphorylation. A significant PWD-mediated C3 phosphorylation requires the preceding phosphorylation by GWD in Arabidopsis thaliana wild-type starch. GWD preferentially acts on crystalline surfaces and GWD-mediated phosphorylation enables a phase transition at the granule surface from a solid to a more soluble state enabling a significant amylolysis
physiological function
the starch-related dikinase utilizes ATP as dual phosphate donor transferring the terminal gamma-phosphate group to water selectively to C6 position of a glucosyl residue within amylopectin. The action of the dikinase is restricted to the granule surface and glucan chains exposed at the surface account only for a minor proportion of the entire granule. Glucan chains that are phosphorylated by the dikinase remain covalently linked to the insoluble starch particle. In Arabidopsis, leaf starch and potato tuber starch about 0.1 and 1% of the glucosyl residues are phosphorylated, respectively. A direct access of AtGWD2 to leaf starch granules in vivo and an overall impact on transitory starch metabolism is excluded
physiological function
the starch-related dikinase utilizes ATP as dual phosphate donor transferring the terminal gamma-phosphate group to water selectively to C6 position of a glucosyl residue within amylopectin. The action of the dikinase is restricted to the granule surface and glucan chains exposed at the surface account only for a minor proportion of the entire granule. Glucan chains that are phosphorylated by the dikinase remain covalently linked to the insoluble starch particle. In potato tuber starch, about 1% of the glucosyl residues are phosphorylated, respectively
physiological function
starch granule re-structuring by starch branching enzyme and glucan water dikinase modulation affects caryopsis physiology and metabolism. Starch composition varied over grain development and starch granules exhibit clear morphological differences over grain development
physiological function
glucan phosphorylation mediated by alpha-glucan, water dikinase is essential in the light phase for a functional transitory starch turnover. The length of the light phase affects the phosphorylation state of the transitory starch and, by this, the average leaf starch content and the resulting growth of the plants. The longer the light period, the higher the starch phosphorylation rate at G-6 of alpha-glucan and the lower the starch content. Starch phosphorylation by GWD in the light phase is in parts necessary for proper starch degradation in the following night
physiological function
phosphorylation of transitory starch by alpha-glucan, water dikinase during starch turnover affects the surface properties and morphology of starch granules
physiological function
-
glucan, water dikinase is the primary enzyme responsible for addition of phosphate groups to starch, in a grain-specific manner
physiological function
enzyme GWD is a subject to redox regulation. A disulfide bond can be reduced in vitro by micromolar concentrations of reduced thioredoxins, resulting in activation of the enzyme. Enzyme GWD in the soluble fraction of plant extracts is in the reduced form, but a fraction of the enzyme bound to starch granules is reported to be in an oxidized, inactive form. Enzyme GWD has a long half-life and a low flux control coefficient for starch degradation. Transcriptional regulation of GWD protein levels is unlikely to be important for the control of starch degradation
physiological function
important enzyme of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties
physiological function
the enzyme plays no role in transient starch metabolism. The enzyme (GWD2) possibly in concert with BAM5, may thus contribute to controlling the ratio between soluble and insoluble polysaccharides in plants
additional information
potato lines GWD phenotype-genotype relationship, ooverview
additional information
-
potato lines GWD phenotype-genotype relationship, ooverview
Show AA Sequence and Transmembrane Helices (410 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14200
-
theoretical, starch-binding domain, SBD, Asp68-Gly184, verified by SDS-PAGE
154000
-
starch-associated, phosphorylated and non-phosphorylated GWD, SDS-PAGE
160000
163484
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
D7RA57; D7RA56
the GWD protein consists of a dikinase domain and a large (approximately 120 kDa) N-terminal domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the protein possesses two vicinal phosphorylation sites, both of which are transiently phosphorylated
phosphoprotein
-
large structural changes on autophosphorylation, indicating that the enzyme employs a swivelling-domain mechanism for enzymatic phosphotransfer
phosphoprotein
autophosphorylation of wild-type enzyme, no histidine autophosphorylation of mutant enzyme H992A
phosphoprotein
