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difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
L-arginine
agmatine + CO2
L-Asp
?
-
2.6% of the activity with L-Arg
-
-
?
L-canavanine
gamma-guanidinoxypropylamine + CO2
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
L-Glu
?
-
2.1% of the activity with L-Arg
-
-
?
L-lysine
1,5-diaminopentane + CO2
L-lysine
?
assay at pH 6.5, 10 min, 50°C
-
-
?
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
L-ornithine
putrescine + CO2
L-Phe
phenylethylamine + CO2
-
1.4% of the activity with L-Arg
-
-
?
L-Pro
?
-
3.8% of the activity with L-Arg
-
-
?
L-Ser
?
-
4.4% of the activity with L-Arg
-
-
?
N-omega-nitro-L-arginine methyl ester
methyl formate + 1-(4-amino-5,5-difluoropentyl)guanidine + CO2
Ngamma-monomethyl-L-Arg
N-(3-aminopropyl)-N'-methylguanidine + CO2
-
-
-
-
?
additional information
?
-
difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 90% activity compared to L-arginine
-
-
?
difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 90% activity compared to L-arginine
-
-
?
L-Arg
?
-
enzyme is involved in synthesis of polyamines
-
-
?
L-Arg
?
-
inducible enzyme
-
-
?
L-Arg
?
-
cAMP receptor protein controls arginine decarboxylase expression by inhibiting the activity of the enzyme indirectly and putrescine represses the gene at the level of transcription
-
-
?
L-Arg
?
-
2 enzyme forms: a biosynthetic arginine decarboxylase and a degradative arginine decarboxylase. The physiological role of the degradative arginine decarboxylase possibly is the regulation of the environmental pH
-
-
?
L-Arg
?
-
the biosynthetic arginine decarboxylase is the first of two enzymes in a putrescine biosynthetic pathway
-
-
?
L-Arg
?
-
higher activity in plants cultivated on ammonium chloride than in plants grown on nitrate
-
-
?
L-Arg
?
-
regulatory role in growth and cell division
-
-
?
L-Arg
?
-
key enzyme in polyamine metabolism of plants
-
-
?
L-Arg
?
-
constitutive enzyme
-
-
?
L-Arg
?
-
agmatine production by the mitochondria could serve as a protective mechanism against cytotoxicity from excessive nitric oxide formation
-
-
?
L-Arg
?
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
?
L-Arg
?
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
?
L-Arg
?
-
important enzyme in putrescine and polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the ADC2 gene is the only gene of polyamine biosynthesis involved in wounding response mediated by methyl jasmonate. A transient increase in the level of free putrescine follows the increase in the mRNA level for ADC2
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
amino acids K136 and C524 of ADC1 are essential for activity and participate in separate active sites
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, mutants spe1-1 and spe2-1 have a lower salt tolerance than the wild type plant
-
-
?
L-arginine
agmatine + CO2
-
rate limiting and key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, induced in response to salt stress
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine and the subsequent synthesis of spermine and spermidine, plays a role in response to mechanical wounding
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, primarily responsible for the biosynthesis of putrescine in non-dividing elongation cells, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
arginine decarboxylase pathway participates in putescine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, possible involved in the development of lateral roots
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
preferred substrate
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
preferred substrate
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
biosynthesis of agmatine
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt and osmotic stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in chilling, salt, and dehydration stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in polyamine biosynthesis and plays a role in stress response, the enzyme is induced by salt stress leading to accumulation of putrescine
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
enzyme is involved in polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
enzyme catalyzes the first step of the polyamine-biosynthetic pathway
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine, Nicotiana species also utilize putrescine to provide the pyrollidine ring of the defensive alkaloid nicotine and its derivatives in roots playing no major role, overview
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the enzyme is involved in synthesis of homospermidine
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
the key enzyme involved with putrescine biosynthesis in plants, the ADC gene shows essentially chilling-specific regulation that also potentially influences putrescine accumulation, a phenomenon previously noted in cold-stressed rice seedlings
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria chlorella virus
-
-
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria chlorella virus
-
the key specificity element is the 310-helix that contains and positions substrate-binding residues such as Glu296,mechanism, the 310-helix in Chlorella virus ADC is shifted over 2 A away from the pyridoxal 5'-phosphate cofactor, the K148 loop functions as an active site lid, overview
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria Chlorella virus-1
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine and is transcriptionally regulated, ADC gene expression and enzyme activity increase during embryogenesis
-
-
?
L-arginine
agmatine + CO2
the localization of the enzyme transcript differs in roots inoculated and non-inoculated with mycorrhizal fungus, e.g. Suillus variegatus, overview
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, involved in chilling and salt stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is the enzyme essential for agmatine synthesis, chronic treatment with glucocorticoids alters rat hippocampal and prefrontal cortical morphology in parallel with endogenous agmatine and arginine decarboxylase levels, neuroprotective effect of agmatine on dexamethasone-induced neuronal damage in brain areas, overview
-
-
?
L-arginine
agmatine + CO2
-
rate-limiting enzyme in polyamine biosynthesis
agmatine is a neurotransmitter or neuromodulator in the brain, agmatine has neuroprotective effects in vitro and in vivo
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
assay at pH 6.5, 10 min, 50°C
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt stress response, high temperature and glucose treatment causes an increase in the specific activity, the specific activity is reduced by iron deficiency
-
-
?
L-arginine
agmatine + CO2
the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway in bacteria and plants, posttranslational regulation involving a putative extra domain, modelling, overview
-
-
?
L-arginine
agmatine + CO2
effects of various types of short-term stresses on the transcript amount and specific activity of the enzyme, overview
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
no activity with ornithine and lysine
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
level and/or activity is posttranslationally regulated
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
ADC is the primary polyamine biosynthetic enzyme in the pathway
-
-
?
L-arginine
agmatine + CO2
the enzyme exists in two different conformational states, one that binds ligand and one that does not
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-Canavanine
?
-
-
-
-
?
L-Canavanine
?
-
40% of the activity with L-Arg
-
-
?
L-Canavanine
?
-
40% of the activity with L-Arg
-
-
?
L-canavanine
gamma-guanidinoxypropylamine + CO2
-
-
-
-
?
L-canavanine
gamma-guanidinoxypropylamine + CO2
-
-
-
-
?
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
decarboxylation at 40% of the activity compared with L-arginine
-
-
?
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
decarboxylation at 40% of the activity compared with L-arginine
-
-
?
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
-
-
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
activity is 1.9% of that with L-arginine
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
activity is 1.9% of that with L-arginine
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
very low activity
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
very low activity
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
activity is 1.4% of that with L-arginine
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
activity is 1.4% of that with L-arginine
-
-
?
L-ornithine
putrescine + CO2
about 90% activity compared to L-arginine
-
-
?
L-ornithine
putrescine + CO2
about 90% activity compared to L-arginine
-
-
?
L-ornithine
putrescine + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
meso-diaminopimelate
?
-
activity is less than 2% of that with L-arginine
-
-
?
meso-diaminopimelate
?
-
activity is less than 2% of that with L-arginine
-
-
?
