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evolution
arginine decarboxylases belong to a family of fold III PLP (pyridoxal 5'-phosphate)-dependent decarboxylases
evolution
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ODC is the major route to polyamine formation in the Chlamydomonas CC-406 cell-wall mutant, in contrast to the preferential ADC route reported for Chlorella vulgaris, suggesting that significant species differences exist in biosynthetic pathways which modulate endogenous polyamine levels in green algae
evolution
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arginine decarboxylases belong to a family of fold III PLP (pyridoxal 5'-phosphate)-dependent decarboxylases
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evolution
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ODC is the major route to polyamine formation in the Chlamydomonas CC-406 cell-wall mutant, in contrast to the preferential ADC route reported for Chlorella vulgaris, suggesting that significant species differences exist in biosynthetic pathways which modulate endogenous polyamine levels in green algae
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malfunction
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mutants overexpressing arginine decarboxylase 2 display dwarfism and late flowering
malfunction
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an adiA deletion strain does not show any survival at pH 2.3. Lack of AdiA does not impair systemic infection
malfunction
adc2 mutants show increased basal expression of salicylic acid and jasmonic acid-dependent PR genes. Simultaneous knockout of both AtADC genes leads to a lethal phenotype. Pseudomonas viridiflava strain Pvalb8 does not affect ADC activity of wild-type plants, but causes a 50% decrease in ADC activity of adc1-3 mutants. In contrast, Pseudomonas viridiflava strain Pvalb8 infection enhances ADC activity of adc2-3 1.3fold. The lack of a functional ADC1 or ADC2 gene does not affect Pseudomonas viridiflava propagation in Arabidopsis thaliana plants. Altered free and conjugated polyamine levels of wild-type Col-0 Arabidopsis thaliana and adc mutants in response to Pseudomonas viridiflava infection, overview
malfunction
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double knockdown of ODC1 (EC 4.1.1.17) and ADC (MAO-ODC1:ADC) results in two phenotypes of conceptuses (a or b): 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. In vivo knockdown of translation of ODC1 and ADC mRNAs individually and in combination affects the abundance of polyamines in the uterine lumen
malfunction
inactivation of two arginine decarboxylases results in reduction of spermidine content and increases biofilm formation in Synechocystis sp. strain PCC 6803. Disruption of the adc genes in Synechocystis results in formation of biofilms even under non-stress conditions, e.g. the absence of salt, while salt stress decreases polyamine content in Synechocystis
malfunction
inactivation of two arginine decarboxylases results in reduction of spermidine content and increases biofilm formation in Synechocystis sp. strain PCC 6803. Disruption of the adc genes in Synechocystis results in formation of biofilms even under non-stress conditions, e.g. the absence of salt, while salt stress decreases the polyamine content in Synechocystis
malfunction
mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium. Disruption of polyamine biosynthetic genes including speA leads to delayed growth in various bacterial species. In contrast to the presence of intracellular spermidine as the sole polyamine in wild-type strain JCM 13471 and DELTA tdk mutant strain MS416, spermidine is barely detected in MS531. The remaining intracellular spermidine level in MS531 may be attributable to the spermidine import from polyamine-reduced medium via a predicted ATP-binding cassette transporter of spermidine, PotABCD
malfunction
pathogen-induced putrescine accumulation is blocked in adc1 mutants. Simultaneous knockout of both AtADC genes leads to a lethal phenotype. Pseudomonas viridiflava strain Pvalb8 does not affect ADC activity of wild-type plants, but causes a 50% decrease in ADC activity of adc1-3 mutants. In contrast, Pseudomonas viridiflava strain Pvalb8 infection enhances ADC activity of adc2-3 1.3fold. The lack of a functional ADC1 or ADC2 gene does not affect Pseudomonas viridiflava propagation in Arabidopsis thaliana plants. Altered free and conjugated polyamine levels of wild-type Col-0 Arabidopsis thaliana and adc mutants in response to Pseudomonas viridiflava infection, overview
malfunction
inactivation of the speA gene impairs diazotrophic growth
malfunction
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adc2 mutants show increased basal expression of salicylic acid and jasmonic acid-dependent PR genes. Simultaneous knockout of both AtADC genes leads to a lethal phenotype. Pseudomonas viridiflava strain Pvalb8 does not affect ADC activity of wild-type plants, but causes a 50% decrease in ADC activity of adc1-3 mutants. In contrast, Pseudomonas viridiflava strain Pvalb8 infection enhances ADC activity of adc2-3 1.3fold. The lack of a functional ADC1 or ADC2 gene does not affect Pseudomonas viridiflava propagation in Arabidopsis thaliana plants. Altered free and conjugated polyamine levels of wild-type Col-0 Arabidopsis thaliana and adc mutants in response to Pseudomonas viridiflava infection, overview
