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evolution
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CaAS1 and its related plant proteins all contain an AsnB domain and an ASN synthetase domain
evolution
genes PpAS1 and PpAS2 encode both class II asparagine synthetases suggesting an ancient origin of the genes in plants. Amino acid residues essential for aspartate, AMP, and glutamine binding are conserved
evolution
genes PpAS1 and PpAS2 encode both class II asparagine synthetases suggesting an ancient origin of the genes in plants. Amino acid residues essential for aspartate, AMP, and glutamine binding are conserved, except valine268, included in the AMP binding site, which has been replaced by an isoleucine in the AS2 sequence
evolution
phylogenetic analysis has grouped ASN1 in dicot-subclass I while ASN2 and ASN3 are placed in dicot-subclass II
evolution
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phylogenetic analysis has grouped ASN1 in dicot-subclass I while ASN2 and ASN3 are placed in dicot-subclass II
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malfunction
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salt tolerance of Arabidopsis knockout mutant with T-DNA insertion in ASN2 gene encoding asparagines synthetase is investigated. Results indicate that the knockout mutant is impaired in nitrogen assimilation and translocation under salt treatment
malfunction
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silencing of CaAS1 gene results in enhanced susceptibility to Xanthomonas campestris pv. vesicatoria infection, phenotypes, overview
malfunction
silencing of the BmASNS gene enhances the sensitivity of silkworm cells to amino acid starvation. Ectopic overexpression of BmASNS gene effectively inhibits cell growth in silkworm cells, whereas its overexpression can rescue cell growth upon amino acid deprivation treatment. Silkworm cells lacking BmASNS under the condition of amino acid deprivation show severely impaired proliferation
malfunction
asparagine synthetase deficiency, ASD, is a neurological disorder having severe impacts on psychomotor development and mortality at an early age. Children with mutations in the ASNS gene exhibit developmental delays, intellectual disability, microcephaly, intractable seizures, and progressive brain atrophy. Mutations in the ASNS gene have been clinically associated with asparagine synthetase deficiency (ASD), phenotype. Neurologic disorder associated with asparagine synthetase deficiency (ASD). The transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Role of ATF4 in tumor cell survival and proliferation, ATF4 knockdown causes reduced survival in HT-1080 fibrosarcoma and DLD-1 colorectal adenocarcinoma cells in the absence of nonessential amino acids. Reduced proliferative capacity and increased apoptosis correlate with lower ASNS expression in the ATF4-deficient cells. Supplementation of the tumor cells with asparagine, but not other amino acids, leads to increased cell survival. Role of ASNS activity in modulating tumor growth
malfunction
enzyme AS-A ablation drives parasites auxotrophic to asparagine, but LiAS-A is not detrimental for parasite survival, growth or infectivity. The parasite burden in the spleen and liver of female BALB/c mice is not statistically different in LiASA mutants when compared to the wild-type
malfunction
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knockdown of asparagine synthetase (ASNS) leads to cell death even in the presence of glutamine, which can be reversed by addition of exogenous asparagine. Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion. ASNS knockdown leads to profound apoptosis even in the presence of glutamine. Addition of extracellular asparagine completely restored cell survival and proliferation. Clinically, the expression of ASNS correlates with the progression of disease and poor prognosis of glioma and neuroblastoma patients. In neuroblastoma with unfavourable prognosis, ASNS expression is significantly higher. Asparagine-induced suppression of apoptosis: asparagine addition to glutamine-deprived cells alters the transcriptional response, suppressing the induction of the reported UPR effectors CHOP and XBP1 while maintaining the transcriptional induction of adaptive components of the UPR-response such as ASNS and HERPUD1. At the protein level, exogenous addition of asparagine suppresses CHOP induction without altering ATF4 accumulation or upstream eIF2alpha phosphorylation
malfunction
no visible phenotype is detected for the asn3-1 and asn3-2 mutant. Both asn3-1 and asn3-2 rosette leaves contain wild-type levels of chlorophyll and ammonium content, indicating that ASN3 disruption does not cause a defective nitrogen status during vegetative growth. During seed development, leaves and stems serve as source tissues to supply nitrogen resources to developing siliques which in turn deliver nitrogen to seeds. When compared to wild-type seeds, asn3-1 seeds display reduced glutamine (by 30%), asparagine (20%) and aspartate (20%) contents while exhibiting increased glutamate (10%) amounts
malfunction
retrotransposon-mediated knockout mutants lacking AS1 show slight stimulation of shoot length and slight reduction in root length at the seedling stage. On the other hand, the mutation causes an approximately 80-90% reduction in free asparagine content in both roots and xylem sap
malfunction
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enzyme AS-A ablation drives parasites auxotrophic to asparagine, but LiAS-A is not detrimental for parasite survival, growth or infectivity. The parasite burden in the spleen and liver of female BALB/c mice is not statistically different in LiASA mutants when compared to the wild-type
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malfunction
