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industry
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copper polyphosphate kinase hybrid nanoflower (ArPPK2-Cu3(PO4)2·3H2O nanoflower) has an application potential in industrial catalytic processes that are coupled with ADP-dependent enzymes
molecular biology
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59 power of ppk1 as a genetic marker for detection of all currently defined Candidatus Accumulibacter clades
additional information
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enviromental protection, overexpression of polyP induces resistance to mercury, poly P in leaves mediates an accumulation of mercury from mercury-contaminated soil, phytoremediation of mercury pollution
analysis
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specific and sensitive assessment of polyphosphate in mycorrhizal system of Tagetes patula inoculated with Archaeospora leptoticha with a polyphosphate kinase/luciferase system
analysis
usage of polyphosphate kinase gene ppk1 as a high-resolution genetic marker to study population structure in activated sludge of Candidatus Accumulibacter phosphatis
analysis
usage of the gene ppk as reporter gene used in monitoring of gene expression in mammalian cells, method development involving 31P-magnetic resonance spectrocopy or 31P-resonance imaging, overview
analysis
enzyme-linked assay in which His-tagged PPK2 is immobilized on a plate and then biotinylated aptamer inhibitors are added
analysis
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enzyme-linked assay in which His-tagged PPK2 is immobilized on a plate and then biotinylated aptamer inhibitors are added
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biotechnology
Thermosynechococcus vestitus
ATP supply for synthesis of D-amino acid dipeptides
biotechnology
ATP supply for synthesis of D-amino acid dipeptides
biotechnology
polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
biotechnology
polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
biotechnology
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polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
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biotechnology
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ATP supply for synthesis of D-amino acid dipeptides
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biotechnology
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polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
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drug development
Q9S646
enzyme PPK1 is an attractive therapeutic target to control infections caused by multiple drug resistant Pseudomonas aeruginosa
drug development
the enzym eis a target for inhibitor development
drug development
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the enzyme might be a potential drug target in bacteria
drug development
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the enzyme might be a potential drug target in bacteria
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environmental protection
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bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in Escherichia coli. Specific application of this process to polyphosphate is of potential application for biological phosphate removal
environmental protection
E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater
environmental protection
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E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater
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medicine
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PPK1 is necessary for survival under anaerobic conditions or oxidative stress
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 is necessary for survival under anaerobic conditions or oxidative stress
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medicine
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PPK1 is necessary for survival under anaerobic conditions or oxidative stress
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synthesis
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synthesis
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used for an ATP regeneration system for acetyl-CoA synthesis
synthesis
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used in place of pyruvate kinase and phosphoenol pyruvate for NTP regeneration followed by synthesis of sugar nucleotides in a cyclic synthesis system for oligosaccharides
synthesis
Thermosynechococcus vestitus
the enzyme is used to establih a thermostable ATP regeneration system from polyphosphate substrate, this is then used for synthesis of D-Ala-D-Ala in a coupled system with the thermostable D-alanine-D-alanine ligase TmDdl from Thermotoga maritima, a useful biocatalyst for synthesizing D-amino acid dipeptides, method development and optimization, overview
synthesis
the enzyme is useful for ATP production from polyphosphate
synthesis
a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
synthesis
a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
synthesis
construction of an ATP regeneration system from AMP using PPK2, coupled with aminoacyl proline (Xaa-Pro) synthesis catalyzed by the adenylation domain of tyrocidine synthetase TycA-A. 0.87 mM of L-Trp-L-Pro is successfully synthesized from AMP after 72 h. Addition of inorganic diphosphatase increases the reaction rate by 14fold. When the coupling reaction is applied to whole-cell reactions in Escherichia coli, ATP is successfully regenerated from AMP, and 6.7 mM of L-Trp-L-Pro is produced after 24 h with the supplementation of 10 mM AMP. Also various other L-Xaa-L-Pro an be produced
synthesis
ANU33171.1
efficient synthesis of gamma-glutamyl compounds by co-expression of gamma-glutamylmethylamide synthetase and polyphosphate kinase in engineered Escherichia coli
synthesis
energy delivery is a critical aspect of cell-free protein synthesis. The single kinase-based regeneration system simplifies cell free protein synthesis from a three-kinase system to single-kinase system, and potentially cheapens the cost of reagent preparations by using polyP instead of phosphocreatine. Incorporation of the PPK2-based NTP regeneration system into synthetic biomembrane vesicles can lead to artificial cell and proto-cell systems more akin to their natural counterparts
synthesis
enzymatic production of glutathione coupling with an ATP regeneration system based on polyphosphate kinase
synthesis
potential application for ATP regeneration in cascade reaction
synthesis
potential application for ATP regeneration in cascade reaction
synthesis
PPK2 is used for ATP regeneration to produce glutathione by a two-enzyme cascade in vitro. 47.1 mM glutathione can be synthesized with a productivity of 13.5 mM/h. ATP is regenerated approximately 471 times in the system within 3.5 h
synthesis
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potential application for ATP regeneration in cascade reaction
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synthesis
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PPK2 is used for ATP regeneration to produce glutathione by a two-enzyme cascade in vitro. 47.1 mM glutathione can be synthesized with a productivity of 13.5 mM/h. ATP is regenerated approximately 471 times in the system within 3.5 h
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synthesis
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the enzyme is useful for ATP production from polyphosphate
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synthesis
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enzymatic production of glutathione coupling with an ATP regeneration system based on polyphosphate kinase
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synthesis
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construction of an ATP regeneration system from AMP using PPK2, coupled with aminoacyl proline (Xaa-Pro) synthesis catalyzed by the adenylation domain of tyrocidine synthetase TycA-A. 0.87 mM of L-Trp-L-Pro is successfully synthesized from AMP after 72 h. Addition of inorganic diphosphatase increases the reaction rate by 14fold. When the coupling reaction is applied to whole-cell reactions in Escherichia coli, ATP is successfully regenerated from AMP, and 6.7 mM of L-Trp-L-Pro is produced after 24 h with the supplementation of 10 mM AMP. Also various other L-Xaa-L-Pro an be produced
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synthesis
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a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
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synthesis
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potential application for ATP regeneration in cascade reaction
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