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malfunction
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pathogen-induced putrescine accumulation is blocked in adc1 mutants. Simultaneous knockout of both AtADC genes leads to a lethal phenotype. Pseudomonas viridiflava strain Pvalb8 does not affect ADC activity of wild-type plants, but causes a 50% decrease in ADC activity of adc1-3 mutants. In contrast, Pseudomonas viridiflava strain Pvalb8 infection enhances ADC activity of adc2-3 1.3fold. The lack of a functional ADC1 or ADC2 gene does not affect Pseudomonas viridiflava propagation in Arabidopsis thaliana plants. Altered free and conjugated polyamine levels of wild-type Col-0 Arabidopsis thaliana and adc mutants in response to Pseudomonas viridiflava infection, overview
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malfunction
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mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium. Disruption of polyamine biosynthetic genes including speA leads to delayed growth in various bacterial species. In contrast to the presence of intracellular spermidine as the sole polyamine in wild-type strain JCM 13471 and DELTA tdk mutant strain MS416, spermidine is barely detected in MS531. The remaining intracellular spermidine level in MS531 may be attributable to the spermidine import from polyamine-reduced medium via a predicted ATP-binding cassette transporter of spermidine, PotABCD
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metabolism
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agmatine is synthesized by the arginine decarboxylase pathway, but is essentially undetectable if the aguBA operon is left intact
metabolism
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agmatine is synthesized by the arginine decarboxylase pathway, but is essentially undetectable if the aguBA operon is left intact
metabolism
arginine decarboxylase (ADC) is the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway, biosynthetic polyamine pathway, overview
metabolism
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arginine decarboxylase is a key enzyme in the biosynthesis of putrescine and thus polyamines
metabolism
bacteria and plants possess an alternative pathway for putrescine biosynthesis from arginine through the action of arginine decarboxylase (Adc) catalyzing the initial step. The product of that reaction, agmatine, is subsequently converted to putrescine, spermidine, and spermine via a series of steps in the polyamine synthetic pathway. The two arginine decarboxylases, isozymes Adc1 and Adc2, possess function in the polyamine synthesis pathway, there is a negative correlation between biofilm formation and polyamine content
metabolism
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FcWRKY70 functions in drought tolerance by, at least partly, promoting production of putrescine via regulating ADC expression
metabolism
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FcWRKY70 functions in drought tolerance by, at least partly, promoting production of putrescine via regulating ADC expression
metabolism
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FcWRKY70 functions in drought tolerance by, at least partly, promoting production of putrescine via regulating ADC expression
metabolism
L-arginine formed by ADC may be transported out from cytosol to extracellular milieu by a transporter protein, AdiC. The metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment
metabolism
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putrescine is the major polyamine in both free (88%) and membrane-bound fractions (93%) in Chlamydomonas reinhardtii, while norspermidine is the next most abundant in these fractions accounting for 11% and 6%, respectively. Low levels of diaminopropane, spermidine and spermine are also observed although no cadaverine or norspermine are detected. Ornithine decarboxylase (ODC, EC 4.1.1.17) activity is almost five times higher than arginine decarboxylase (ADC) and is the major route of putrescine synthesis
metabolism
the enzyme is involved in synthesis of homospermidine
metabolism
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L-arginine formed by ADC may be transported out from cytosol to extracellular milieu by a transporter protein, AdiC. The metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment
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metabolism
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putrescine is the major polyamine in both free (88%) and membrane-bound fractions (93%) in Chlamydomonas reinhardtii, while norspermidine is the next most abundant in these fractions accounting for 11% and 6%, respectively. Low levels of diaminopropane, spermidine and spermine are also observed although no cadaverine or norspermine are detected. Ornithine decarboxylase (ODC, EC 4.1.1.17) activity is almost five times higher than arginine decarboxylase (ADC) and is the major route of putrescine synthesis
