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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 + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
ATP + amylopectin + H2O
?
-
phosphorylation at the C3 position of glucose residues in amylopectin
-
-
?
ATP + amylopectin + H2O
AMP + phospho-amylopectin + 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 + crystalline maltodextrin + H2O
AMP + phospho-alpha-glucosyl-maltodextrin + phosphate
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
-
-
?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
ATP + elongated glucogen + H2O
AMP + elongated phosphoglucogen + phosphate
-
-
-
-
?
ATP + granular potato starch + H2O
AMP + phosphorylated granular potato starch + phosphate
-
-
-
?
ATP + maltodextrin + H2O
?
-
crystallized maltodextrins, A- and B-type allomorphs
-
-
?
ATP + postelongated glycogen + H2O
AMP + postelongated phospho-glycogen + 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
phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
starch + ATP + H2O
AMP + phospho-starch + phosphate
additional information
?
-
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
-
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
essential step within starch metabolism. In Arabidopsis leaves starch turnover requires a close collaboration of alpha-glucan, water dikinase and phosphoglucan, water dikinase
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
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
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
the enzyme is involved in the cold-induced development of freezing tolerance in Arabidopsis
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
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
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
-
-
-
?
amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
exclusive phosphorylation of C-6 position, in vitro
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
phosphorylation at C-6 position, crystallized maltodextrin, natural starch from maize, potato, Arabidopsis, A- and B-allomorph type
-
-
?
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
-
-
?
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 followingnucleotide binding and hydrolysis
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
GWD phosphorylates the hydroxyl group at carbon atoms 6
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
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. 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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
phosphorylation at C6
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
activity required for pollen tube germination
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
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
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
4.5fold accumulation of starch and 1.8fold reduction in level of soluble sugars in absence of functional GWD
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
rescue of pollen germination in GWD-deficient mutant tomato plant
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
-
-
?
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
-
-
?
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
-
light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
light-induced GWD phosphorylation and subsequent starch breakdown only in presence of sufficient amount of nitrogen to ensure utilisation of released carbohydrate
-
-
?
ATP + alpha-glucan + H2O
AMP + phospho-alpha-glucan + phosphate
-
GWD phosphorylates the hydroxyl group at carbon atoms 6 and 3
-
-
?
ATP + amylopectin + H2O
AMP + phospho-amylopectin + phosphate
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
reaction stop by boiling
-
?
ATP + amylopectin + H2O
AMP + phospho-amylopectin + phosphate
-
-
-
-
?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
-
-
-
-
?
ATP + crystalline maltodextrin + H2O
AMP + phosphorylated crystalline maltodextrin + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
XM_015787980.2
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
XP_015579774.1
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
the enzyme is active in the wheat endosperm and contributes to the phosphorylation of wheat starch at the C-6 position
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
ATP + starch + H2O
AMP + phosphorylated starch + phosphate
-
-
-
?
phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
the enzyme is involved in degradation of transistory starch
-
-
?
phospho-amylopectin + ATP + H2O
AMP + phospho-amylopectin + phosphate
-
AtGWD3 primarily catalyzes phosphorylation at the C-3 position of the glucose unit of preferably pre-phosphorylated amylopectin substrate with lon side chains
-
-
?
starch + ATP + H2O
AMP + phospho-starch + phosphate
-
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
-
-
?
starch + ATP + H2O
AMP + phospho-starch + phosphate
-
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
-
-
?
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
?
-
not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
-
-
?
additional information
?
-
-
not involved in transient starch degradation, plants lacking AtGWD show similar starch and sugar content as wild-type plants
-
-
?
additional information
?
-
-
phosphorylation by GWD mediates phase transition from highly ordered to hydrated state glucans
-
-
?
additional information
?
-
-
phosphorylation of crystalline maltodextrin initiates solubilisation of both phosphorylated and neutral glucans
-
-
?
additional information
?
-
-
substrate-specificity defined by physical arrangements of alpha glucans and by molecular order of glucan helices
-
-
?
additional information
?
-
activity is independent of pre-phosphorylation of glucan substrate
-
-
?
additional information
?
-
-
activity is independent of pre-phosphorylation of glucan substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
GDW activity stimulates release of maltose from granular starch (by beta-amylase activity)
-
-
?
additional information
?
-
-
GWD3-SBD shows strongest binding towards alpha-cyclodextrin and no detectable affinity for linear maltooligosaccharides or for phosphorylated beta-cyclodextrin
-
-
?
additional information
?
-
the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
-
-
?
additional information
?
-
-
the activity of GWD correlates with the amount of accessible glucan chains on the starch granule surface
-
-
?
additional information
?
-
no phosphorylation of the hydroxyl group at the C2 position
-
-
?
additional information
?
-
no phosphorylation of the hydroxyl group at the C2 position
-
-
?
additional information
?
-
-
starch degradation
-
-
?
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
?
-
-
starch degradation is accompanied by modifications at the granule surface affecting the binding of R1
-
-
?
additional information
?
-
-
autocatalytic phosphorylation with beta not with gamma-phosphate
-
-
?
additional information
?
-
-
starch degradation
-
-
?
additional information
?
-
-
starch degradation
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
no phosphorylation of the hydroxyl group at the C2 position
-
-
?
additional information
?
-
-
starch degradation
-
-
?
additional information
?
-
-
enzyme binds to starch granules
-
-
?
additional information
?
-
-
enzyme involved in phosphorylation and/or degradation of starch
-
-
?
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evolution
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
-
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
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
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
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
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
AtGWD2 knockout mutants do not accumulate high amounts of starch nor have a visible growth phenotype compared to wild-type plants
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
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
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
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
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
primary enzyme required for starch phosphorylation
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
-
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
glucan, water dikinase is a key enzyme of starch metabolism
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 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
-
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
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
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 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
the enzyme is involved in starch degradation
physiological function
enzyme GWD catalyzes starch phosphorylation both in leaves and different plant storage organs
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
enzyme GWD mediates starch breakdown through glucan phosphorylation
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
-
glucan, water dikinase is the primary enzyme responsible for addition of phosphate groups to starch, in a grain-specific manner
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
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
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
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
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Arabidopsis thaliana (Q9SAC6)
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9
1101
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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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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 (Q6ZY51), Arabidopsis thaliana (Q9STV0)
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brenda