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Information on EC 2.7.9.4 - alpha-glucan, water dikinase and Organism(s) Solanum tuberosum and UniProt Accession Q9AWA5
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2.7.9.4 alpha-glucan, water dikinaseIUBMB 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 beta-phosphate of ATP, which is then transferred to the glucan .
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Word Map
- 2.7.9.4
- glucans
- ribonucleotide
- deoxyribonucleotides
- alpha-glucans
- phosphoglucans
- amylopectin
- beta-amylase
-
allomorph
-
spirodela
-
beta-phosphate
- turions
-
starch-binding
- polyrhiza
- food industry
- biotechnology
The taxonomic range for the selected organisms is: Solanum tuberosum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
r1 protein, glucan water dikinase, alpha-glucan water dikinase, atgwd3, atgwd2, starch-related r1 protein, glucan water dikinase 2, glucan water dikinase 3, starch-related alpha-glucan/water dikinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glucan, water dikinase, GWD
-
-
-
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GWD
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
-
-
?
ATP + 6-O-alpha-maltosyl-beta-cyclodextrin + H2O
AMP + phospho-6-O-alpha-maltosyl-beta-cyclodextrin + phosphate
-
-
-
?
ATP + alpha-cyclodextrin + H2O
AMP + phospho-alpha-cyclodextrin + phosphate
-
-
-
?
ATP + amylose 18 + H2O
AMP + phosphorylated amylose 18 + phosphate
-
very poor substrate
-
?
ATP + amylose 24 + H2O
AMP + phosphorylated amylose 24 + phosphate
-
very poor substrate
-
?
ATP + amylose 53 + H2O
AMP + phosphorylated amylose 53 + phosphate
-
-
-
?
ATP + amylose 85 + H2O
AMP + phosphorylated amylose 85 + phosphate
-
-
-
?
ATP + beta-cyclodextrin + H2O
AMP + phospho-beta-cyclodextrin + phosphate
-
-
-
?
ATP + granular potato starch + H2O
AMP + phosphorylated granular potato starch + phosphate
-
-
-
?
ATP + potato amylopektin + H2O
AMP + phosphorylated potato amylopektin + phosphate
-
-
-
?
ATP + potato amylose + H2O
AMP + phosphorylated potato amylose + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
-
-
-
-
?
ATP + elongated glucogen + H2O
AMP + elongated phosphoglucogen + phosphate
-
-
-
-
?
ATP + maltodextrin + H2O
?
-
crystallized maltodextrins, A- and B-type allomorphs
-
-
?
ATP + postelongated glycogen + H2O
AMP + postelongated phospho-glycogen + phosphate
-
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
levels of starch phosphorylation at the C6 and C3 positions of the glucosyl residues are determined by mass spectrometry of hydrolyzed starch from tubers
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
enzyme catalyzes the phophorylation of both C-6 and C-3 position of the glucose residues
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
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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-
?
additional information
?
-
no phosphorylation of the hydroxyl group at the C2 position
-
-
?
additional information
?
-
-
autocatalytic phosphorylation with beta not with gamma-phosphate
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-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme involved in phosphorylation and/or degradation of starch
-
-
?
additional information
?
-
-
enzyme involved in phosphorylation and/or degradation of starch
-
-
?
additional information
?
-
-
starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
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-
?
additional information
?
-
-
alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
-
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
levels of starch phosphorylation at the C6 and C3 positions of the glucosyl residues are determined by mass spectrometry of hydrolyzed starch from tubers
-
-
?
additional information
?
-
-
enzyme involved in phosphorylation and/or degradation of starch
-
-
?
additional information
?
-
-
enzyme involved in phosphorylation and/or degradation of starch
-
-
?
additional information
?
-
-
starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
-
-
?
additional information
?
-
-
alpha-glucan phosphorylation enhances beta-amylolytic starch degradation and vice versa: effective starch mobilization dependent on simultaneous action of GDW and beta-amylase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
20°C: about 75% of maximal activity, 40°C: about 85% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
predominantly located at the surface of the particle of starch granule
-
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
-
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
-
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
metabolism
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
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
physiological function
enzyme GWD catalyzes starch phosphorylation both in leaves and different plant storage organs
additional information
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
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
additional information
potato lines GWD phenotype-genotype relationship, ooverview
additional information
-
potato lines GWD phenotype-genotype relationship, ooverview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GWD1_SOLTU
1464
0
163237
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphoprotein
autophosphorylation of wild-type enzyme, no histidine autophosphorylation of mutant enzyme H992A
phosphoprotein
-
large structural changes on autophosphorylation, indicating that the enzyme employs a swivelling-domain mechanism for enzymatic phosphotransfer
phosphoprotein
-
the protein possesses two vicinal phosphorylation sites, both of which are transiently phosphorylated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells and in Nicotiana tabacum leaf mesophyll cells
gene GWD, genotyping included determination of allele dosage of 193 potato lines by amplicon sequencing and microsatellite analysis, overview
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
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
Pisum sativum, Solanum tuberosum
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
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
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)
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
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
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
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
-
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
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
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
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
-
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)
Hejazi, M.; Steup, M.; Fettke, J.
The plastidial glucan, water dikinase (GWD) catalyses multiple phosphotransfer reactions
FEBS J.
279
1953-1966
2012
Arabidopsis thaliana, Solanum tuberosum
Mahlow, S.; Orzechowski, S.; Fettke, J.
Starch phosphorylation: insights and perspectives
Cell. Mol. Life Sci.
73
2753-2764
2016
Solanum tuberosum (Q9AWA5), Arabidopsis thaliana (Q9SAC6), Arabidopsis thaliana (Q9STV0)
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
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)
-
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)
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, Brassica rapa, Carica papaya, Coffea arabica, Fragaria vesca, Gossypium hirsutum, Hordeum vulgare, Linum usitatissimum, Malus domestica, Physcomitrium patens, Porphyra umbilicalis, Sphagnum magellanicum, Triticum aestivum, Vigna unguiculata, Citrus clementina, Selaginella moellendorffii, Capsella rubella, Brachypodium distachyon, Chromochloris zofingiensis, Dioscorea alata, Amborella trichopoda, Malcolmia maritima, Myagrum perfoliatum, Musa acuminata subsp. malaccensis, Theobroma cacao (A0A061FDU7), Auxenochlorella protothecoides (A0A087SJ57), Solanum chacoense (A0A0V0IZQ3), Ananas comosus (A0A199UE45), Zea mays (A0A1D6LTL9), Cucumis melo (A0A1S3BEF3), Nicotiana tabacum (A0A1S3YFK2), Helianthus annuus (A0A251T3N7), Capsicum annuum (A0A2G2YEX8), Chlamydomonas reinhardtii (A0A2K3DIY0), Marchantia polymorpha (A0A2R6X3K3), Panicum miliaceum (A0A3L6S324), Panicum miliaceum, Solanum lycopersicum (B5B3R3), Sorghum bicolor (C5Z316), Vitis vinifera (D7TDL2), Glycine max (I1KXC2), Solanum tuberosum (Q9AWA5), Arabidopsis thaliana (Q9STV0), Chondrus crispus (R7QKK2), Phaseolus vulgaris (V7C6L3), Manihot esculenta (V9K6M5), Oryza sativa Japonica Group (XM_015787980.2), Ricinus communis (XP_015579774.1)
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