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evolution
arginine kinase genes in trypanosomatids, phylogenetic analysis, overview
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
phosphoarginine and arginine kinase are the most commonly found phosphagen and phosphagen kinase in invertebrates, such as arthropods, marine invertebrates, Haemonchus contortus larvae, the entomopathogenic nematode Steinernema carpocapsae, and the protozoan parasite Trypanosoma cruzi
evolution
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phylogenetic analysis of amino acid sequences of phosphagen kinases indicate that the Myzostoma AK gene lineage differs from that of the polychaete Sabellastarte spectabilis AK, which is a dimer of creatine kinase (CK) origin. It is likely that the Myzostoma AK gene lineage was lost at an early stage of annelid evolution and that Sabellastarte AK evolved secondarily from the CK gene. Analysis of evolution of phosphagen kinases of annelids with marked diversity, overview
evolution
the enzyme belongs to the family of phosphagen kinases, molecular genetic and phylogenetic analysis, overview. The gene family has undergone extensive intron loss and gain within the suborder Rhabditina.
evolution
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the enzyme is widely distributed in invertebrate animals. The enzyme is also found in unicellular organisms, protists and bacteria, but its occurrence is intermittent among species. Detailed phylogenetic analysis, overview
evolution
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the enzyme is widely distributed in various invertebrates and many lower chordates but absent in vertebrates
evolution
two putative AK genes in the genome of Tetrahymena thermophila: one is a typical AK with a 40-kDa subunit (AK1) and the other is an unusual two-domain AK2 having an 80-kDa contiguous dimer, which appears to be the result of gene duplication and subsequent fusion
evolution
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arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
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arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
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arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
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arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
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arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
-
arginine kinases are divided into two groups. Two-domain arginine kinases are subjected to strong positive selection. 16 positively selective sites are detected and five of them show posterior probabilities of 0.95 or more. Comparative analysis finds that domain 2 might be suffered from more evolutionary selection pressure than domain 1, as most positively sites are located at domain 2. Residue Pro (positively selective site) (587P in ApAK) in domain 2 from all Vesicomyidae arginine kinases might participate in change of the synergism and in the function of its cold-adapted characteristics. The studies provide evidence of positive Darwinian selection in the two-domain arginine kinase family of Vesicomyidae clams
evolution
two distinct arginine kinase gene lineages are present in cnidarians. Phylogenetic analysis suggestes that the Corallium rubrum arginine kinase sequence has a distinct origin from that of other known cnidarian arginine kinases with unusual two-domain structure
evolution
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two distinct arginine kinase gene lineages are present in cnidarians. Phylogenetic analysis suggestes that the Corallium rubrum arginine kinase sequence has a distinct origin from that of other known cnidarian arginine kinases with unusual two-domain structure
malfunction
elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
malfunction
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larval settlement rate decreases and larval movement is inhibited in response to treatments with high concentrations of enzyme inhibitors rutin and quercetin
malfunction
RNAi knockdown of all three arginine kinase isozymes induces a growth defect that is more prominent when the cells are exposed to oxidative stress. Loss of flagellar isozyme AK1 reduces swim velocity without visible alteration of flagellar morphology. The absence of isozyme AK1 results in reduced infectivity by procyclic trypanosomes for tsetse flies
malfunction
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elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
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malfunction
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
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elimination of the total cellular arginine kinase activity by RNA interference significantly decreases growth of procyclic form Trypanosoma brucei by 90% under standard culture conditions and is lethal for this life cycle stage in the presence of hydrogen peroxide
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metabolism
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arginine kinase mainly participates in energy metabolism in invertebrates. Arginine kinase is functionally analogous to creatine kinase, EC 2.7.3.2, in vertebrates
metabolism
the opposite hormonal regulation of arginine kinase TcAK1 and arginine kinase TcAK2 is mediated by transcription factor Broad-Complex
physiological function
arginine kinase may play an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
arginine kinase is involved in the antiviral process of Bombyx mori larvae against nucleopolyhedrovirus infection
physiological function
the enzyme plays an important role in the coupling of energy production and utilization and the immune response in shrimps
physiological function
the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
physiological function
