Information on EC 4.1.1.19 - Arginine decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.1.1.19
-
RECOMMENDED NAME
GeneOntology No.
Arginine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine = agmatine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
arginine dependent acid resistance
-
-
L-arginine degradation III (arginine decarboxylase/agmatinase pathway)
-
-
L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway)
-
-
Metabolic pathways
-
-
polyamine pathway
-
-
putrescine biosynthesis I
-
-
putrescine biosynthesis II
-
-
putrescine biosynthesis IV
-
-
spermidine biosynthesis III
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-77-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ssp. oleifera
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Kajaani 6, gene CPn1032
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-
Manually annotated by BRENDA team
strain Kajaani 6, gene CPn1032
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-
Manually annotated by BRENDA team
serovar L2 and D strains
-
-
Manually annotated by BRENDA team
Chlamydophila caviae
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
Helicobacter pylori ATCC 700392
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Heliotropium spathulatum
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
variant Nugget
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
(L) var. Ventus
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain TMC 1546
-
-
Manually annotated by BRENDA team
strain TMC 1546
-
-
Manually annotated by BRENDA team
no activity in Trypanosoma cruzi
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Paramecium bursaria chlorella virus
-
-
-
Manually annotated by BRENDA team
Paramecium bursaria Chlorella virus-1
enzyme displays ornithine decarboxylase as well as arginine decarboxylase activity
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
endemic in subantarctic region, high levels of polyamines and agmatine
-
-
Manually annotated by BRENDA team
Mochizuki and Akatsuki fruits
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bl
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain RA
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-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arginine
?
show the reaction diagram
-
-
-
-
?
L-Arg
?
show the reaction diagram
L-arginine
agmatine + CO2
show the reaction diagram
L-Asp
?
show the reaction diagram
-
2.6% of the activity with L-Arg
-
-
-
L-Canavanine
?
show the reaction diagram
L-canavanine
gamma-guanidinoxypropylamine + CO2
show the reaction diagram
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
show the reaction diagram
L-Glu
?
show the reaction diagram
-
2.1% of the activity with L-Arg
-
-
-
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
L-lysine
?
show the reaction diagram
assay at pH 6.5, 10 min, 50C
-
-
?
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-Orn
?
show the reaction diagram
-
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
L-ornithine
putrescine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
L-Phe
phenylethylamine + CO2
show the reaction diagram
-
1.4% of the activity with L-Arg
-
-
-
L-Pro
?
show the reaction diagram
-
3.8% of the activity with L-Arg
-
-
-
L-Ser
?
show the reaction diagram
-
4.4% of the activity with L-Arg
-
-
-
meso-diaminopimelate
?
show the reaction diagram
Ngamma-monomethyl-L-Arg
N-(3-aminopropyl)-N'-methylguanidine + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Arg
?
show the reaction diagram
L-arginine
agmatine + CO2
show the reaction diagram
L-ornithine
putrescine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Pyruvoyl group
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser82) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activates at 1 mM, overview
Mn2+
-
0.1 mM increases activity by 35%. 0.01-0.1 mM, enhances activity. Inhibition at higher concentrations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
4-Guanidinobutyrate
-
-
5-Deoxypyridoxal
-
-
agmatine
alpha-Difluoromethylarginine
alpha-difluoromethylornithine
Arcain
-
-
beta-(2-Methyl-3-hydroxy-4-formylpyridine-5)-propionic acid
-
-
canavanine
citrulline
D-arginine
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
Fluorescein isothiocyanate
-
0.09 mM, 40% inhibition
guanidine
Guanidinoacetic acid
-
-
homoarginine
hydroxylamine
iodoacetamide
-
-
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-argininamide
L-arginine methyl ester
L-arginineamide
-
-
L-Argininic acid
-
-
L-canavanine
L-histidine
1 mM, 20-30% inhibition
L-homoarginine
Methyl bis-[guanylhydrazone]
-
-
-
methylglyoxal bisguanylhydrazone
-
-
Methylguanidine
Monofluoromethylagmatine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
N-benzylguanidine
-
-
N-Carbamoylputrescine
-
-
n-propylguanidine
-
-
N5-Hydroxy-DL-Arg
-
-
Na+
-
10 mM, 20% decrease of activity
Nalpha-acetyl-L-arginine
1 mM, 20-30% inhibition
NG-methylarginine
-
-
NG-Nitroarginine
-
-
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
phenylhydrazine
-
-
phosphate
-
-
Polyamines
putrescine
pyridoxal
Pyridoxine-HCl
Semicarbazide
-
-
spermidine
spermine
urethane
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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.
dithiothreitol
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
EDTA
-
stimulates
gibberellic acid
-
stimulates
indoleacetic acid
-
stimulates
kinetin
-
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
pyridoxal 5'-phosphate
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.