-
the protein possesses two vicinal phosphorylation sites, both of which are transiently phosphorylated
phosphoprotein
-
light induces phosphorylation of glucan water dikinase, autophosphorylation precedes the initiation of starch degradation under physiological conditions
phosphoprotein
-
autophosphorylation upon irradiation with continuous red light leads dependent on presence of nitrate
phosphoprotein
-
autophosphorylation upon irradiation with continuous red light leads dependent on presence of nitrate
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C1019S
site-directed mutagenesis, the mutant is redox-insensitiv in contrast to the wild-type enzyme
H1004A
-
lacks autophosphorylation, fails to stimulate beta-amylase 3-catalyzed starch breakdown, similar binding to starch granules as wild-type enzyme (in vitro), H1004: conserved residue within phosphohistidine domain
H992A
mutant enzyme backgroun level of activity, no autophosphorylation
W117A
mutation in tandem repeat sequence SBD-1, mutant shows extremely weak glucan binding
W62A
mutation in tandem repeat sequence SBD-1, mutant shows extremely weak glucan binding
additional information
additional information
-
in enzyme deficient mutant plants, phosphorylation at both C6- and C3-positions of glucose moieties in starch is dramatically decreased. In mutant plants lacking phosphoglucan, water dikinase EC 2.7.9.5, C3-bound phosphate is reduced to levels close to detection limit
additional information
construction of transgenic Arabidopsis thaliana plants, i.e. gwd-c1, gwd-c2, and gwd-c1/gwd-c2 or sex1-8, with reduced or no GWD activity. Absence of GWD results in altered starch granule morphology but no change in the physicochemical properties of starch granules, phenotype, overview. Partially complemented GWD transgenic lines exhibit an intermediate phenotype. Effects of the mutations on starch-related enzymes in the four Arabidopsis lines, overview
additional information
-
construction of transgenic Arabidopsis thaliana plants, i.e. gwd-c1, gwd-c2, and gwd-c1/gwd-c2 or sex1-8, with reduced or no GWD activity. Absence of GWD results in altered starch granule morphology but no change in the physicochemical properties of starch granules, phenotype, overview. Partially complemented GWD transgenic lines exhibit an intermediate phenotype. Effects of the mutations on starch-related enzymes in the four Arabidopsis lines, overview
additional information
generation of transgenic plants expressing constitutively active GWD and of Arabidopsis plants expressing a dexamethasone-inducible silencing (RNAi) construct targeted at GWD. These plants retain normal control of starch degradation in leaves. Analysis of changes in GWD protein abundance in relation to starch levels in wild-type plants, in transgenic plants in which GWD transcripts are strongly reduced by induction of RNA interference, and in transgenic plants overexpressing GWD, overview
additional information
recombinant production of enzyme fragments SBD and N11 corresponding to the fragments resulting from limited proteolysis of enzyme by trypsin. Fragment N11 shows starch phosphorylating activity and a specific activity 2fold higher than that of wild-type and a doubling of Km value for potato starch substrate. N11 exhibits a higher preference for phosphorylating shorter chains compared to wild-type. Using amylose as substrate, N11 shows 5fold higher specific activity
additional information
-
recombinant production of enzyme fragments SBD and N11 corresponding to the fragments resulting from limited proteolysis of enzyme by trypsin. Fragment N11 shows starch phosphorylating activity and a specific activity 2fold higher than that of wild-type and a doubling of Km value for potato starch substrate. N11 exhibits a higher preference for phosphorylating shorter chains compared to wild-type. Using amylose as substrate, N11 shows 5fold higher specific activity
additional information
generation of antisense transgenic lines which reveal more but smaller tubers
additional information
-
production of transgenic Triticum aestivum lines using RNAi targeted to the endosperm only resulting in reduction in both GWD protein abundance and starch phosphate content
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by metal-affinity chromatography after expression in Saccharomyces cerevisiae with C-terminal V5- and hexa-His-tag
by metal-affinity chromatography on a His-Trap-HP column (elution: imidazole gradient, 50-500 mM), followed by buffer exchange and concentration
-
extracted from starch granules with SDS, washed with methanol and chloroform and identified by 2D-SDS-PAGE and immunodetection
-
Ni-nitrilotriacetic acid column chromatography, and gel filtration
recombinant GWD3-SBD is purified on a beta-cyclodextrin Sepharose column and by an additional His-trap purification step
