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EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + alpha-glucan + H2O 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. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water Solanum tuberosum AMP + phospho-alpha-glucan + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + alpha-glucan + H2O 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. The phosphoramidate bond is acid labile, but rather stable under alkaline conditions. The gamma-phosphate group is transferred to water Arabidopsis thaliana AMP + phospho-alpha-glucan + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + alpha-glucan + H2O GWD phosphorylates the hydroxyl group at carbon atom 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. GWD-dependent phosphorylation alters the granule surface structure, which favors the action of PWD. PWD phosphorylates also non pre-phosphorylated glucan chains Arabidopsis thaliana AMP + phospho-alpha-glucan + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + crystalline maltodextrin + H2O 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. Significant phosphorylation of MDcryst by PWD requires the preceding action of GWD. GWD-dependent phosphorylation alters the granule surface structure, which favors the action of PWD Arabidopsis thaliana AMP + phospho-alpha-glucosyl-maltodextrin + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + phospho-maltodextrin + H2O only pre-phosphorylated, crystallised (insoluble) maltodextrin Arabidopsis thaliana AMP + O-phospho-[phospho-maltodextrin] + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + [phospho-alpha-glucan] the enzyme phosphorylates granular starch that has previously been phosphorylated by EC 2.7.9.4, alpha-glucan, water dikinase Arabidopsis sp. AMP + O-phospho-[phospho-alpha-glucan] + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + [phospho-alpha-glucan] the enzyme transfers the beta-phosphate of ATP to the phosphoglucan, whereas the gamma-phosphate is transferred to water. The protein phosphorylates itself with the beta-phosphate of ATP at a His residue of the enzyme, which is then transferred to the glucan Arabidopsis sp. AMP + O-phospho-[phospho-alpha-glucan] + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + [phospho-alpha-glucan] + H2O - Solanum tuberosum AMP + O-phospho-[phospho-alpha-glucan] + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + [phospho-alpha-glucan] + H2O - Arabidopsis thaliana AMP + O-phospho-[phospho-alpha-glucan] + phosphate - ?
Display the word mapDisplay the reaction diagram Show all sequences 2.7.9.5ATP + [phospho-alpha-glucan] + H2O important enzymes of starch metabolism. Catalyzes the addition of phosphate groups to amylopectin chains at the surface of starch granules, changing its physicochemical properties Arabidopsis thaliana AMP + O-phospho-[phospho-alpha-glucan] + phosphate - ?
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