N-omega-nitro-L-arginine methyl ester
methyl formate + 1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 80% activity compared to L-arginine
-
-
?
N-omega-nitro-L-arginine methyl ester
methyl formate + 1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 80% activity compared to L-arginine
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
?
additional information
?
-
-
the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
?
additional information
?
-
-
the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine
-
-
?
additional information
?
-
-
enzyme activity detection using radioactive-labeled substrate
-
-
?
additional information
?
-
-
the enzyme is involved in the polyamine metabolism, effects of long term cadmium or copper stress, overview
-
-
?
additional information
?
-
-
human ornithine decarboxylase paralogue (ODCp) is not an arginine decarboxylase
-
-
?
additional information
?
-
-
arginine decarboxylase is involved in stress protection against environmental cues and pathogens
-
-
?
additional information
?
-
-
recent evidence suggests a potential involvement of agmatine in learning and memory processing
-
-
?
additional information
?
-
-
enzyme activity assay using cucurbit[7]uril (CB7) and fluorescent dye acridine orange, overview
-
-
?
additional information
?
-
purified recombinant isozyme Adc2 shows high arginine decarboxylase activity compared to purified isozyme Adc1
-
-
?
additional information
?
-
purified recombinant isozyme Adc2 shows high arginine decarboxylase activity compared to purified isozyme Adc1
-
-
?
additional information
?
-
purified recombinant isozyme Adc2 shows high arginine decarboxylase activity compared to purified isozyme Adc1. The absolute activity of Adc1, in absence of salt, is extremely low
-
-
?
additional information
?
-
purified recombinant isozyme Adc2 shows high arginine decarboxylase activity compared to purified isozyme Adc1. The absolute activity of Adc1, in absence of salt, is extremely low
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-arginine
agmatine + CO2
L-ornithine
putrescine + CO2
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
additional information
?
-
L-Arg
?
-
enzyme is involved in synthesis of polyamines
-
-
?
L-Arg
?
-
inducible enzyme
-
-
?
L-Arg
?
-
cAMP receptor protein controls arginine decarboxylase expression by inhibiting the activity of the enzyme indirectly and putrescine represses the gene at the level of transcription
-
-
?
L-Arg
?
-
2 enzyme forms: a biosynthetic arginine decarboxylase and a degradative arginine decarboxylase. The physiological role of the degradative arginine decarboxylase possibly is the regulation of the environmental pH
-
-
?
L-Arg
?
-
the biosynthetic arginine decarboxylase is the first of two enzymes in a putrescine biosynthetic pathway
-
-
?
L-Arg
?
-
higher activity in plants cultivated on ammonium chloride than in plants grown on nitrate
-
-
?
L-Arg
?
-
regulatory role in growth and cell division
-
-
?
L-Arg
?
-
key enzyme in polyamine metabolism of plants
-
-
?
L-Arg
?
-
constitutive enzyme
-
-
?
L-Arg
?
-
agmatine production by the mitochondria could serve as a protective mechanism against cytotoxicity from excessive nitric oxide formation
-
-
?
L-Arg
?
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
?
L-Arg
?
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
?
L-Arg
?
-
important enzyme in putrescine and polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
the ADC2 gene is the only gene of polyamine biosynthesis involved in wounding response mediated by methyl jasmonate. A transient increase in the level of free putrescine follows the increase in the mRNA level for ADC2
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, mutants spe1-1 and spe2-1 have a lower salt tolerance than the wild type plant
-
-
?
L-arginine
agmatine + CO2
-
rate limiting and key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, induced in response to salt stress
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine and the subsequent synthesis of spermine and spermidine, plays a role in response to mechanical wounding
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, primarily responsible for the biosynthesis of putrescine in non-dividing elongation cells, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
L-arginine
agmatine + CO2
-
arginine decarboxylase pathway participates in putescine biosynthesis
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, possible involved in the development of lateral roots
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
biosynthesis of agmatine
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt and osmotic stress response
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in chilling, salt, and dehydration stress response
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in polyamine biosynthesis and plays a role in stress response, the enzyme is induced by salt stress leading to accumulation of putrescine
-
-
?
L-arginine
agmatine + CO2
-
enzyme is involved in polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
enzyme catalyzes the first step of the polyamine-biosynthetic pathway
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
key enzyme of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine, Nicotiana species also utilize putrescine to provide the pyrollidine ring of the defensive alkaloid nicotine and its derivatives in roots playing no major role, overview
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-arginine
agmatine + CO2
the enzyme is involved in synthesis of homospermidine
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the key enzyme involved with putrescine biosynthesis in plants, the ADC gene shows essentially chilling-specific regulation that also potentially influences putrescine accumulation, a phenomenon previously noted in cold-stressed rice seedlings
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria chlorella virus
-
-
-
-
?
L-arginine
agmatine + CO2
Paramecium bursaria Chlorella virus-1
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine and is transcriptionally regulated, ADC gene expression and enzyme activity increase during embryogenesis
-
-
?
L-arginine
agmatine + CO2
the localization of the enzyme transcript differs in roots inoculated and non-inoculated with mycorrhizal fungus, e.g. Suillus variegatus, overview
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, involved in chilling and salt stress response
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is the enzyme essential for agmatine synthesis, chronic treatment with glucocorticoids alters rat hippocampal and prefrontal cortical morphology in parallel with endogenous agmatine and arginine decarboxylase levels, neuroprotective effect of agmatine on dexamethasone-induced neuronal damage in brain areas, overview
-
-
?
L-arginine
agmatine + CO2
-
rate-limiting enzyme in polyamine biosynthesis
agmatine is a neurotransmitter or neuromodulator in the brain, agmatine has neuroprotective effects in vitro and in vivo
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-arginine
agmatine + CO2
-
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt stress response, high temperature and glucose treatment causes an increase in the specific activity, the specific activity is reduced by iron deficiency
-
-
?
L-arginine
agmatine + CO2
the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway in bacteria and plants, posttranslational regulation involving a putative extra domain, modelling, overview
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
-
-
-
?
L-arginine
agmatine + CO2
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
-
level and/or activity is posttranslationally regulated
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-arginine
agmatine + CO2
ADC is the primary polyamine biosynthetic enzyme in the pathway
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the polyamine metabolism, effects of long term cadmium or copper stress, overview
-
-
?
additional information
?
-
-
arginine decarboxylase is involved in stress protection against environmental cues and pathogens
-
-
?
additional information
?