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physiological function
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high putrescine accumulation by overexpression of ADC2 results in reduced water loss
physiological function
in transgenic plants expressing ADC, putrescine synthesis is enhanced even under normal conditions, stress results in the trigger level being exceeded and the accumulation of spermidine and spermine leads to the restoration of normal growth and development, even under stress
physiological function
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AdiA promotes survival of Salmonella at pH 2.3
physiological function
higher level of hexahistidine tagged human ADC transgene expression completely trigger the endogenous agmatine synthesis during H2O2 injury thus protecting NIH3T3 cells against cytotoxicity
physiological function
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the Bacillus subtilis biosynthetic aspartate aminotransferase fold arginine decarboxylase is essential for biofilm formation
physiological function
a gene disruptant lacking arginine decarboxylase is constructed, showing that it grows only in the medium in the presence of agmatine but not in the absence of agmatine. The results indicates that agmatine is essential for the cell growth of Thermococcus kodakaraensis
physiological function
enzyme is able to restor acid shock survival in a transgenic Escherichia coli DeltaadiA mutant
physiological function
Helicobacter pylori uses arginine in an acid response mechanism required for its growth in acid conditions
physiological function
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increases in arginine decarboxylase/agmatinase mRNA levels and in the translation of agmatinase mRNA among conceptuses in ornithine decarboxylase 1 knockdown in conceptusses compensates for the loss of ODC1
physiological function
overexpression in an Arabidopsis thaliana arginine decarboxylase mutant adc1-1 promotes putrescine synthesis in the transgenic line and the stomatal density is reverted to that in the wild type. The transgenic line shows enhanced resistance to high osmoticum, dehydration, long-term drought, and cold stress compared with the wild type and the mutant. The accumulation of reactive oxygen species in the transgenic line is appreciably decreased under the stresses. Plants of the transgenic line have longer roots than the wild type and the mutant under both normal and stressful conditions, consistent with larger cell number and length of the root meristematic zone
physiological function
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Xanthomonas campestris pv vesicatoria effector AvrBsT induces a hypersensitive cell death in pepper. Arginine decarboxylase isoform ADC1 is an AvrBsT-interacting protein, which is early and strongly induced in incompatible interactions between pepper and Xanthomonas campestris. The ADC1-AvrBsT complex is localized to the cytoplasm. Transient coexpression of ADC1 with avrBsT in Nicotiana benthamiana leaves specifically enhance AvrBsT-triggered cell death, accompanied by an accumulation of polyamines, nitric oxide, and hydrogen peroxide bursts. ADC1 silencing in pepper leaves significantly compromises NO and H2O2 accumulation and cell death induction, leading to the enhanced avirulent Xcv growth during infection. The levels of salicylic acid, polyamines, and g-aminobutyric acid, and the expression of defense response genes during avirulent Xcv infection, are distinctly lower in ADC1-silenced plants than those in the empty vector control plants
physiological function
a gene deletion strain is auxotrophic for agmatine and requires 5 microM agmatine for full growth. Partial growth is observed at lower agmatine concentrations, but no growth is observed below 1 microM agmatine. Polyamines such as putrescine, spermidine, cadaverine, or ornithine do not rescue the growth defect
physiological function
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agmatine, an endogenous polyamine catalyzed from L-arginine by arginine decarboxylase (ADC), is a neuromodulator that protects neurons/glia against various injuries. Agmatine, is naturally found in the mammalian central nervous system (CNS) and acts as a multifunctional neuromodulator. It is packed into synaptic vesicles and released from synaptosomes by neuronal depolarization. Agmatine can stimulate alpha2-adrenergic and imidazoline receptors. Retroviral expression of human arginine decarboxylase reduces oxidative stress injury in mouse cortical astrocytes
physiological function
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arginine decarboxylase (ADC) is a key enzyme in the central agmatinergic system
physiological function
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FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene. FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene
physiological function
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FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene. FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene
physiological function