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells and in Nicotiana tabacum leaf mesophyll cells
expressed in Escherichia coli BL21(DE3) cells
from pBluescript-GWD via pAA100-35S and pBinPlus to construct pLAT52::StGWD for expression in Micro-Tom tomato plants under control of a late pollen-specific promoter following Agrobacterium-mediated transformation
gene GWD, genotyping included determination of allele dosage of 193 potato lines by amplicon sequencing and microsatellite analysis, overview
gene gwd, recombinant expression of Arabidopsis thaliana GWD mutant C1019S C-terminally fused to GFP from a 35S promoter in transgenic Arabidopsis thaliana plants
gene GWD1, construction of transgenic plants expressing the soluble StrepII-tagged mutant enzyme, transformation via Agrobacterium tumefaciens mediation method
gene GWD1, the gene is located on chromosome 1, phylogenetic tree
gene R1 or GWD, DNA and amino acid sequence determination and analysis by reverse transcription PCR approach using tuber RNA, detailed sequence comparison and phylogenetic analysis, semi-quantitative RT-PCR gene expression analysis
genotype TMS 4(2)1425, DNA and amino acid sequence determination and analysis of the enzyme and the nucleotide-binding domain of the enzyme, sequence comparisons and phylogenetic tree
D7RA57; D7RA56
heterologously expressed in potato tubers (Solanum tuberosum). Expression of AtGWD2 and AtGWD3 are not suitable for engineering starch with a high phosphate content in potato tubers but can provide new insights in the process of starch phosphorylation in the amyloplast
in pKGWFS7 for expression N-terminally of an (eGFP)-beta-glucoronidase fusion and Agrobacterium-mediated transformation of Arabidopsis plants, in pK7FWG2 (as full-length or 158 N-terminal amino acid fragment) for expression as eGFP-fusion and subcellular localization in onion epidermis and Arabidopsis thaliana, in pPS48uYFP as full-length, C-terminal truncations (N-terminal 610, 158, or 61 amino acids) or C-terminally fused to transit peptide of AtGWD isoform 1 for Agrobacterium-mediated expression in Nicotiana benthamiana, in pGEM-4Z (as full-length or as fusion with transit peptide of AtGWD1) for in vitro transcription, translation and chloroplast import assays
lacking nucleotides 1-225 (encoding amino acids 1-75: putative chloroplast transit peptide) in pGEM-T Easy or in pET23b for expression with C-terminal hexa-His-tag in Escherichia coli BL21(DE3)
-
overexpression of the enzyme in Hordeum vulgare using the hordein-D promoter, the promoter activates storage protein accumulation, mostly at a later grain developmental stage than 10 DAP
the starch-binding domain, SBD, Asp68-Gly184, of glucan, water dikinase 3 is cloned into the vector pET-28a+ for expression in Escherichia coli BL21DE3 cells, the region encoding residues 1-201, containing the chloroplast transit peptide and the SBD is fused to YFP and transiently expressed in Nicotiana benthamiana
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform GWD1 expression reaches its maximum after 10 h of illumination, The lowest expression of isoform GWD1 occurs 4 h after turning the light on, and it is approximately 7times lower than the expression measured 6 h late
-
the SEX1 gene expression is induced in HsPIPKIalpha lines, i.e. transgenic Arabidopsis thaliana plants constitutively expressing human phosphatidylinositol 4-phosphate 5-kinase Ialpha, HsPIPKIalpha, in plasma membranes. Transcripts of genes involved in starch metabolism such as SEX1 (glucan water dikinase) and SEX4 (phosphoglucan phosphatase), DBE (debranching enzyme), MEX1 (maltose transporter), APL3 (ADP-glucose pyrophosphorylase) and glucose-6-phosphate transporter (Glc6PT) are upregulated in the HsPIPKIalpha plants, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
the starch-phosphorylating enzymes are attractive candidates for the control of flux through starch degradation
food industry
rice starch contains only low concentrations of starch bound phosphate monoesters, which limits its usage in various industrial processes. Six stable individual transgenic lines with hyper-phosphorylated starch are produced by the overexpression of the StGWD1 in rice (Oryza sativa japonica cv. Zhonghua 11). The transgenic lines have 9fold and double higher Glc-6-P and Glc-3-P, respectively and increased amylose content. The starch granules display only minor morphological alterations, notably the presence of surface pores and moderately distorted edges and surfaces. The novel starch introduces unique combinations of functionality for rice starch, such as reduced gelatinization temperature, decreased pasting viscosity, increased gel formation capacity and increased gel hardness
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ritte, G.; Eckermann, N.; Haebel, S.; Lorberth, R.; Steup, M.
