4.1.1.19: arginine decarboxylase
This is an abbreviated version!
For detailed information about arginine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.19
-
4.1.1.19
-
polyamine
-
putrescine
-
ornithine
-
spermidine
-
s-adenosylmethionine
-
arginase
-
diamine
-
samdc
-
decarboxylases
-
agmatinase
-
deiminase
-
alpha-difluoromethylornithine
-
cadaverine
-
imidazoline
-
d-arginine
-
pao
-
3.5.3.1
-
iminohydrolase
-
arginine-dependent
-
scots
-
ureohydrolase
-
difluoromethylornithine
-
pyrogenic
-
drug development
-
agriculture
-
hyoscyamine
-
trifoliata
-
poncirus
-
speb
-
tropane
-
dl-alpha-difluoromethylornithine
-
antizyme
-
datura
- 4.1.1.19
- polyamine
- putrescine
- ornithine
- spermidine
- s-adenosylmethionine
- arginase
-
diamine
- samdc
- decarboxylases
- agmatinase
- deiminase
- alpha-difluoromethylornithine
- cadaverine
-
imidazoline
- d-arginine
- pao
-
3.5.3.1
-
iminohydrolase
-
arginine-dependent
-
scots
-
ureohydrolase
- difluoromethylornithine
-
pyrogenic
- drug development
- agriculture
- hyoscyamine
- trifoliata
- poncirus
- speb
-
tropane
- dl-alpha-difluoromethylornithine
- antizyme
- datura
Reaction
Synonyms
AaxB, AaxB protein, acid-induced biodegradative arginine decarboxylase, ADC, ADC 1, ADC 2, ADC1, ADC2, AdiA, ARGDC, arginine decarboxlase 2, arginine decarboxylase, arginine decarboxylase2, arginine:agmatine exchange system, ATADC1, AtADC2, AtDC2, bADC, Biosynthetic arginine decarboxylase, biosynthetic arginine decarboxylase 1, biosynthetic arginine decarboxylase 2, ClADC, CPn1032 homolog, dADC, Decarboxylase, arginine, HP0422, HVO_1958, L-Arginine decarboxylase, More, NtADC1, NtADC2, PaADC1, PaADC2, PBCV-1 DC, PdaD, PpADC, protein SSO0536, PtADC, PvlArgDC, pyruvoyl-dependent arginine decarboxylase, pyruvoyl-dependent arginine decraboxylase, slr0662, slr1312, SPE1, SPE2, SpeA, speA1, speA2, StADC, Synthetic arginine decarboxylase, Tk-PdaD, TK0149
ECTree
4.1.1.19 arginine decarboxylaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 4.1.1.19 - arginine decarboxylase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
-
-
-
-
?
N-omega-nitro-L-arginine methyl ester
methyl formate + 1-(4-amino-5,5-difluoropentyl)guanidine + CO2
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
Helicobacter pylori ATCC 700392 / 26695
over 90% activity compared to L-arginine
-
-
?
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
?
-
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-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
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
-
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
-
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
-
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
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
-
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
-
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
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
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
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
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
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
-
-
?
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
the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
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
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
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
no activity with ornithine and lysine
-
-
?
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
-
-
?
L-arginine
agmatine + CO2
the enzyme exists in two different conformational states, one that binds ligand and one that does not
-
-
?
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-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
-
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
Helicobacter pylori ATCC 700392 / 26695
about 90% activity compared to L-arginine
-
-
?
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
Helicobacter pylori ATCC 700392 / 26695
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
-
-
?
