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metabolism
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adenylate kinase 2 links mitochondrial energy metabolism to the induction of the unfolded protein response
malfunction
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adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness
malfunction
although homozygous adenylate kinsase 2 mutated embryos develop without any visible defects, their growth ceases and they die before reaching the third instar larval stage
malfunction
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reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2
malfunction
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adenylate kinase 2 knockdown in larvae by RNA interference causes larval growth defects, including body weight decrease and development delay. Adenylate kinase 2 knockdown in larvae also decreases the number of circulating hemocytes
malfunction
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depletion of adenylate kinase 2 (AK2) by RNAi impairs adiponectin secretion in 3T3-L1 adipocytes, immunoglobulin M secretion in BCL1 cells, and the induction of the unfolded protein response during differentiation of both cell types. Depletion of AK2 results in changes in adipocyte energy homeostasis, but these effects do not detectably impair key adipocyte properties such as mitochondrial biogenesis and triglyceride storage
malfunction
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the absence of denylate kinase 6 reduces stem elongation but does not delay development
malfunction
rrecombinant expression of wild-type adk gene in fucose-inducible strains rescues a growth defect, but expression of the Arg89 mutant does not. Lack of functional SpAdK causes a growth defect in vivo, SpAdK deficiency abolishes pneumococcal growth
malfunction
adenylate kinase deficiency disrupts cell energetics and causes severe human diseases. Knockdown of overexpressed AK2 in human lung adenocarcinoma cells suppresses proliferation, migration, and invasion as well as induced apoptosis and autophagy
physiological function
adenylate kinase 4 is a unique member of the adenylate kinases family which shows no enzymatic activity in vitro
physiological function
maternally provided adenylate kianse 2 is sufficient for embryonic development, adenylate kinase 2 plays a critical role in adenine nucleotide metabolism in the mitochondrial intermembrane space and is essential for growth in Drosophila melanogaster
physiological function
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adenylate kinase 2 regulates cell growth, viability, and proliferation in insect growth and development
physiological function
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adenylate kinase 6 is an essential stem growth factor in Arabidopsis
physiological function
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nuclear adenylate kinase isoform is involved in ribosome biogenesis by performing ribosomal 18S RNA processing by direct interaction with ribosomal protein TcRps14
physiological function
adenylate kinases play a critical role in intercellular homeostasis by the interconversion of ATP and AMP to two ADP molecules
physiological function
SpAdK plays an essential role in pneumococcal growth and ATP synthesis, the enzyme is essential for growth through its catalytic activity, it controls cell growth via cellular energy homeostasis. SpAdK increases total cellular ATP levels regulated by fucose in the fucose-inducible strain
physiological function
adenylate kinase is an antigen that induces high cellular and antibody responses in active TB patients
physiological function
adenylate kinase is the critical enzyme in the metabolic monitoring of cellular adenine nucleotide homeostasis. It also directs adenylate kinase/AMP/adenine nucleotide translocase signaling controlling cell cycle and proliferation, and ATP energy transfer from mitochondria to distribute energy among cellular processes. Adenylate kinase 2 and mitochondrial creatine kinase interplay in malignant transformation. Adenylate kinase modulate tumor cell response to survive under oxidative stress
physiological function
adenylate kinase potentiates the capsular polysaccharide by modulating Cps2D in Streptococcus pneumoniae D39. Interaction between SpAdK and Cps2D plays an important role in enhancing Cps2D phosphorylation, which results in increased synthesis of capsular polysaccharide
physiological function
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cytosolic adenylate kinase is required for yeast viability. The relative fitness of the yeast strains is depending on the level of adenylate kinase activity
physiological function
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during seed imbibition, adenylate balance is rapidly restored from the AMP stock by the concerted action of adenylate kinase and mitochondria
physiological function
MeADK2 might play a vital role in energy homeostasis in cassava mitochondria
physiological function
XP_019937160.1
the enzyme catalyzes a principal step in adenine nucleotide metabolism and cellular energy homeostasis
physiological function
the enzyme catalyzes a principal step in adenine nucleotide metabolism and cellular energy homeostasis
physiological function
the enzyme is involved in regulating concentration of ATP in cells
physiological function
the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
physiological function
the enzyme plays an important role in cellular energy homeostasis
physiological function
the human vitreous fluid is responsible for maintaining an inflammatory status in diabetic eyes
physiological function
the reaction is a major player in cellular energy homeostasis and the isoform network of adenylate kinase plays an important role in AMP metabolic signaling circuits
physiological function
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cytosolic adenylate kinase is required for yeast viability. The relative fitness of the yeast strains is depending on the level of adenylate kinase activity
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physiological function
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adenylate kinase is an antigen that induces high cellular and antibody responses in active TB patients
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physiological function
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the enzyme plays a key role in maintaining the balance of ADP and ATP in cell
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physiological function
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the reaction is a major player in cellular energy homeostasis and the isoform network of adenylate kinase plays an important role in AMP metabolic signaling circuits
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physiological function
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the enzyme is involved in regulating concentration of ATP in cells
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additional information
Arg89 is a key active site residue, enzyme structure comparisons
additional information
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Arg89 is a key active site residue, enzyme structure comparisons
additional information
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ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. The active center of an adenylate kinase comprises separate ATP- and AMP-binding sites, and comprises ATP-binding site 2. Construction of a three-dimensional model of the CFTR NBD1-NBD2 heterodimer, molecular modelling with bound ATP molecules, overview
additional information
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enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ANK, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
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enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1DVR, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
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enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ZIN, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
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enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 2BBW, comparisons of different enzyme structures and substrate binding structures, detailed overview
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
additional information
the ligand-free enzyme structure reveals an open conformation
additional information
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
additional information
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optimization of stabilizing interactions connecting distant polypeptide regions, Lys19-Glu202 and Arg116-Glu198 ion pairs are formed in enzyme mutant AKm1, hydrophobic packing is improved by incorporating Tyr109, Val193, and Ile211 into enzyme mutant AKm2
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