-
-
recent evidence suggests a potential involvement of agmatine in learning and memory processing
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E)-alpha-Monofluoromethyl-3-4-dehydroarginine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
2-Nor-2-butylpyridoxal phosphate
-
-
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
alpha-difluoromethylarginine
alpha-difluoromethylornithine
beta-(2-Methyl-3-hydroxy-4-formylpyridine-5)-propionic acid
-
-
difluoromethyl-L-arginine
1 mM, 80 °C, 15 min, 64% loss of activity, irreversible inhibition
difluoromethyl-L-ornithine
1 mM, reduces activity by 20%
DL-alpha-difluoromethylarginine
ethylmercury
-
54% inhibition at 0.005 mM
Fe2+
80% inhibition at 4 mM
Fluorescein isothiocyanate
-
0.09 mM, 40% inhibition
K+
-
100 mM, 50% decrease of activity
L-2-Amino-3-guanidinopropanoate
-
-
L-2-Amino-4-guanidinobutyrate
-
-
L-2-amino-5-guanidinopentanoate
-
-
L-2-amino-6-guanidinohexanoate
-
-
L-2-Chloro-5-guanidinopentanoate
-
-
L-2-Hydroxy-5-guanidinopentanoate
-
-
L-histidine
1 mM, 20-30% inhibition
methylglyoxal bisguanylhydrazone
-
-
methylglyoxal-bis(guanylhydrazone)
-
-
methylmercury
-
33% inhibition at 0.005 mM
Monofluoromethylagmatine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
N-Carbamoylputrescine
-
-
Na+
-
10 mM, 20% decrease of activity
Nalpha-acetyl-L-arginine
1 mM, 20-30% inhibition
Ngamma-methyl-D-arginine
-
-
O-(4-nitrobenzyl)hydroxylamine
1 mM, 50% inhibition, pyruvoyl group modification
O-methyl hydroxylamine
-
69% inhibition at 2 mM
O-Methylhydroxylamine
1 mM, 50% inhibition, pyruvoyl group modification
O-nitrobenzylhydroxylamine
-
75% inhibition at 2 mM
p-hydroxymercuribenzoate
-
-
phenanthrene
-
concentrations above 0.5 microM cause either no change or a significant reduction in ADC activity irrespective of treatment with or without DL-alpha-difluoromethylarginine
phenylmercury
-
72% inhibition at 0.005 mM
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
-
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
NSD 1055
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
-
agmatine
-
-
agmatine
-
1.4 mM, 50% inhibition
agmatine
-
10 mM, 57% inhibition
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
alpha-difluoromethylarginine
-
DFMA, a suicide inhibitor, at 5 mM for 72 h, it inhibits ADC activity. DFMA, inhibits ADC activity in both supernatant and pellet fractions (43% and 26% respectively)
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
DFMA, competitive inhibition
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
Paramecium bursaria Chlorella virus-1
-
1 mM causes almost complete inhibition after 30 min incubation, irreversible
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylarginine
-
-
alpha-difluoromethylornithine
-
alpha-difluoromethylornithine
Paramecium bursaria Chlorella virus-1
-
10 mM causes 74% inhibition after 30 min incubation, irreversible
Ca2+
-
-
Ca2+
-
100 mM, 90% decrease of activity
canavanine
-
L-canavanine
canavanine
-
L-canavanine
canavanine
-
L-canavanine
citrulline
-
L-citrulline
Co2+
-
0.1 mM, 70% loss of activity
Cu2+
-
0.1 mM, 70% loss of activity
Cu2+
87% inhibition at 4 mM, complete inhibition at 8 mM
Cu2+
-
1 mM, 25% inhibition. 5 mM, 94% inhibition
D-Arg
-
1 mM, 60% inhibition
D-arginine
decreases enzyme activity and inhibits growth of apple callus
D-arginine
-
causes further damage to callus under salt stress, reversible by addition of putrescine
DL-alpha-difluoromethylarginine
-
In the absence of phenanthrene, treatment with 1.5 mM DL-alpha-difluoromethylarginine with reduces ADC activity by 61%
DL-alpha-difluoromethylarginine
-
DL-alpha-difluoromethylarginine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
DL-alpha-difluoromethylarginine
-
-
guanidine
-
-
guanidine
-
5-10 mM, 50% inhibition
Hg2+
-
-
Hg2+
-
85% inhibition at 0.005 mM
homoarginine
-
-
hydroxylamine
-
-
L-argininamide
-
33% inhibition at 2 mM
L-argininamide
-
5 mM, complete inhibition
L-argininamide
1 mM, almost completely abolished arginine decarboxylase activity
L-arginine methyl ester
-
5 mM, complete inhibition
L-arginine methyl ester
1 mM, 70% loss of activity
L-arginine methyl ester
-
-
L-canavanine
1 mM, 46% inhibition
L-homoarginine
1 mM, 20-30% inhibition
L-Lys
-
-
methylguanidine
-
-
methylguanidine
-
5-10 mM, 50% inhibition
Mg2+
-
-
Mg2+
-
100 mM, 90% decrease of activity
Mn2+
-
-
Mn2+
-
100 mM, 90% decrease of activity
Mn2+
-
0.01-0.1 mM, enhances activity. Inhibition at higher concentrations
NEM
-
-
NEM
-
3 mM, 65% inhibition
Orn
-
-
PCMB
-
-
PCMB
-
dithiothreitol prevents inhibition
polyamines
-
-
-
putrescine
-
-
pyridoxal
-
-
Pyridoxine-HCl
-
-
spermidine
-
-
spermine
-
-
spermine
-
1 mM, 30% loss of activity
spermine
-
1 mM, 5% inhibition of the enzyme from fully developed fruit, 65% inhibition of the enzyme from the seed coat of 4-week-old fruitlets
Urea
-
-
Urea
-
4 M, 80% inhibition
urethane
-
-
Zn2+
97% inhibition at 4 mM, complete inhibition at 8 mM
additional information
-
alpha-difluoromethylornithine, DFMO, a suicide inhibitor, does not inhibit ADC activity
-
additional information
-
activity not affected by Mg2+ or Ca2+ at 0.1 mM
-
additional information
-
the mRNA level of adiA is 4fold lower in the mutants deficient in both alpha-subunit and beta-subunit of major histon-like protein HU
-
additional information
no inhibition by 1 mM alpha-difluoromethylornithine
-
additional information
-
no inhibition by 1 mM alpha-difluoromethylornithine
-
additional information
-
no inhibition by DL-alpha-difluoromethylornithine
-
additional information
-
mercury compounds inhibits the enzyme activity but induce the enzyme expression in PC12 cells, molecular mechanism of mercury compounds' neurotoxicity and enzyme inhibition mechanism, molecular dynamics simulation, product-competitive displacement method, method optimization, overview
-
additional information
-
inhibition of ADC results in much greater levels of oxidative damage than seen in plants treated with 0.5 microM phenanthrene; treatment with DL-alpha-difluoromethylarginine suppresses the large increase in ADC activity observed when the plants are exposed to 0.1 or 0.5 microM phenanthrene in the absence of DL-alpha-difluoromethylarginine; treatment with methylglyoxal-bis(guanylhydrazone) does not significantly influence ADC activity
-
additional information
1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine
-
additional information
-
1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine
-
additional information
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. darkness and cold reduce enzyme expression, overview
-
additional information
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. darkness and cold reduce enzyme expression, overview
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2-Norpyridoxal phosphate
-
reactivation of the apoenzyme
6-Methylpyridoxal phosphate
-
reactivation of the apoenzyme
abscisic acid
mRNA level of ADC is induced in the shoots subjected to the concentration of 0.2 mM abscisic acid. After treatment of peach shoots with 0.1 mM abscisic acid to study time-course change of ADC expression over 2 days, are markable increase of the expression level is observed 1 h after the treatment, followed by quick decline until the end of treatment.
alpha-difluoromethylornithine
-
-
arsenic
-
ADC is analyzed in plants treated with arsenic and compared with untreated plants and with positive (TMV-inoculated or DL-beta-aminobutyric acid-treated) controls. ADC transcripts are significantly increased, at both the local and systemic levels, relative to untreated controls.