Compartmentation of the starch-related R1 protein in higher plants
Starch Staerke
52
179-185
2000
Solanum tuberosum
-
brenda
Ritte, G.; Lorberth, R.; Steup, M.
Reversible binding of the starch-related R1 protein to the surface of transitory starch granules
Plant J.
21
387-391
2000
Solanum tuberosum, Lathyrus oleraceus
brenda
Reimann, R.; Ritte, G.; Steup, M.; Appenroth, K.J.
Association of alpha-amylase and the R1 protein with starch granules precedes the initiation of net starch degradation in turions of Spirodela polyrhiza
Physiol. Plant.
114
2-12
2002
Spirodela polyrhiza
brenda
Ritte, G.; Lloyd, J.R.; Eckermann, N.; Rottmann, A.; Kossmann, J.; Steup, M.
The starch-related R1 protein is an alpha-glucan, water dikinase
Proc. Natl. Acad. Sci. USA
99
7166-7171
2002
Solanum tuberosum
brenda
Ritte, G.; Steup, M.; Kossmann, J.; Lloyd James, R.
Determination of the starch-phosphorylating enzyme activity in plant extracts
Planta
216
798-801
2003
Arabidopsis thaliana, Solanum tuberosum
brenda
Kotting, O.; Pusch, K.; Tiessen, A.; Geigenberger, P.; Steup, M.; Ritte, G.
Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase
Plant Physiol.
137
242-252
2005
Arabidopsis thaliana
brenda
Mikkelsen, R.; Baunsgaard, L.; Blennow, A.
Functional characterization of alpha-glucan,water dikinase, the starch phosphorylating enzyme
Biochem. J.
377
525-532
2004
Solanum tuberosum (Q9AWA5)
brenda
Mikkelsen, R.; Blennow, A.
Functional domain organization of the potato alpha-glucan, water dikinase (GWD): evidence for separate site catalysis as revealed by limited proteolysis and deletion mutants
Biochem. J.
385
355-361
2005
Solanum tuberosum
brenda
Sherameti, I.; Shahollari, B.; Venus, Y.; Altschmied, L.; Varma, A.; Oelmueller, R.
The endophytic fungus Piriformospora indica stimulates the expression of nitrate reductase and the starch-degrading enzyme glucan-water dikinase in tobacco and Arabidopsis roots through a homeodomain transcription factor that binds to a conserved motif in their promoters
J. Biol. Chem.
280
26241-26247
2005
Arabidopsis thaliana, Nicotiana tabacum
brenda
Baunsgaard, L.; Lutken, H.; Mikkelsen, R.; Glaring, M.A.; Pham, T.T.; Blennow, A.
A novel isoform of glucan, water dikinase phosphorylates pre-phosphorylated alpha-glucans and is involved in starch degradation in Arabidopsis
Plant J.
41
595-605
2005
Arabidopsis thaliana
brenda
Reimann, R.; Hippler, M.; Machelett, B.; Appenroth, K.J.
Light induces phosphorylation of glucan water dikinase, which precedes starch degradation in turions of the duckweed Spirodela polyrhiza
Plant Physiol.
135
121-128
2004
Spirodela polyrhiza
brenda
Yano, R.; Nakamura, M.; Yoneyama, T.; Nishida, I.
Starch-related alpha-glucan/water dikinase is involved in the cold-induced development of freezing tolerance in Arabidopsis
Plant Physiol.
138
837-846
2005
Arabidopsis thaliana
brenda
Mikkelsen, R.; Mutenda, K.E.; Mant, A.; Schurmann, P.; Blennow, A.
alpha-Glucan, water dikinase (GWD): a plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity
Proc. Natl. Acad. Sci. USA
102
1785-1790
2005
Solanum tuberosum
brenda
Mikkelsen, R.; Suszkiewicz, K.; Blennow, A.