arginine kinase is a key enzyme for cellular energy metabolism, catalyzing the reversible phosphoyl transfer from phosphoarginine to ADP in invertebrates
physiological function
arginine kinase is a key enzyme for energetic balance in invertebrates and plays an important role in invertebrate physiology by buffering the ATP pool accordingly to cellular energy requirements
physiological function
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arginine kinase plays a key role in ATP buffering systems of tissues and nerves that display high and variable rates of ATP turnover
physiological function
isozyme AK1 confers a competitive advantage in infections of tsetse flies in midgut by the parasite, overview
physiological function
isozyme AK1 plays a role in the phosphoarginine shuttle, which enables a continuous energy flow to dynein for ciliary movement in Tetrahymena pyriformis
physiological function
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the enzyme is involved in the larval settlement through mediating energy supply in muscle tissues. The enzyme mainly provides energy for muscle movements and is essential for motility in arthropods
physiological function
the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
physiological function
arginine kinase AK3 is likely to be located in theciliary membrane and influences swimming velocity, presumably through the phosphoarginine shuttle system present in cilia
physiological function
arginine kinase MnAK2 may play a crucial role in the response to salinity stress in Macrobrachium nipponense. Arginine kinase plays imperative roles in innate immune feedback and stress resistance in invertebrates
physiological function
arginine kinase plays a fundamental role in energy homeostasis. The enzyme interacts with the transmembrane protein 2MIT and is involved in Drosophila melanogaster short-term memory
physiological function
arginine kinase TcAK1 and arginine kinase TcAK2 play similar roles in adult fertility and stress response
physiological function
the enzyme has a regulatory role during larval settlement. It is involved in both locomotion and substratum exploration during larval settlement. Decreased arginine kinase activity in swimming larvae leads to inhibition of larval settlement
physiological function
the enzyme is an enzyme crucial for energy metabolism, keeping the pool of phosphagens in invertebrates, and also an allergen for humans
physiological function
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the enzyme is involved in temporal and spatial ATP buffering systems. It plays an important role in physiological function and metabolic regulations, in particular tissues with high and fluctuating energy demands. Possible involvement of arginine kinases (PyAKs) in energetic homeostasis during environmental changes
physiological function
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the putative arginine kinase from Myxococcus xanthus is required for fruiting body formation and cell differentiation
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physiological function
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the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
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physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
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the phosphoarginine energy-buffering system of Trypanosoma brucei involves multiple arginine kinase isoforms with different subcellular locations. Increased arginine kinase activity improves growth of procyclic form Trypanosoma brucei during oxidative challenges with hydrogen peroxide
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additional information
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enzyme structure homology modeling and docking simulations, overview
additional information
enzyme structure homology modelling, overview
additional information
isozyme AK1 has two insertions of respectively 22 and 26 amino acids at the N- and C-terminus
additional information
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isozyme AK1 has two insertions of respectively 22 and 26 amino acids at the N- and C-terminus
additional information
residue C271 is involved in the enzyme activity and constraining the orientation of the substrate arginine. Residue T273 interacts with C271 and plays a vital role in the enzyme activity, substrate synergism, and structural stability
additional information
the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
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the active region of enzyme AK is more flexible than the overall enzyme molecule
additional information
the arginine guanidinium group makes ionic contacts with Glu225, Cys271 and a network of ordered water molecules. On the zwitterionic side of the amino acid, the backbone amide nitrogens of Gly64 and Val65 coordinate the arginine carboxylate. Glu314, one of proposed acid-base catalytic residues, does not interact with arginine in the binary complex. Residue Glu324 is located in the flexible loop 310-320 that covers the active site and only stabilizes in the ternary transition state analogue complex, LvAK-TSAC
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate
additional information
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the five residues S63, Y68, E225, C271, and E314 that interact with the arginine substrate are conserved, as well as the five Arg residues R124, R126, R229, R280 and R309 that interact with substrate ATP. Residues D62 and R193 are suggested to play a key role in stabilizing the substrate-bound structures of AK by forming an ion pair. Tyr89 is also a key residue in typical invertebrate AKs and is strictly conserved. This residue is not directly involved in substrate binding but it is located close to the site that bindswith the substrate arginine, it significantly and specifically affects guanidino substrate