DL-alpha-difluoromethylarginine
-
plants exposed to 0.1 or 0.5 microM phenanthrene plus DL-alpha-difluoromethylarginine have significantly greater ADC activities when compared with plants treated with DL-alpha-difluoromethylarginine in the absence of phenanthrene
DL-alpha-difluoromethylornithine
gibberellic acid
-
stimulates
indoleacetic acid
-
stimulates
mercaptoethanol
-
stimulates
MG-132
ADC proteins are degraded by ubiquitin-dependent mechanisms carried out by 26S proteasome, the major degradation pathway for soluble proteins. Experiments carry out with ADC-transgenic cultures of Trypanosoma cruzi incubated with the peptide aldehyde proteasome inhibitor MG-132 show a marked increase of ADC activity probably due to the reduction of the enzyme turnover rate as shown after blocking protein synthesis with cycloheximide.
phenanthrene
-
concentrations of phenanthrene up to 0.5 microM cause significant increases in the activity of ADC, with a resultant increase in tissue polyamine levels
putrescine
treatment of peach shoots from Mochizuki with exogenous putrescine (indirect product of ADC) remarkably induces accumulation of ADC mRNA, incubation of shoots in 1 and 5 mM exogenous putrescine for 2 days leads to obvious and significant increase in endogenous putrescine
spermidine
-
ADC is analyzed in plants treated with spermidine and compared with untreated plants and with positive (TMV-inoculated or DL-beta-aminobutyric acid-treated) controls. ADC transcripts are significantly increased, at both the local and systemic levels, relative to untreated controls.
dithiothreitol
-
stimulates
dithiothreitol
-
absolute requirement
DL-alpha-difluoromethylornithine
-
ADC activity increases by 21% in plants exposed to DL-alpha-difluoromethylornithine in the absence of phenanthrene
DL-alpha-difluoromethylornithine
-
activates
pyridoxal 5'-phosphate
-
recombinant enzyme, extracts from Trypanosoma cruzi have an about six times higher activity in the presence of pyridoxal 5-phosphate
pyridoxal 5'-phosphate
Paramecium bursaria Chlorella virus-1
-
included in enzyme assay
additional information
arginine decarboxylase activity is modulated by external pH and active at acidic pH
-
additional information
-
arginine decarboxylase activity is modulated by external pH and active at acidic pH
-
additional information
-
the enzyme is induced by 200 mM NaCl salt stress leading to accumulation of putrescine, during recovery the enzyme expression decreases
-
additional information
-
no photoinduction of arginine decarboxylase activity
-
additional information
the gene encoding the enzyme is up-regulated by chilling stress in rice seedling leaves, effects of environmental stress, overview, the enzyme is induced by cold stress at 5°C and 12°C, by drought and by methyljasmonic acid and abscisic acid treatment
-
additional information
-
the gene encoding the enzyme is up-regulated by chilling stress in rice seedling leaves, effects of environmental stress, overview, the enzyme is induced by cold stress at 5°C and 12°C, by drought and by methyljasmonic acid and abscisic acid treatment
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additional information
ADC gene expression and enzyme activity increase during embryogenesis
-
additional information
-
ADC gene expression and enzyme activity increase during embryogenesis
-
additional information
inoculation with the mycorrhizal fungus Suillus variegatus leads to 3.0fold induction of the enzyme in roots and 1.4fold induction in shoots
-
additional information
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inoculation with the mycorrhizal fungus Suillus variegatus leads to 3.0fold induction of the enzyme in roots and 1.4fold induction in shoots
-
additional information
transcripts of ADC in peach leaves are quickly induced, either transiently or continuously, in response to dehydration, high salinity (200 mM NaCl), low temperature (4°C) and heavy metal (0.15 mM CdCl2), but represses by high temperature (37°C) during a 2-day treatment, which changes in an opposite direction when the stresses are otherwise removed with the exception of CdCl2 treatment.
-
additional information
-
transcripts of ADC in peach leaves are quickly induced, either transiently or continuously, in response to dehydration, high salinity (200 mM NaCl), low temperature (4°C) and heavy metal (0.15 mM CdCl2), but represses by high temperature (37°C) during a 2-day treatment, which changes in an opposite direction when the stresses are otherwise removed with the exception of CdCl2 treatment.
-
additional information
-
chronic treatment, over 21 days, with glucocorticoids, via dexamethasone, alters endogenous agmatine and arginine decarboxylase levels in the brain, reversible by exogenous agmatine, overview
-
additional information
-
ADC protein levels and endogenous agmatine levels are significantly increased in the prefrontal cortex, hippocampus, striatum and hypothalamus by immobilization stress. As one element of self-protection mechanisms in the brain, agmatine synthesis is triggered by repeated immobilization through activation of ADC expression, which in turn increases endogenous agmatine levels as an initial protective response to stress.