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00031 - 7.1
L-Arg
0.03 - 5.6
L-arginine
0.233 - 1.2
L-canavanine
9.53
L-N5-(iminoethyl)-ornithine
-
pH 7.5, 37C
7.5 - 180
L-ornithine
0.163
Ngamma-methyl-L-arginine
-
pH 7.5, 37C
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 6.9
L-Arg
0.025 - 11
L-arginine
0.11
L-canavanine
Yersinia pestis
-
pH 7.5, 37C
0.419
L-N5-(iminoethyl)-ornithine
Yersinia pestis
-
pH 7.5, 37C
0.04
L-ornithine
Bacillus subtilis
-
at pH 7.5, 70C
1.22
Ngamma-methyl-L-arginine
Yersinia pestis
-
pH 7.5, 37C
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 18
L-arginine
0.0056
L-ornithine
Bacillus subtilis
-
at pH 7.5, 70C
192
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.77
agmatine
-
pH 7.5, 37C
0.0206
D-Arg
-
pH 7.5, 37C
0.8
DL-alpha-Difluoromethylarginine
-
3.39
guanidine
-
pH 7.5, 37C
0.897
L-argininamide
-
pH 7.5, 37C
0.189
L-arginine methyl ester
-
pH 7.5, 37C
0.327
L-Argininic acid
-
pH 7.5, 37C
0.427
L-canavanine
-
pH 7.5, 37C
1.53
L-homoarginine
-
pH 7.5, 37C
3.09
Methylguanidine
-
pH 7.5, 37C
1.4
N-benzylguanidine
-
pH 7.5, 37C
1.93
n-propylguanidine
-
pH 7.5, 37C
0.168
NG-methyl-D-arginine
-
pH 7.5, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8
Ca2+
Rattus norvegicus
-
IC50: 0.8 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0012
untagged ADC
0.002
-
murtant N47A, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
0.0023
-
-
0.00738
crude extract
0.0096
-
-
0.01104
heat treatment
0.02394
after purification with DEAE-Toyopearl 650M
0.0331
His-tagged ADC
0.0381
after purification with DEAE-5PW
0.113
-
-
0.132
-
mutant E109Q, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
0.151
-
crude extract, in 67 mM Tris-HCl (pH 7.5), 3.3 mM EDTA, 3.3 mM dithiothreitol, 0.04 mM pyridoxal 5'-phosphate
0.39
-
at pH 7.5, 37C
1.014
-
wild type enzyme, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
1.026
at the semi-final step of purification with HA-1000 column chromatography
1.5
-
at pH 7.5, 37C
2.8
-
purified enzyme, in 67 mM Tris-HCl (pH 7.5), 3.3 mM EDTA, 3.3 mM dithiothreitol, 0.04 mM pyridoxal 5'-phosphate
8.1
-
purified recombinant enzyme
14.94
final step of purification with MonoQ HR 5/5
16.4
-
biosynthetic arginine decarboxylase
350 - 370
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
-
7.2 - 7.4
-
-
7.8
-
assay at
8 - 9
-
at 60C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5 - 5.5
-
activity range
3.5 - 7
-
pH 3.5: about 50% of maximal activity, pH 7.0: 23% of maximal activity
4 - 6
pH 4.0: about 65% of maximal activity, pH 6.0: optimum
4 - 9
-
about 50% of maximal activity at pH 4 and 9
5 - 8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
6.5 - 9
80% enzyme activity at pH 7.0, 70% enzyme activity at pH 8.0, 50% enzyme activity at pH 9.0
7 - 11
-
pH 7: about 25% of maximal activity, pH 11: 80% of maximal activity
7.2 - 8.8
-
pH 7.2: about 45% of maximal activity, pH 8.8: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
-
37
assay at
37 - 40
-
-
50
-
around 50C
75
-
optimum temperature at above 75C
90
-
activity increases up to
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
-
about 50% of maximal activity at 20C and 80C
20 - 50
-
20C: about 40% of maximal activity, 50C: about 70% of maximal activity
20 - 80
-
-
30 - 37
-
30C: maximal activity, 37C: about 35% of maximal activity
37 - 45
-
37C: about 50% of maximal activity, 45C: maximal activity
40 - 70
after 10 min incubation at 50C 4fold higher enzyme activity than at 40C, after 10 min incubation at 55C 7fold higher enzyme activity than at 40C, after 10 min incubation at 60C 10fold higher enzyme activity than at 40C, after 10 min incubation at 70C 1.2fold higher enzyme activity than at 40C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
calculated from amino acid sequence
5.2
predicted from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
about 5% of the activity in aorta
Manually annotated by BRENDA team
-
highest activity of all tissues tested
Manually annotated by BRENDA team
-
presence of both arginine decarboxylase and arginase in principal neurons and putative interneurons
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
Manually annotated by BRENDA team
-
about 40% of the activity in aorta
Manually annotated by BRENDA team
-
about 75% of the activity in aorta
Manually annotated by BRENDA team
-
significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
Manually annotated by BRENDA team
-
of both 4-week-old avocado fruitlet and fully developed fruit
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
-
about 60% of the activity in aorta
Manually annotated by BRENDA team
-
about 15% of the activity in aorta
Manually annotated by BRENDA team
additional information