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FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene. FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene
physiological function
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functional roles of ornithine decarboxylase (EC 4.1.1.17) and arginine decarboxylase during the peri-implantation period of pregnancy in sheep. Polyamines stimulate DNA transcription and mRNA translation for protein synthesis in trophectoderm cells, as well as proliferation and migration of cells. Therefore, they are essential for development and survival of conceptuses (embryo/fetus and placenta). The ovine conceptus produces polyamines via classical and non-classical pathways. In the classical pathway, arginine (Arg) is transformed into ornithine, which is then decarboxylated by ornithine decarboxylase (ODC1) to produce putrescine which is the substrate for the production of spermidine and spermine. In the non-classical pathway, Arg is converted to agmatine (Agm) by arginine decarboxylase (ADC), and Agm is converted to putrescine by agmatinase (AGMAT)
physiological function
gene speA encodes a putative arginine decarboxylase, an enzyme necessary for spermidine biosynthesis in cells
physiological function
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human ornithine decarboxylase paralogue (ODC-like protein, ODCp or ODC paralogue), which has been suggested to function either as mammalian arginine decarboxylase, ADC, or ornithine decarboxylase, ODC, is actually an antizyme inhibitor but not an arginine or ornithine decarboxylase. Human ODCp has no intrinsic ADC activity. ODCp acts as a regulator of ODC activity and inhibits its proteasomal degradation. ODCp is degraded by ubiquitination like AZI (AZ inhibitor)
physiological function
in Arabidopsis thaliana, putrescine is synthesised exclusively by arginine decarboxylase (ADC) catalyzing decarboxylation of arginine. Arginine decarboxylase exists as two isoforms (ADC1 and 2) that are differentially regulated by abiotic stimuli and that play a role in defence against pathogens and participate in Arabidopsis defence against Pseudomonas viridiflava. ADC2 contributes to a much higher extent than ADC1 to basal ADC activity and putrescine biosynthesis
physiological function
in bacteria agmatine serves as a precursor to polyamine synthesis and enhances biofilm development in some strains of the respiratory pathogen Pseudomonas aeruginosa. Agmatine is at the center of a competing metabolism in the human lung during airways infections and is influenced by the metabolic phenotypes of the infecting pathogens, e.g. Pseudomonas aeruginosa. The agu2ABCA' operon in Pseudomonas aeruginosa has a mechanism to detect extracellular agmatine and react by augmenting its biofilm. Pseudomonas aeruginosa encounters agmatine in lung infections, and this triggers planktonic pseudomonads to form a biofilm
physiological function
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in humans, enzyme-produced agmatine is a neurotransmitter with affinities towards alpha2-adrenoreceptors, serotonin receptors, and may inhibit nitric oxide synthase. Agmatine exposure to inflammatory cells and in mice demonstrate its role as a direct immune activator with effects on TNF-alpha production, likely through NF-kappaB activation
physiological function
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in humans, enzyme-produced agmatine is a neurotransmitter with affinities towards alpha2-adrenoreceptors, serotonin receptors, and may inhibit nitric oxide synthase. Agmatine is at the center of a competing metabolism in the human lung during airways infections and is influenced by the metabolic phenotypes of the infecting pathogens, e.g. Pseudomonas aeruginosa
physiological function
of the two isozymes in Synechocystis sp. PCC 6803, Adc2 has high arginine decarboxylase activity, whereas Adc1 is much less active
physiological function
of the two isozymes in Synechocystis sp. PCC 6803, Adc2 has high arginine decarboxylase activity, whereas Adc1 is much less active. Adc2 is the major arginine decarboxylase, Adc2 activity leads to inhibition of biofilm formation
physiological function
the arginine decarboxylase enzyme (ADC) carries out the production of agmatine from arginine, which is the precursor of the first polyamine known as putrescine. Subsequently, putrescine is turned into the higher polyamines, spermidine and spermine. In Arabidopsis thaliana polyamine production occurs only from arginine, and this step is initiated by two ADC paralogues, AtADC1 and AtADC2. Polyamine production is essential for Arabidopsis thaliana life cycle
physiological function
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the enzyme is active during growth and somatic embryogenesis and contributes to polyamine biosynthesis, its activity lead to putrescine and, subsequently, to spermidine and spermine formation
physiological function
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the enzyme plays a role in cold tolerance in Poncirus trifoliata. ADC is a key enzyme responsible for the synthesis of putrescine
physiological function
the enzyme plays a role in cold tolerance in Poncirus trifoliata. ADC is a key enzyme responsible for the synthesis of putrescine
