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Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, atadc2, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, ptadc,
more
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acid-induced biodegradative arginine decarboxylase
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arginine decarboxlase 2
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arginine decarboxylase2
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arginine:agmatine exchange system
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Biosynthetic arginine decarboxylase
biosynthetic arginine decarboxylase 1
UniProt
biosynthetic arginine decarboxylase 2
UniProt
Decarboxylase, arginine
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PaADC1
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expressed in all stages of development, up-regulated in response to chilling or salt stress in seedling stage
PaADC2
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expressed mainly in mature plant
PBCV-1 DC
Paramecium bursaria Chlorella virus-1
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pyruvoyl-dependent arginine decarboxylase
pyruvoyl-dependent arginine decraboxylase
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Synthetic arginine decarboxylase
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ADC

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ADC
Paramecium bursaria chlorella virus
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ADC1

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ADC2

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AdiA

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ARGDC

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arginine decarboxylase

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arginine decarboxylase
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arginine decarboxylase
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arginine decarboxylase
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arginine decarboxylase
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arginine decarboxylase
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ATADC1

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AtADC2

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Biosynthetic arginine decarboxylase

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Biosynthetic arginine decarboxylase
UniProt
Biosynthetic arginine decarboxylase
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CPn1032 homolog

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HP0422

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HVO_1958

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L-Arginine decarboxylase

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L-Arginine decarboxylase
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PdaD

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protein SSO0536

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PvlArgDC

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pyruvoyl-dependent arginine decarboxylase

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pyruvoyl-dependent arginine decarboxylase
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pyruvoyl-dependent arginine decarboxylase
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SpeA

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StADC

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additional information

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the enzyme is a decarboxylase of the AR structural family
additional information
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the enzyme is a decarboxylase of the AR structural family
additional information
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the enzyme is a decarboxylase of the AR structural family
additional information
Paramecium bursaria chlorella virus
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the enzyme belongs to the group IV of pyridoxal 5'-phosphate-dependent decarboxylases belonging to the alpha/beta barrel structural family
additional information
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the enzyme is a decarboxylase of the AR structural family
additional information
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the enzyme is a decarboxylase of the AR structural family
additional information
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the enzyme is a decarboxylase of the AR structural family
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L-arginine = agmatine + CO2
L-arginine = agmatine + CO2

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L-arginine = agmatine + CO2
reaction mechanism via geminal diamine intermediate
L-arginine = agmatine + CO2
the K148-loop movement may be kinetically linked to the rate-limiting step of product release, active site structure, mechanism
Paramecium bursaria chlorella virus
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difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
L-arginine
agmatine + CO2
L-Asp
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2.6% of the activity with L-Arg
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?
L-canavanine
gamma-guanidinoxypropylamine + CO2
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
L-Glu
?
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2.1% of the activity with L-Arg
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?
L-lysine
1,5-diaminopentane + CO2
L-lysine
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assay at pH 6.5, 10 min, 50°C
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?
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
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L-Orn
Putrescine + CO2
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?
L-ornithine
1,4-diaminobutane + CO2
L-ornithine
putrescine + CO2
L-Phe
phenylethylamine + CO2
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1.4% of the activity with L-Arg
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?
L-Pro
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3.8% of the activity with L-Arg
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?
L-Ser
?
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4.4% of the activity with L-Arg
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?
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
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?
additional information
?
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difluoromethylornithine

1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 90% activity compared to L-arginine
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?
difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 90% activity compared to L-arginine
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?
L-Arg

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enzyme is involved in synthesis of polyamines
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L-Arg
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inducible enzyme
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L-Arg
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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
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L-Arg
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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
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?
L-Arg
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the biosynthetic arginine decarboxylase is the first of two enzymes in a putrescine biosynthetic pathway
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L-Arg
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higher activity in plants cultivated on ammonium chloride than in plants grown on nitrate
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L-Arg
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regulatory role in growth and cell division
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L-Arg
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key enzyme in polyamine metabolism of plants
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L-Arg
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constitutive enzyme
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L-Arg
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agmatine production by the mitochondria could serve as a protective mechanism against cytotoxicity from excessive nitric oxide formation
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?
L-Arg
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possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
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L-Arg
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possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
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L-Arg
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important enzyme in putrescine and polyamine biosynthesis
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L-arginine

agmatine + CO2
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?
L-arginine
agmatine + CO2
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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
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
amino acids K136 and C524 of ADC1 are essential for activity and participate in separate active sites
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?
L-arginine
agmatine + CO2
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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
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?
L-arginine
agmatine + CO2
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rate limiting and key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, induced in response to salt stress
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
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L-arginine
agmatine + CO2
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key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
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L-arginine
agmatine + CO2
first reaction of a putrescine synthetic pathway found in bacteria and plants
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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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
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?
L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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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
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2
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?
L-arginine
agmatine + CO2