A novel type carbohydrate-binding module identified in alpha-glucan, water dikinases is specific for regulated plastidial starch metabolism
Biochemistry
45
4674-4682
2006
Solanum tuberosum (Q9AWA5), Solanum tuberosum
brenda
Fettke, J.; Eckermann, N.; Koetting, O.; Ritte, G.; Steup, M.
Novel starch-related enzymes and carbohydrates
Cell. Mol. Biol.
52
OL883-OL904
2006
Solanum tuberosum
-
brenda
Ritte, G.; Heydenreich, M.; Mahlow, S.; Haebel, S.; Koetting, O.; Steup, M.
Phosphorylation of C6- and C3-positions of glucosyl residues in starch is catalysed by distinct dikinases
FEBS Lett.
580
4872-4876
2006
Arabidopsis thaliana
brenda
Edner, C.; Li, J.; Albrecht, T.; Mahlow, S.; Hejazi, M.; Hussain, H.; Kaplan, F.; Guy, C.; Smith, S.M.; Steup, M.; Ritte, G.
Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases
Plant Physiol.
145
17-28
2007
Arabidopsis thaliana, Solanum tuberosum
brenda
Kozlov, S.S.; Blennow, A.; Krivandin, A.V.; Yuryev, V.P.
Structural and thermodynamic properties of starches extracted from GBSS and GWD suppressed potato lines
Int. J. Biol. Macromol.
40
449-460
2007
Solanum tuberosum
brenda
Glaring, M.A.; Zygadlo, A.; Thorneycroft, D.; Schulz, A.; Smith, S.M.; Blennow, A.; Baunsgaard, L.
An extra-plastidial alpha-glucan, water dikinase from Arabidopsis phosphorylates amylopectin in vitro and is not necessary for transient starch degradation
J. Exp. Bot.
58
3949-3960
2007
Arabidopsis thaliana (Q9STV0), Arabidopsis thaliana
brenda
Appenroth, K.J.; Ziegler, P.
Light-induced degradation of storage starch in turions of Spirodela polyrhiza depends on nitrate
Plant Cell Environ.
31
1460-1469
2008
Spirodela polyrhiza, Spirodela polyrhiza SJ
brenda
Hejazi, M.; Fettke, J.; Haebel, S.; Edner, C.; Paris, O.; Frohberg, C.; Steup, M.; Ritte, G.
Glucan, water dikinase phosphorylates crystalline maltodextrins and thereby initiates solubilization
Plant J.
55
323-334
2008
Arabidopsis thaliana
brenda
Nashilevitz, S.; Melamed-Bessudo, C.; Aharoni, A.; Kossmann, J.; Wolf, S.; Levy, A.A.
The legwd mutant uncovers the role of starch phosphorylation in pollen development and germination in tomato
Plant J.
57
1-13
2009
Solanum lycopersicum, Solanum lycopersicum (B5B3R3)
brenda
Christiansen, C.; Abou Hachem, M.; Janecek, S.; Viks?-Nielsen, A.; Blennow, A.; Svensson, B.
The carbohydrate-binding module family 20--diversity, structure, and function
FEBS J.
276
5006-5029
2009
Arabidopsis thaliana
brenda
Christiansen, C.; Hachem, M.A.; Glaring, M.A.; Viks?-Nielsen, A.; Sigurskjold, B.W.; Svensson, B.; Blennow, A.
A CBM20 low-affinity starch-binding domain from glucan, water dikinase
FEBS Lett.
583
1159-1163
2009
Arabidopsis thaliana
brenda
Hejazi, M.; Fettke, J.; Paris, O.; Steup, M.
The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the A- and B-type allomorphs of crystallized maltodextrins but the mode of action differs
Plant Physiol.
150
962-976
2009
Solanum tuberosum
brenda
Orzechowski, S.; Grabowska, A.; Sitnicka, D.; Siminska, J.; Felus, M.; Dudkiewicz, M.; Fudali, S.; Sobczak, M.
Analysis of the expression, subcellular and tissue localisation of phosphoglucan, water dikinase (PWD/GWD3) in Solanum tuberosum L.: A bioinformatics approach for the comparative analysis of two alpha-glucan, water dikinases (GWDs) from Solanum tuberosum L.
Acta Physiol. Plant.