-
additional information
-
DL-alpha-difluoromethylornithine does not influence the general trend of increased ADC activitiy observed in plants exposed to 0.1 or 0.5 microM phenanthrene
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
additional information
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. photoheterotrophy, high temperature and high light conditions activate enzyme expression, overview
-
additional information
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. photoheterotrophy, high temperature and high light conditions activate enzyme expression, overview
-
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about 5% of the activity in aorta
brenda
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highest activity of all tissues tested
brenda
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bronchial cell line
brenda
-
-
brenda
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analysis of in vivo activity of arginine decarboxylase in three different cell lines of Daucus carota, namely N1 (embryogenic), F1 (non-embryogenic), and O3 (habituated and non-embryogenic), during growth and somatic embryogenesis. The enzyme activity in the presence of various levels of auxin (2,4-dichlorophenoxy acetic acid) is highest during periods of active cell division. During somatic embryo development, the enzyme activity is highest during globular stage formation. Stage-specific activity of ADC, overview
brenda
-
-
brenda
-
-
brenda
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presence of both arginine decarboxylase and arginase in principal neurons and putative interneurons
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-
-
brenda
-
-
brenda
-
brenda
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significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
brenda
-
-
brenda
abaxial epidermis
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-
-
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-
-
brenda
SpeA accumulates at higher levels in vegetative cells than in heterocysts
brenda
-
-
brenda
-
-
brenda
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about 40% of the activity in aorta
brenda
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about 75% of the activity in aorta
brenda
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-
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-
brenda
-
brenda
-
-
brenda
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brenda
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-
brenda
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significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
brenda
-
-
brenda
-
-
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somatic
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-
-
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-
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of both 4-week-old avocado fruitlet and fully developed fruit
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germinating
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-
-
brenda
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-
brenda
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about 60% of the activity in aorta
brenda
-
-
brenda
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about 15% of the activity in aorta
brenda
-
-
brenda
-
-
brenda
SpeA accumulates at higher levels in vegetative cells than in heterocysts
brenda
-
-
brenda
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-
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about 40% of the activity in aorta
brenda
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arginine decarboxylase and arginase are both constitutively and widely expressed in rat brain neurons
brenda
transcript levels are highest in buds and rolled leaves and lower in other organs
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-
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-
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-
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derived from young fruits
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-
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activity is not affected by hormone deprivation
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vascular tissue
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low activity
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-
-
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-
-
brenda
protein and mRNA transcript are present at different phases of mitosis in Scots pine zygotic embryogenesis, ADC gene expression and enzyme activity increase during embryogenesis, overview, localization of ADC gene expression in the cells of primary shoot and root meristem of late embryo and in the mitotic cells of shoot meristem in the late embryo at the cotyledonary stage, in situ immunohistochemic detection, overview
brenda
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enzyme activity is only present in the early stage of the parasite exponential growth, between 4 and 23 h of cultivation in presence of Arg, with a maximum at 14 h and disappears completely at the mid logarithmic phase. It is never detected during the stationary phase
brenda
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enzyme activity is only present in the early stage of the parasite exponential growth, between 4 and 23 h of cultivation in presence of Arg, with a maximum at 14 h and disappears completely at the mid logarithmic phase. It is never detected during the stationary phase
-
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highest activity
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-
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-
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young fruit, almost no activity in ripe fruit
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-
-
brenda
the fruit collected at 107 days after full bloom shows stronger expression than that at 23 days after full bloom
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-
-
brenda
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presence of both arginine decarboxylase and arginase in principal neurons and putative interneurons
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vascular tissue
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-
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increasing activity during developmental stages, high activity in final stage
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increasing activity during developmental stages, high activity in final stage
-
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weak
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cortex
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about 85% of the activity in aorta
brenda
-
-
brenda
-
brenda
-
brenda
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vascular tissue
brenda
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-
-
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-
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increased activity after mechanical wounding, highest activity 1-2 h after wounding
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-
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-
brenda
transcript levels are highest in buds and rolled leaves and lower in other organs
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-
brenda
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no significant effect of sorbitol or NaCl treatment
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young leaves have higher activity than mature leaves
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-
-
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-
brenda
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diurnal changes in enzyme activity and polyamine contents, overview
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-
brenda
Adc1 is expressed in leaf, root and stem
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young leaves have higher ADC expression levels
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-
-
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-
brenda
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enzyme activity and agmatine levels in human sputum peak during cystic fibrosis illness, decrease with treatment, and is positively correlated with inflammatory cytokines. Bacterial pathways of agmatine metabolism are able to impact the agmatine levels within the lung during infection
brenda
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enzyme activity and agmatine levels in human sputum peak during cystic fibrosis illness, decrease with treatment, and is positively correlated with inflammatory cytokines
brenda
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-
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-
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-
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-
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-
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-
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significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
brenda
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brenda
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tips, junction between hypocotyls and roots, vascular tissue
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-
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tips
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significantly increased activity in roots grown for 24 h in the presence of 260 mM NaCl or 360 mM sorbitol
brenda
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-
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-
brenda
Adc1 is expressed in leaf, root and stem
brenda
localization in specific root parenchyma cells adjacent to tracheids and in mitotic cells of the root apical meristem, difference in ADC transcript localization between roots inoculated and non-inoculated with mycorrhizal fungus
brenda
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great increase of ADC2 mRNA level at low temperature cultivation and after salt exposure, ADC1 and ADC2 in mature plants
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developing seed
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shotts of seedlings
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high level in sieve tubes of main root in 6-8 days old seedlings
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-
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-
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ADC2 mRNA hardly detectable when cultivated at 22°C
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-
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great increase of ADC2 mRNA level at low temperature cultivation and after salt exposure, ADC1 but not ADC2 accumulated in shoots of mature plants
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brenda
Adc2 expression is restricted to stem tissue, Adc1 is expressed in leaf, root and stem
brenda
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brenda
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-
brenda
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-
brenda
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-
brenda
additional information
in non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression. ADC2 expression is strongly associated with seed germination, root and leaf development
brenda
additional information
in non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression. ADC2 expression is strongly associated with seed germination, root and leaf development
brenda
additional information
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in non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression. ADC2 expression is strongly associated with seed germination, root and leaf development
brenda
additional information
the ADC1 promoter activity is low during vegetative development. In non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression
brenda
additional information
the ADC1 promoter activity is low during vegetative development. In non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression
brenda
additional information
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the ADC1 promoter activity is low during vegetative development. In non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression
brenda
additional information
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in non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression. ADC2 expression is strongly associated with seed germination, root and leaf development
-
brenda
additional information
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the ADC1 promoter activity is low during vegetative development. In non-infected wild-type plants, isozyme ADC2 expression is much higher than ADC1 expression
-
brenda
additional information
not detected in roots
brenda
additional information
-
not detected in roots
brenda
additional information
method optimization, overview. Optimum conditions for agmatine production of the recombinant enzyme in vivo are 3.5 g/l intact cells, 4 mM Mg2+, 30 mM pyridoxal 5'-phosphate, pH 7, 37°C. SOC medium is optimal for ADC production compared to others
brenda
additional information
no activity detectable in lateral roots emergence region
brenda
additional information
-
no activity detectable in lateral roots emergence region
brenda
additional information
Pinus sylvestris forms a symbiosis with ectomycorrhizal fungi, e.g. Suillus variegatus, that entirely cover short roots with a hyphal mantle, inducing effects in different tissues, overview
brenda
additional information
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Pinus sylvestris forms a symbiosis with ectomycorrhizal fungi, e.g. Suillus variegatus, that entirely cover short roots with a hyphal mantle, inducing effects in different tissues, overview
brenda
additional information
expression levels of PpADC in different tissues of peach are spatially and developmentally regulated
brenda
additional information
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expression levels of PpADC in different tissues of peach are spatially and developmentally regulated
brenda
additional information
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profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions
brenda
additional information
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions
brenda
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evolution
arginine decarboxylases belong to a family of fold III PLP (pyridoxal 5'-phosphate)-dependent decarboxylases
evolution
-
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
-
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
-
malfunction
-
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
-
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
-
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
-
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
-
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
-
agmatine is synthesized by the arginine decarboxylase pathway, but is essentially undetectable if the aguBA operon is left intact
metabolism
-
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
-
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
-
FcWRKY70 functions in drought tolerance by, at least partly, promoting production of putrescine via regulating ADC expression
metabolism
-
FcWRKY70 functions in drought tolerance by, at least partly, promoting production of putrescine via regulating ADC expression
metabolism
-
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
-
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
-
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
-
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
-
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
arginine decarboxylase (ADC) is a key enzyme in the central agmatinergic system
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
the Bacillus subtilis biosynthetic aspartate aminotransferase fold arginine decarboxylase is essential for biofilm formation
-
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
-
Helicobacter pylori uses arginine in an acid response mechanism required for its growth in acid conditions
-
physiological function
-
gene speA encodes a putative arginine decarboxylase, an enzyme necessary for spermidine biosynthesis in cells
-
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
-
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
-
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
-
additional information
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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115000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
11759
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
12600
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
16000
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
163100
-
apo-ADC, light-scattering analysis
178000
-
holo-ADC, light-scattering analysis
17940
inactive proenzyme, mass spectrometry
195000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
23000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
25000
-
His-tagged-AaxB protein from strain D/UW-3, SDS-PAGE
38000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
39400
-
x * 39400, SDS-PAGE
407000
purified recombinant His-tagged enzyme, gel filtration
42000
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
54000
-
x * 54000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
58900
-
4 * 58900, SDS-PAGE
6123
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
68000
ADC2, predicted from amino acid sequence
72821
x * 72821, calculated
77700
predicted from amino acid sequence
80000
His10-tagged enzyme, gel filtration
88000
-
recombinant enzyme, gel filtration
9000
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
additional information
-
-
24000
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
24000
-
x * 24000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
240000
-
gel filtration
58000
-
SDS-PAGE
63000
SDS-PAGE
63000
-
3 * 63000, SDS-PAGE
66000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
66000
inactive precursor protein, active recombinant ADC is formed in vivo by a complex of two His-tagged polypeptide chains of 42 and 24 kDa by a subsequent incubation during different times with extracts of Arabidopsis seedlings which contain a proteolytic activity, processing of oat ADC does not require a specific protease
74000
ADC1, predicted from amino acid sequence
74000
-
3 * 74000, SDS-PAGE
74000
-
4 * 74000, biosynthetic arginine decarboxylase
74000
-
4 * 74000, crystal structure analysis
74000
x * 74000, about, sequence calculation, ADC1
78000
-
4 * 78000, subunit mass calculated from the deduced amino acid sequence, SDS-PAGE
78000
x * 78000, calculated from the deduced amino acid sequence
800000
gel filtration
800000
about, recombinant enzyme, crystal structure
82000
-
2 * or 10 * 82000, degradative arginine decarboxylase
82000
-
10 * or 1 * 82000, degradative arginine decarboxylase
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heterodimer
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
?