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no visible phenotype is detected for the asn3-1 and asn3-2 mutant. Both asn3-1 and asn3-2 rosette leaves contain wild-type levels of chlorophyll and ammonium content, indicating that ASN3 disruption does not cause a defective nitrogen status during vegetative growth. During seed development, leaves and stems serve as source tissues to supply nitrogen resources to developing siliques which in turn deliver nitrogen to seeds. When compared to wild-type seeds, asn3-1 seeds display reduced glutamine (by 30%), asparagine (20%) and aspartate (20%) contents while exhibiting increased glutamate (10%) amounts
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metabolism
Asn is a major amino acid in maize and since AsnS is the primary means of Asn synthesis in plants it plays a very important role in nitrogen metabolism
metabolism
asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA, EC 6.3.1.1), and the other is asparagine synthetase B (AsnB, EC 6.3.5.4) that uses glutamine or ammonia as a nitrogen source. Sequence-based analysis suggests that Leishmania spp. possess the asparagine tRNA synthetase paralogue asparagine synthetase A (LdASNA) that is ammonia-dependent, but enzyme LdASNA from Leishmania donovani is both ammonia- and glutamine-dependent, EC 6.3.5.4
metabolism
asparagine synthetase (AS) is responsible for the conversion of aspartate into Asn in an ATP-dependent manner, using ammonia or glutamine as a nitrogen source. There are two structurally distinct AS: the strictly ammonia-dependent type A, and the type B, which preferably uses glutamine
metabolism
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asparagine synthetase (AS) is responsible for the conversion of aspartate into Asn in an ATP-dependent manner, using ammonia or glutamine as a nitrogen source. There are two structurally distinct AS: the strictly ammonia-dependent type A, and the type B, which preferably uses glutamine
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metabolism
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asparagine is formed by two structurally distinct asparagine synthetases in prokaryotes. One is the ammonia-utilizing asparagine synthetase A (AsnA, EC 6.3.1.1), and the other is asparagine synthetase B (AsnB, EC 6.3.5.4) that uses glutamine or ammonia as a nitrogen source. Sequence-based analysis suggests that Leishmania spp. possess the asparagine tRNA synthetase paralogue asparagine synthetase A (LdASNA) that is ammonia-dependent, but enzyme LdASNA from Leishmania donovani is both ammonia- and glutamine-dependent, EC 6.3.5.4
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physiological function
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Arabidopsis knockout mutant with T-DNA insertion in ASN2 gene, subject to 100 mM NaCl stress for 6 to 24 h. The salt treatment decreases chlorophyll and soluble protein contents, and increases ammonium level in the asn2-1 leaves. The salinity induces ASN1 mRNA level in the wild-type and asn2-1 leaves. The salt treatment inhibits the transcript and protein levels of chloroplastic glutamine synthetase 2, EC 6.3.1.2 in the wild-type and asn2-1 leaves
physiological function
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silencing of the gene encoding AS1 results in enhanced susceptibility to Xanthomonas campestris pv. vesicatoria infection. Transgenic Arabidopsis thaliana plants that overexpress CaAS1 exhibit enhanced resistance to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis. Increased CaAS1 expression influences early defense responses in diseased leaves, including increased electrolyte leakage, reactive oxygen species and nitric oxide burst. In CaAS1-silenced pepper and/or CaAS1-overexpressing Arabidopsis, CaAS1-dependent changes in asparagine levels correlate with increased susceptibility or defense responses to microbial pathogens, respectively
physiological function
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asparagine synthetase 1 is essential for plant defense to microbial pathogens. Increased CaAS1 expression influences early defense responses in diseased leaves, including increased electrolyte leakage, reactive oxygen species and nitric oxide bursts. In plants, increased conversion of aspartate to asparagine appears to be associated with enhanced resistance to bacterial and oomycete pathogens, phenotypes, overview
physiological function
BmAsns protein negatively regulates silkworm cell proliferation. The recovery of cell growth by overexpressed BmAsns protein is due to the rapid turnover of autophagic vacuoles in the cells
physiological function
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elevated expression of ASNS protein is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia and may be a predictive factor in drug sensitivity for certain solid tumors as well. Activation of the GCN2-eIF2-ATF4 signaling pathway, leading to increased ASNS expression, appears to be a component of solid tumor adaptation to nutrient deprivation and/or hypoxia, roles of the enzyme in fetal development, tissue differentiation, and tumor growth, overview. Possible correlation between ASNase sensitivity and the DNA methylation status of the ASNS gene
physiological function
the expression of PpAS1 is regulated by developmental and environmental factors
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine, isozyme TaASN1 is an active asparagine synthetase, producing asparagine and glutamate from glutamine and aspartate, reaction modeling. There are large differences in the free asparagine concentration of grain from different wheat varieties
physiological function
asparagine synthesis is catalyzed by the enzyme asparagine synthetase, and occurs by the ATP-dependent transfer of the amino group of glutamine to a molecule of aspartate to generate glutamate and asparagine, isozyme TaASN2 is an active asparagine synthetase, producing asparagine and glutamate from glutamine and aspartate, reaction modeling, There are also large differences in the free asparagine concentration of grain from different wheat varieties