physiological function
the enzyme plays a role in cold tolerance in Poncirus trifoliata. ADC is a key enzyme responsible for the synthesis of putrescine
physiological function
the enzyme specific activity or the steady-state accumulation of ADC transcripts are markedly changed by photo-heterotrophic growth mode, salt stress under normal growth light or high-light intensity and stresses due to high temperature or iron deficiency. There is no general relationship between steady-state transcript accumulation and enzyme activity under the conditions studied, since both parameters are not regulated in a similar manner. The enzymatic activity of Synechocystis ADCs is posttranslationally regulated
physiological function
the metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment. To neutralize the pH of the stomach, it transports L-arginine (+1 charge) into the cell and agmatine (+2 charge) out of the cell, which results in the export of 1 proton during each turnover and thus the bacteria can survive in the acidic environment
physiological function
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the Bacillus subtilis biosynthetic aspartate aminotransferase fold arginine decarboxylase is essential for biofilm formation
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physiological function
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in Arabidopsis thaliana, putrescine is synthesised exclusively by arginine decarboxylase (ADC) catalyzing decarboxylation of arginine. Arginine decarboxylase exists as two isoforms (ADC1 and 2) that are differentially regulated by abiotic stimuli and that play a role in defence against pathogens and participate in Arabidopsis defence against Pseudomonas viridiflava. ADC2 contributes to a much higher extent than ADC1 to basal ADC activity and putrescine biosynthesis
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physiological function
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Helicobacter pylori uses arginine in an acid response mechanism required for its growth in acid conditions
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physiological function
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gene speA encodes a putative arginine decarboxylase, an enzyme necessary for spermidine biosynthesis in cells
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physiological function
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in bacteria agmatine serves as a precursor to polyamine synthesis and enhances biofilm development in some strains of the respiratory pathogen Pseudomonas aeruginosa. Agmatine is at the center of a competing metabolism in the human lung during airways infections and is influenced by the metabolic phenotypes of the infecting pathogens, e.g. Pseudomonas aeruginosa. The agu2ABCA' operon in Pseudomonas aeruginosa has a mechanism to detect extracellular agmatine and react by augmenting its biofilm. Pseudomonas aeruginosa encounters agmatine in lung infections, and this triggers planktonic pseudomonads to form a biofilm
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physiological function
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the metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment. To neutralize the pH of the stomach, it transports L-arginine (+1 charge) into the cell and agmatine (+2 charge) out of the cell, which results in the export of 1 proton during each turnover and thus the bacteria can survive in the acidic environment
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physiological function
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a gene deletion strain is auxotrophic for agmatine and requires 5 microM agmatine for full growth. Partial growth is observed at lower agmatine concentrations, but no growth is observed below 1 microM agmatine. Polyamines such as putrescine, spermidine, cadaverine, or ornithine do not rescue the growth defect
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additional information
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ADC in vivo activity varies with auxin concentration in the medium, overview
additional information
analysis of agatine content in clinical isolates PA002. PA004, PA005, PA006, and PA016, and PA14 wild-type strain, as well as the PA14 aguA-Gm, DELTAagu2ABCA' mutant strain, which lacks a functional agmatine deiminase
additional information
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analysis of agatine content in clinical isolates PA002. PA004, PA005, PA006, and PA016, and PA14 wild-type strain, as well as the PA14 aguA-Gm, DELTAagu2ABCA' mutant strain, which lacks a functional agmatine deiminase
additional information
Cys487, a conserved residue located at the active-site, is involved in the catalysis, with a pKa value of about 7.2. The homology model of the protein shows conserved alpha/beta TIM barrel and beta-sandwich domains, which are characteristic features of fold III decarboxylases. Cys487 has a marginal role in the stability. Helicobacter pylori ADC homology modeling and docking studies, overview
additional information