x * 72821, calculated
?
x * 70000, recombinant enzyme, SDS-PAGE
?
-
x * 24000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
?
-
x * 54000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
?
x * 78000, calculated from the deduced amino acid sequence
?
x * 74000, about, sequence calculation, ADC1
?
x * 70600, about, recombinant His6-tagged enzyme, sequence calculation
?
-
x * 70600, about, recombinant His6-tagged enzyme, sequence calculation
-
?
x * 74500, about, sequence calcualtion of His-tagged isozyme Adc1
?
x * 78200, about, sequence calcualtion of His-tagged isozyme Adc2
decamer
-
decamer dissociates in stages rather than all at once to a dimer
decamer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
decamer
-
10 * 82000-96000, SDS-PAGE
decamer
-
10 * or 1 * 82000, degradative arginine decarboxylase
decamer
pentamer of homodimers, X-ray crystallography
decamer
-
10 * 82000-96000, SDS-PAGE
-
decamer
(alphabeta)5, 10 * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE
decamer
-
(alphabeta)5, 10 * 80000, about, recombinant His6-tagged enzyme, SDS-PAGE
-
dimer
the enzyme is a head-to-tail homodimer with two active sites acting in trans across the interface of the dimer
dimer
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
dimer
-
decamer dissociates in stages rather than all at once to a dimer
dimer
-
2 * or 10 * 82000, degradative arginine decarboxylase
dimer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
dimer
stabilized by two inter-subunit disulfide bonds, structural modeling
dimer
the enzyme dimer is stablized by the disulfide bridge involving Cys196
dimer
-
in solution at pH 8.0, light-scattering analysis
hexamer
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
hexamer
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
-
hexamer
6 * 68000, about, recombinant His-tagged enzyme, SDS-PAGE
hexamer
-
6 * 68000, about, recombinant His-tagged enzyme, SDS-PAGE
-
hexamer
-
6 * 36000-36500, SDS-PAGE
hexamer
-
3 * alpha 11000-13000 + 3 * beta 5000-7000, SDS-PAGE
hexamer
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
octamer
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
octamer
-
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
-
tetramer
x-ray crystallography
tetramer
-
x-ray crystallography
-
tetramer
-
4 * 78000, subunit mass calculated from the deduced amino acid sequence, SDS-PAGE
tetramer
-
4 * 74000, biosynthetic arginine decarboxylase
tetramer
x-ray crystallography
tetramer
-
4 * 58900, SDS-PAGE
tetramer
-
4 * 58900, SDS-PAGE
-
tetramer
x-ray crystallography
tetramer
-
4 * 74000, crystal structure analysis
trimer
-
3 * 74000, SDS-PAGE
trimer
Mutant E109Q, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. All 6 protomers are fully processed and contain the product agmatine at the active site. The presence of the product agmatine confirms that the mutant is active because the substrate arginine is added to the protein during crystallization.
trimer
Mutant N47A, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. The mutant protein does not show complete processing in all protomers. The first protomer of N47A is processed showing clear cleavage of the protomer to form the beta-chain (residues 1-52) and the alpha-chain (residues 53-165). A second protomer is unprocessed, showing clear density connecting residues Ser52 and Ser53. The final protomer in the first trimer can not easily be classified as either processed or unprocessed and is likely to be a mixture of the two states. The density between Ser52 and Ser53 is weak, density is also present corresponding to the pyruvoyl group and the product agmatine.