physiological function
asparagine synthetase (ASNS) catalyzes the synthesis of asparagine and glutamate from aspartate and glutamine in an ATP-dependent amidotransferase reaction
physiological function
asparagine synthetase (ASNS) catalyzes the synthesis of asparagine and glutamate from aspartate and glutamine in an ATP-dependent amidotransferase reaction. Elevated ASNS protein expression is associated with resistance to asparaginase therapy in childhood acute lymphoblastic leukemia. Regulation of ASNS expression, overview. transcription factor ATF4 binds to an enhancer element within the proximal promoter of the ASNS gene and activates transcription. Asparagine depletion activates the amino acid response, AAR, whereas endoplasmic reticulum stress activates the unfolded protein response, UPR
physiological function
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asparagine synthetase (ASNS) plays an important role during tumor cell accumulation and progression by maintaining cell viability. The enzyme synthesizes asparagine de novo from aspartate and glutamine. Asparagine plays a critical role in regulating cellular adaptation to glutamine depletion. The anti-apoptotic function of glutamine depends on the ability of asparagine synthetase to maintain glutamine-dependent biosynthesis of asparagine. Transcription factor ATF4 induces asparagine synthetase which results in glutamine-dependent asparagine synthesis from aspartate, in turn asparagine accumulation then suppresses GCN2 and reduces ATF4
physiological function
asparagine synthetase transfers the amide group of glutamine to aspartate, forming asparagine and glutamate. Asparagine, glutamine, aspartate and glutamate are important nitrogen carriers transported in the phloem, asparagine is a major nitrogen transporter since it contains more nitrogen per carbon (2N:4C) compared to glutamine (2N:5C), aspartate (1N:4C) and glutamate (1N:5C). Role of isozyme ASN3-encoded asparagine synthetase during vegetative growth, seed development and germination of Arabidopsis thaliana, overview
physiological function
asparagine synthetase1, but not asparagine synthetase2, is responsible for the biosynthesis of asparagine following the supply of ammonium to rice roots
physiological function
asparagine synthetase1, but not asparagine synthetase2, is responsible for the biosynthesis of asparagine following the supply of ammonium to rice roots. AS1 is apparently coupled to the primary assimilation of NH+4 in rice roots
physiological function
enzyme LdASNA is essential for survival of the Leishmania parasite
physiological function
Leishmania infantum encodes for a functional AS-A enzyme, which uses either ammonia or glutamine as nitrogen donor for asparagine synthesis. LiAS-A is required for promastigotes growth only in asparagine limiting conditions
physiological function
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Leishmania infantum encodes for a functional AS-A enzyme, which uses either ammonia or glutamine as nitrogen donor for asparagine synthesis. LiAS-A is required for promastigotes growth only in asparagine limiting conditions
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physiological function
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asparagine synthetase transfers the amide group of glutamine to aspartate, forming asparagine and glutamate. Asparagine, glutamine, aspartate and glutamate are important nitrogen carriers transported in the phloem, asparagine is a major nitrogen transporter since it contains more nitrogen per carbon (2N:4C) compared to glutamine (2N:5C), aspartate (1N:4C) and glutamate (1N:5C). Role of isozyme ASN3-encoded asparagine synthetase during vegetative growth, seed development and germination of Arabidopsis thaliana, overview
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physiological function
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enzyme LdASNA is essential for survival of the Leishmania parasite
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additional information
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human enzyme activity is highly regulated in response to cell stress, primarily by increased transcription from a single gene located on chromosome 7, ASNS transcription control by C/EBP-ATF response element within the promoter. Protein limitation or an imbalanced dietary amino acid composition activate the ASNS gene through the amino acid response, a process that is replicated in cell culture through limitation for any single essential amino acid
additional information
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transgenic Arabidopsis thaliana plants that overexpress CaAS1 exhibit enhanced resistance to Pseudomonas syringae pv. tomato DC3000 and Hyaloperonospora arabidopsidis
additional information
enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
additional information
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enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
additional information
glutamine binds in a manner so that the carboxamide group is oriented toward the interface of the two domains to allow the transfer of an ammonia group from glutamine to aspartate
additional information
glutamine is predicted to bind in a manner so that the carboxamide group is oriented toward the interface of the two domains to allow the transfer of an ammonia group from glutamine to aspartate
additional information
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enzyme structure homology modeling, structure and sequence comparisons of the enzymes from Leishmania infantum and Leishmania major, overview
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