35
483-500
2013
Solanum tuberosum
-
brenda
Glaring, M.A.; Baumann, M.J.; Abou Hachem, M.; Nakai, H.; Nakai, N.; Santelia, D.; Sigurskjold, B.W.; Zeeman, S.C.; Blennow, A.; Svensson, B.
Starch-binding domains in the CBM45 family - low-affinity domains from glucan, water dikinase and alpha-amylase involved in plastidial starch metabolism
FEBS J.
278
1175-1185
2011
Solanum tuberosum (Q9AWA5)
brenda
Hejazi, M.; Steup, M.; Fettke, J.
The plastidial glucan, water dikinase (GWD) catalyses multiple phosphotransfer reactions
FEBS J.
279
1953-1966
2012
Solanum tuberosum, Arabidopsis thaliana
brenda
Ral, J.P.; Bowerman, A.F.; Li, Z.; Sirault, X.; Furbank, R.; Pritchard, J.R.; Bloemsma, M.; Cavanagh, C.R.; Howitt, C.A.; Morell, M.K.
Down-regulation of glucan, water-dikinase activity in wheat endosperm increases vegetative biomass and yield
Plant Biotechnol. J.
10
871-882
2012
Triticum aestivum (D7PCT9)
brenda
Mahlow, S.; Orzechowski, S.; Fettke, J.
Starch phosphorylation: insights and perspectives
Cell. Mol. Life Sci.
73
2753-2764
2016
Arabidopsis thaliana (Q9STV0), Arabidopsis thaliana (Q9SAC6), Solanum tuberosum (Q9AWA5)
brenda
Carpenter, M.A.; Joyce, N.I.; Genet, R.A.; Cooper, R.D.; Murray, S.R.; Noble, A.D.; Butler, R.C.; Timmerman-Vaughan, G.M.
Starch phosphorylation in potato tubers is influenced by allelic variation in the genes encoding glucan water dikinase, starch branching enzymes I and II, and starch synthase III
Front. Plant Sci.
6
143
2015
Solanum tuberosum (Q9AWA5), Solanum tuberosum
brenda
Opabode, J.; Oyelakin, O.; Akinyemiju, O.; Ingelbrecht, I.
Cloning and sequence analysis of the nucleotide-binding domain of an alpha-glucan, water dikinase gene from cassava (Manihot esculenta Crantz)
J. Agric. Sci.
5
56-64
2013
Manihot esculenta (D7RA57 AND D7RA56)
-
brenda
Bansal, A.; Das, N.
Molecular cloning and sequence comparison of a cDNA encoding alpha-glucan, water dikinase (GWD) from potato (Solanum tuberosum L.), and analysis of gene expression
J. Plant Biochem. Biotechnol.
22
441-452
2013
Solanum tuberosum (B2M0R3)
-
brenda
Mahlow, S.; Hejazi, M.; Kuhnert, F.; Garz, A.; Brust, H.; Baumann, O.; Fettke, J.
Phosphorylation of transitory starch by alpha-glucan, water dikinase during starch turnover affects the surface properties and morphology of starch granules
New Phytol.
203
495-507
2014
Arabidopsis thaliana (Q9SAC6), Arabidopsis thaliana
brenda
Bowerman, A.F.; Newberry, M.; Dielen, A.S.; Whan, A.; Larroque, O.; Pritchard, J.; Gubler, F.; Howitt, C.A.; Pogson, B.J.; Morell, M.K.; Ral, J.P.
Suppression of glucan, water dikinase in the endosperm alters wheat grain properties, germination and coleoptile growth
Plant Biotechnol. J.
14
398-408
2016
Triticum aestivum
brenda
Skeffington, A.W.; Graf, A.; Duxbury, Z.; Gruissem, W.; Smith, A.M.
Glucan, water dikinase exerts little control over starch degradation in Arabidopsis leaves at night
Plant Physiol.
165
866-879
2014
Arabidopsis thaliana (Q9SAC6)
brenda
Hejazi, M.; Mahlow, S.; Fettke, J.
The glucan phosphorylation mediated by alpha-glucan, water dikinase (GWD) is also essential in the light phase for a functional transitory starch turn-over
Plant Signal. Behav.
9
e28892
2014
Arabidopsis thaliana (Q9SAC6)
brenda
Im, Y.J.; Smith, C.M.; Phillippy, B.Q.; Strand, D.; Kramer, D.M.; Grunden, A.M.; Boss, W.F.