trimer
-
3 * 63000, SDS-PAGE
additional information
-
the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds
additional information
-
structural modelling
additional information
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
additional information
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
-
additional information
-
structural modelling
additional information
-
structural modelling
additional information
-
effects of substrate, coenzyme, and positive and negative effectors on the enzyme structure
additional information
Paramecium bursaria chlorella virus
-
the mobile loop, the K148-loop, is observed in a closed, substrate-bound conformation, this loop adopts different conformations throughout the catalytic cycle, overview
additional information
-
structural modelling
additional information
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
additional information
-
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
additional information
-
a pentamer of dimers, structure of dimer and decamer, overview. unlike the interactions between 5fold related protomers, interactions that stabilize the dimeric structure are not pH-dependent
-
additional information
-
Synechocystis ADCs have a putative extra domain, which might be involved in the posttranslational regulation of ADC activity, structural modeling, overview
additional information
Synechocystis ADCs have a putative extra domain, which might be involved in the posttranslational regulation of ADC activity, structural modeling, overview
additional information
-
structural modelling
additional information
-
structural modelling
additional information
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview
additional information
-
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview
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C524A
91.8% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
K136A
97.7% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
X128W
-
the purified X128W variant protein catalyzes the decarboxylation of L-arginine with a pH optimum near 3.4 with increased Km and decreased kcat values compared to the wild type enzyme
E109Q
E109Q mutation reduces the activity by 7.7fold compared to the wild type enzyme, reduced decarboxylation activity results in part from incomplete pyruvoyl-group formation
N47A
The activity of N47A is reduced by 500fold compared with the wild type protein
S53A
nonprocessing mutant enzyme
T142A
Paramecium bursaria chlorella virus
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site-directed mutagenesis, structural comparison to the wild-type enzyme, overview
D296E
Paramecium bursaria Chlorella virus-1
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responsible for changes in substrate specificity
E296D
Paramecium bursaria Chlorella virus-1
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increased Km and decreased turnover with L-Arg, minor effect on Km with L-ornithine, decreased turnover with L-ornithine
T52S
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site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
T52S
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site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
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C487A
site-directed mutagenesis, the mutant shows less than 10% of wild-type activity, but only slightly reduced temperature stability compared to wild-type
C487A
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site-directed mutagenesis, the mutant shows less than 10% of wild-type activity, but only slightly reduced temperature stability compared to wild-type
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additional information
construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
additional information
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construction of an ADC2 null mutant by T-DNA insertion. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
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additional information
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construction of an ADC1 null mutant by T-DNA insertion. As opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. ADC1 expression in adc2-3 mutants is similar to wild-type plants, and ADC2 expression in adc1-3 mutants is also similar to wild-type plants
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additional information
construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
additional information
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construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
additional information
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agmatine-producing mouse cortical astrocytes were developed through transduction of the transformed heterologous human ADC gene
additional information
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downregulation of nicotine biosynthesis via antisense approach, diminishing of ADC activity in transformed roots, alkaloid profile of cultured hairy roots and regenerated transgenic plants, growth of transformed roots is unaltered, overview
additional information
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in vivo knockdown of translation of ODC1 (EC 4.1.1.17) and ADC mRNAs individually and in combination. Double knockdown of ODC1 and ADC (MAO-ODC1:ADC) results in two phenotypes (a or b) of conceptuses: 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. Phenotypes, overview
additional information
marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
additional information
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marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
additional information
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marker-less gene speA deletion by by double-crossover recombination, construction of a double knockout DELTAtdk/DELTAspeA mutant strain MS531 by knockout of gene speA in DELTAtdk strain MS416. DELTAtdk strains show 5-fluoro-2'-deoxyuridine resistance. Mutant DELTAtdk/DELTAspeA strain MS531 shows a severe growth defect in polyamine-reduced medium
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additional information
the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
additional information
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the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
additional information
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the PA14 aguA-Gm, DELTAagu2ABCA' mutant cannot break down agmatine. Some clinical isolates of Pseudomonas aeruginosa also lack a functional agmatine deiminase
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additional information
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
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modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
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modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
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construction of negative mutant
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Escherichia coli strain MachI is used as a recipient for transformations during plasmid construction and for plasmid propagation and storage. Site-directed mutagenesis is performed on pPRDC.19. The mutant plasmids are transformed into Escherichia coli B834 (DE3) competent cells.
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysE
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expressed in Arabidopsis thaliana
expressed in Arabidopsis thaliana ecotype Col-0
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expressed in Escherichia coli
expressed in Escherichia coli BL21 as GST-fusion protein
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expressed in Escherichia coli BL21(DE3) cells
expressed in hairy roots of Lotus corniculatus
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expressed in Oryza sativa
expressed in the T7 expression system as a cleavable poly-Histagged fusion construct in Escherichia coli strain Rosetta (DE3) pLysS
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expressed in Trypanosoma cruzi, which lacks arginine decarboxylase in wild type
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expression as His-tag fusion protein in Escherichia coli
Paramecium bursaria Chlorella virus-1
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expression in COS-7 cells
expression in Escherichia coli
expression in Escherichia coli strain DE3
expression in Escherichia coli. The phylogeny of the crenarchaeal homologs suggests that the arginine decarboxylase gene evolves from a single duplication of an ancestral S-adenosylmethionine decarboxylase gene early in the crenarchaeota
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Paramecium bursaria chlorella virus
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expression of sense and anti-sense constructs
expression of the enzyme in transformed hairy root lines in sense and antisense orientation, expression analysis
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gene ADC, expression analysis under salt stress in calli, overview
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gene ADC, functional overexpression from retroviral vector hADC pLXSN in murine cortical astrocytes leading to and astrocyte-protective effect of human arginine decarboxylase transduction against oxygen-glucose deprivation (OGD), overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
gene ADC, quantitative real-time PCR expression analysis
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gene ADC, quantitative real-time PCR expression analysis, recombinant expression of C-terminally YFP-tagged enzyme in Nicotiana benthamiana leaves via transformation method with Agrobacterium tumefaciens strain EHA105, coexpression with transcription factor ICE1 from Poncirus trifoliata
gene ADC, real-time RT-PCR enzyme expression analysis
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gene ADC, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene ADC1, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression analysis
gene ADC1, quantitative real-time PCR expression analysis
gene ADC1, quantitative real-time PCR isozyme expression analysis
gene ADC1, recombinant heterologous expression of GFP-tagged isozyme ADC1 as homodimers in Nicotiana benthamiana using the Agrobacterium tumefaciens GV3101/pMP90 strain for transformation. The green fluorescence of GFP-AtADC1 fusion is slightly present in the cytosol and it colocalized with the red auto-fluorescence of chlorophyll channel in Nicotiana benthamiana leaf epidermal cells
gene ADC1, semi-quantitative RT-PCR enzyme expression analysis, Adc1 shows constitutive expression, recombinant expression of His-tagged isozyme in Escherichia coli
gene ADC1, sequence comparisons
gene ADC2, quantitative real-time PCR expression analysis
gene ADC2, quantitative real-time PCR isozyme expression analysis
gene ADC2, recombinant expression as GFP-tagged protein in Arabidopsis thaliana, recombinant heterologous expression in Nicotiana benthamiana in using the Agrobacterium tumefaciens GV3101/pMP90 strain for transformation, the GFP-AtADC2 fluorescence occurs in the cytosol, and it colocalizes with the red autofluorescence of chlorophyll of tobacco leaf epidermal cells
gene ADC2, semi-quantitative RT-PCR enzyme expression analysis, Adc2 shows constitutive expression, recombinant expression of His-tagged isozyme in Escherichia coli
gene ADC2, sequence comparisons
gene adiA, expression of untagged and N-terminally His10-tagged wild-type enzyme and inactivated mutant in strain BW25113
gene adiA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene CPn1032, expression of untagged and N-terminally His10-tagged enzyme in Escherichia coli strain Bl21(DE3), CPn1032 expression complements the adiA null mutation in Escherichia coli strain DEG0121, which shows low arginine decarboxylase enzyme activity and is deficient in AdiC transporter
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gene speA, expression of His-tagged enzyme in Escherichia coli
gene speA, recombinant expression of His6-tagged enzyme in Escherichia coli strain SM10
gene speA, recombinant overexpression of the enzyme in a soluble and active form in Escherichia coli strain BL21(DE3), method optimization leading to significant improvement of the production of agmatine. Method optimization, optimum conditions for agmatine production of the recombinant enzyme in vivo are 3.5 g/l intact cells, 4 mM Mg2+, 30 mM pyridoxal-5'-phosphate, pH 7, 37°C, method validation, overview. The specific activity of the overexpressing cell extract is 0.21 U/mg, which is 6.6fold higher than that of the BL21 cells not containing the overexpression plasmid
oat enzyme is expressed in Trypanosoma cruzi epimastigotes after transfection with a C-terminal six-His tag and as untagged enzyme, active ADC is expressed in the parasites and the primary translational product is cleaved into 2 polypeptides through a proteolytic process. When the his-tag is added to the C-terminal end of ADC it causes very significant changes on the metabolic stability and catalytic parameters of the heterologous enzyme expressed in the transformed parasites.