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Cys487, a conserved residue located at the active-site, is involved in the catalysis, with a pKa value of about 7.2. The homology model of the protein shows conserved alpha/beta TIM barrel and beta-sandwich domains, which are characteristic features of fold III decarboxylases. Cys487 has a marginal role in the stability. Helicobacter pylori ADC homology modeling and docking studies, overview
additional information
isozymes AtADC1 and AtADC2 are able to form homodimers in the cytosol and chloroplast. The formation of AtADC1/AtADC2 heterodimers occurs with similar subcellular localization than homodimers. Both ADC proteins are located in the same cell compartments, and they are able to form protein interaction complexes with each other
additional information
isozymes AtADC1 and AtADC2 are able to form homodimers in the cytosol and chloroplast. The formation of AtADC1/AtADC2 heterodimers occurs with similar subcellular localization than homodimers. Both ADC proteins are located in the same cell compartments, and they are able to form protein interaction complexes with each other
additional information
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isozymes AtADC1 and AtADC2 are able to form homodimers in the cytosol and chloroplast. The formation of AtADC1/AtADC2 heterodimers occurs with similar subcellular localization than homodimers. Both ADC proteins are located in the same cell compartments, and they are able to form protein interaction complexes with each other
additional information
protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC1
additional information
protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC1
additional information
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protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC1
additional information
protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC2
additional information
protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC2
additional information
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protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and NtADC2
additional information
protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and PtADC
additional information
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protein-protein interaction analysis confirming the interaction between transcription factor PtrICE1 and PtADC
additional information
residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates, Asp521A, Asp548B, and Asp550B in ADC1
additional information
residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates, Asp521A, Asp548B, and Asp550B in ADC1
additional information
residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs, formed by a highly conserved cysteine residue, needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates. Asp548B and Asp550B are probably important for substrate binding in ADCs
additional information
residue Cys196 in ADC1 and ADC2 is highly conserved and involved in disulfide bonding. The putative disulfide bond in Synechocystis ADCs, formed by a highly conserved cysteine residue, needs to be broken for catalytic activity. Synechocystis ADCs are posttranslationally regulated which might include the cleavage into two parts. In the model, the side chain of the arginine substrate can be bound by three aspartates. Asp548B and Asp550B are probably important for substrate binding in ADCs
additional information
the cofactor binding at the active site induces conformational changes in the enzyme, pyridoxal 5'-phosphate binding is important for substrate binding, the substrate might bind to ADC only after pyridoxal 5'-phosphate binding
additional information
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the cofactor binding at the active site induces conformational changes in the enzyme, pyridoxal 5'-phosphate binding is important for substrate binding, the substrate might bind to ADC only after pyridoxal 5'-phosphate binding
additional information
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the cofactor binding at the active site induces conformational changes in the enzyme, pyridoxal 5'-phosphate binding is important for substrate binding, the substrate might bind to ADC only after pyridoxal 5'-phosphate binding
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additional information
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analysis of agatine content in clinical isolates PA002. PA004, PA005, PA006, and PA016, and PA14 wild-type strain, as well as the PA14 aguA-Gm, DELTAagu2ABCA' mutant strain, which lacks a functional agmatine deiminase
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additional information
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Cys487, a conserved residue located at the active-site, is involved in the catalysis, with a pKa value of about 7.2. The homology model of the protein shows conserved alpha/beta TIM barrel and beta-sandwich domains, which are characteristic features of fold III decarboxylases. Cys487 has a marginal role in the stability. Helicobacter pylori ADC homology modeling and docking studies, overview
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