Increasing phosphatidylinositol (4,5)-bisphosphate biosynthesis affects basal signaling and chloroplast metabolism in Arabidopsis thaliana
Plants (Basel)
3
27-57
2014
Arabidopsis thaliana (Q9SAC6)
brenda
Shaik, S.S.; Obata, T.; Hebelstrup, K.H.; Schwahn, K.; Fernie, A.R.; Mateiu, R.V.; Blennow, A.
Starch granule re-structuring by starch branching enzyme and glucan water dikinase modulation affects caryopsis physiology and metabolism
PLoS ONE
11
e0149613
2016
Hordeum vulgare (C3W8P1), Hordeum vulgare
brenda
Pirone, C.; Gurrieri, L.; Gaiba, I.; Adamiano, A.; Valle, F.; Trost, P.; Sparla, F.
The analysis of the different functions of starch-phosphorylating enzymes during the development of Arabidopsis thaliana plants discloses an unexpected role for the cytosolic isoform GWD2
Physiol. Plant.
160
447-457
2017
Arabidopsis thaliana (Q9STV0), Arabidopsis thaliana (Q9SAC6), Arabidopsis thaliana
brenda
Malinova, I.; Mahto, H.; Brandt, F.; Al-Rawi, S.; Qasim, H.; Brust, H.; Hejazi, M.; Fettke, J.
EARLY STARVATION1 specifically affects the phosphorylation action of starch-related dikinases
Plant J.
95
126-137
2018
Solanum tuberosum (Q9AWA5)
brenda
Adegbaju, M.S.; Morenikeji, O.B.; Borrego, E.J.; Hudson, A.O.; Thomas, B.N.
Differential evolution of alpha-glucan water dikinase (GWD) in plants
Plants (Basel)
9
1101
2020
Amaranthus hypochondriacus, Amborella trichopoda, Ananas comosus (A0A199UE45), Arabidopsis thaliana (Q9STV0), Auxenochlorella protothecoides (A0A087SJ57), Brachypodium distachyon, Brassica rapa, Capsella rubella, Capsicum annuum (A0A2G2YEX8), Carica papaya, Chlamydomonas reinhardtii (A0A2K3DIY0), Chondrus crispus (R7QKK2), Chromochloris zofingiensis, Citrus x clementina, Coffea arabica, Cucumis melo (A0A1S3BEF3), Dioscorea alata, Fragaria vesca, Glycine max (I1KXC2), Gossypium hirsutum, Helianthus annuus (A0A251T3N7), Hordeum vulgare, Linum usitatissimum, Malcolmia maritima, Malus domestica, Manihot esculenta (V9K6M5), Marchantia polymorpha (A0A2R6X3K3), Musa acuminata subsp. malaccensis, Myagrum perfoliatum, Nicotiana tabacum (A0A1S3YFK2), Oryza sativa Japonica Group (XM_015787980.2), Panicum miliaceum (A0A3L6S324), Panicum miliaceum, Phaseolus vulgaris (V7C6L3), Physcomitrium patens, Porphyra umbilicalis, Ricinus communis (XP_015579774.1), Selaginella moellendorffii, Solanum chacoense (A0A0V0IZQ3), Solanum lycopersicum (B5B3R3), Solanum tuberosum (Q9AWA5), Sorghum bicolor (C5Z316), Sphagnum magellanicum, Theobroma cacao (A0A061FDU7), Triticum aestivum, Vigna unguiculata, Vitis vinifera (D7TDL2), Zea mays (A0A1D6LTL9)
brenda
Chen, Y.; Sun, X.; Zhou, X.; Hebelstrup, K.H.; Blennow, A.; Bao, J.
Highly phosphorylated functionalized rice starch produced by transgenic rice expressing the potato GWD1 gene
Sci. Rep.
7
3339
2017
Solanum tuberosum (Q9AWA5)
brenda
Xu, X.; Dees, D.; Huang, X.; Visser, R.; Trindade, L.
Heterologous expression of two Arabidopsis starch dikinases in potato
Starch
70
1600324
2018
Arabidopsis thaliana (Q9STV0), Arabidopsis thaliana (Q6ZY51)
-
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.9.4)
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