overexpression in Escherichia coli
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profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, overview
rapid amplification of cDNA ends (RACE) give rise to a full-length ADC cDNA (PpADC) with a complete open reading frame of 2178 bp, encoding a 725 amino acid polypeptide.
the hexahistidine tagged human ADC gene is delivered into mouse fibroblast cell line (NIH3T3) using retroviral vector and transfected into the PT-67 cell line
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Oryza sativa
expressed in Oryza sativa
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
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0.005 mlM MeHg, EtHg, PhHg and HgCl2 increase the protein expression by 1.23, 1.06, 1.45, and 1.33fold, respectively
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ADC is active early during pollen hydration and germination in vitro, ADC activity is activated during pollen germination
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ADC protein and transcript are increasingly expressed at early stages of hop internode culture (12 h). Protein and transcript continue accumulating until organogenic nodule formation after 28 days, decreasing thereafter
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after exposure to 0.2 mM methyl jasmonate for 6 h, the intensity of the Adc mRNA signal fell by approximately 90%, and after 24 h of treatment it returns to near the original level
arginine decarboxylase has been shown to be upregulated from the macrophage-like cell line RAW-264.7 in response to lipopolysaccharides and cytokines resulting in more intracellular agmatine. Bacterial agmatine secretion after infection with Pseudomonas aeruginosa is evident in changes in the inflammatory phenotype including increased total cell count
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as opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. High osmolarity, drought, salinity and wounding induce ADC2 expression. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also caused a several fold increase in ADC1 expression at both times after inoculation
bacterial infection induces putrescine accumulation and ADC1 expression in wild-type plants, but pathogen-induced putrescine accumulation is blocked in adc1 mutant. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also causes a several fold increase in ADC1 expression at both times after inoculation
enzyme activity and agmatine levels in human sputum peak during cystic fibrosis illness, decrease with treatment, and is positively correlated with inflammatory cytokines
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enzyme mRNA and protein expression are acutely induced by acid stress. Transcriptional factor Fur regulates the expression of the speA gene in the acid response
FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene, the promoter region of FcADC contains two W-box elements, which interacts with FcWRKY70
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FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene. Overexpression of FcWRKY70 in Citrus lemon confers enhances tolerance to dehydration and drought stresses. Transgenic lemon exhibits higher expression levels of ADC and accumulats larger amount of putrescine in comparison with the wild-type
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FcWRKY70, a WRKY protein of Fortunella crassifolia, functions in drought tolerance and modulates putrescine synthesis by regulating arginine decarboxylase gene. Overexpression of FcWRKY70 in Nicotiana nudicaulis confers enhanced tolerance to dehydration and drought stresses. Transgenic lemon exhibits higher expression levels of ADC and accumulats larger amount of putrescine in comparison with the wild-type
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ICE1 (inducer of CBF expression 1) encodes a MYC-like basic helix-loop-helix transcription factor that acts as a central regulator of cold response. Yeast two-hybrid screening reveals that 21 proteins belong to the PtrICE1 interactome, in which PtADC (arginine decarboxylase) is confirmed as a bona fide protein interacting with PtrICE1 (nuclear localization). Transcript levels of ADC genes in the transgenic lines are slightly elevated under normal growth conditions but substantially increased under cold conditions, consistent with changes in free polyamine levels
in enteroinvasive strains the presence of CadC reduces the expression of the arginine decarboxylase encoding gene adiA
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mercury compounds inhibits the enzyme activity but induce the enzyme expression in PC12 cells. The results indicate that ADC inhibition in PC12 cells by the four Hg compounds is due to the loss of enzyme activity, not protein level
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no effect of NaCl at 0.5 M on the expression of adc1
no effect of NaCl at 0.5 M on the expression of adc2
relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
salicylic acid treatment results in a significant increase in the expression of ADC after 3 h
salt stress clearly results in an increased steady-state transcript accumulation even though the specific activity shows no apparent change
steady-state accumulation of arginine decarboxylase transcripts and its specific activity are unaffected by dark incubation
transcript levels are up-regulated by low temperature and dehydration
transcription factor ICE1 from Poncirus trifoliata, PtICE1 (inducer of CBF expression 1) is a MYC-like basic helix-loop-helix transcription factor that acts as a central regulator of cold response. Transcript levels of ADC genes in the transgenic Nicotiana tabacum lines are slightly elevated under normal growth condition but substantially increased under cold conditions, consistent with changes in free polyamine levels
transcription factor ICE1 from Poncirus trifoliata, PtICE1 (inducer of CBF expression 1) is a MYC-like basic helix-loop-helix transcription factor that acts as a central regulator of cold response. Transcript levels of ADC genes in the transgenic Nicotiana tabacum lines are slightly elevated under normal growth condition but substantially increased under cold conditions, consistent with changes in free polyamine levels. Expression patterns of NtADC1 and NtADC2 in wild-type and transgenic tobacco lines before and after cold stress, overview
transcription factor ICE1 from Poncirus trifoliata, PtICE1 (inducer of CBF expression 1) is a MYC-like basic helix-loop-helix transcription factor that acts as a central regulator of cold response. Transcript levels of Citrus limon ADC gene in the transgenic lines are slightly elevated under normal growth condition but substantially increased under cold conditions, consistent with changes in free polyamine levels. Expression patterns of ClADC in lemon wild-type and transgenic lines before and after 5 h of cold stress, overview
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as opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. High osmolarity, drought, salinity and wounding induce ADC2 expression. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also caused a several fold increase in ADC1 expression at both times after inoculation
as opposed to wild-type plants, bacterial infection with Pseudomonas viridiflava strain Pvalb8 increases ADC2 expression and ADC activity in adc1 mutants, which can counterbalance the lack of ADC1. High osmolarity, drought, salinity and wounding induce ADC2 expression. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also caused a several fold increase in ADC1 expression at both times after inoculation
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bacterial infection induces putrescine accumulation and ADC1 expression in wild-type plants, but pathogen-induced putrescine accumulation is blocked in adc1 mutant. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also causes a several fold increase in ADC1 expression at both times after inoculation
bacterial infection induces putrescine accumulation and ADC1 expression in wild-type plants, but pathogen-induced putrescine accumulation is blocked in adc1 mutant. In non-inoculated adc mutants, the lack of each ADC isoform has no effect on expression of the other isoforms. Infection of the adc2-3 mutant also causes a several fold increase in ADC1 expression at both times after inoculation
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enzyme mRNA and protein expression are acutely induced by acid stress. Transcriptional factor Fur regulates the expression of the speA gene in the acid response
enzyme mRNA and protein expression are acutely induced by acid stress. Transcriptional factor Fur regulates the expression of the speA gene in the acid response
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relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
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relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
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relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
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