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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Escherichia coli and UniProt Accession P21170
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4.1.1.19 arginine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, atadc2, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, ptadc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADC
AdiA
ARGDC
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic arginine decarboxylase
-
-
-
-
ADC
-
-
-
-
ARGDC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-77-5
-
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-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-arginine
agmatine + CO2
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
NATURAL SUBSTRATE
NATURAL 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-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-arginine
agmatine + CO2
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
a formyl group of pyridoxal 5'-phosphate is bound to the 6-amino group of a Lys residue. Binds 10 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
structure of the pyridoxal 5'-phosphate binding site: Ala-Thr-His-Ser-Thr-His-(pyridoxal 5'-phosphate)Lys-Leu-Leu-Asn-Ala-Leu-Ser-Gln-Ala-Ser-Tyr
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
required, best at 4 mM in vivo assay, 88% activation of recombinant enzyme at 4 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
over 70% of maximal activity within this range, profile overview
3.5 - 7
-
pH 3.5: about 50% of maximal activity, pH 7.0: 23% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
over 70% of maximal activity within this range, profile overview
20 - 50
-
20°C: about 40% of maximal activity, 50°C: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
82000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
additional information
-
effects of substrate, coenzyme, and positive and negative effectors on the enzyme structure
decamer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
dimer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with a sulfate ion, microbatch method, using 100 mM HEPES pH 8.5 and 1.6 M ammonium sulfate
hanging drop vapor diffusion method, using 1 M lithium sulfate monohydrate, 0.1 M Na citrate tribasic dihydrate pH 5.6, and 0.5 M ammonium sulfate
-
sparse matrix method, using 100 mM MES, pH 6.5, 13% PEG 8000, and 400 mM sodium acetate, at 20°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
additional information
-
construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
stable at, purified recombinant enzyme, 1 h, over 80% activity remaining
748413
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
stable at, the purified recombinant enzyme is stable only up to 40°C with 78.6% of the activity remaining after a 1 h incubation at 40°C. Incubation at temperatures above this causes a rapid drop in activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 12.4fold from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and dialysis
Ni-NTA column chromatography, HiTrap Q column chromatography, and DEAE Sepharose column chromatography
-
nickel chelating column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expressed in the T7 expression system as a cleavable poly-Histagged fusion construct in Escherichia coli strain Rosetta (DE3) pLysS
-
gene adiA, expression of untagged and N-terminally His10-tagged wild-type enzyme and inactivated mutant in strain BW25113
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morris, D.R.; Boeker, E.A.
Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli
Methods Enzymol.
94
125-134
1983
Escherichia coli
Wu, W.H.; Morris, D.R.
Biosynthetic arginine decarboxylase from E. coli: Biosynthetic arginine decarboxylase from Escherichia coli
J. Biol. Chem.
248
1696-1699
1973
Escherichia coli
Boeker, E.A.; Snell, E.E.
Arginine decarboxylase (Escherichia coli B)
Methods Enzymol.
17B
657-662
1971
Escherichia coli, Escherichia coli B / ATCC 11303
-
Blethen, S.L.; Boeker, E.A.; Snell, E.E.
Arginine decarboxylase from Escherichia coli: Arginine decarboxylase from escherichia coli. I. Purification and specificity for substrates and coenzyme
J. Biol. Chem.
243
1671-1677
1968
Escherichia coli, Escherichia coli B / ATCC 11303
Boecker, E.A.
Arginine decarboxylase from Escherichia coli B: mechanism of dissociation from the decamer to the dimer
Biochemistry
17
258-263
1978
Escherichia coli
Boeker, A.B.
Kinetics of the decamer - dimer dissociation of arginine decarboxylase
Biochem. Biophys. Res. Commun.
75
179-185
1977
Escherichia coli
Boecker, E.A.; Fischer, E.H.; Snell, E.
Arginine decarboxylase from Escherichia coli
J. Biol. Chem.
246
6776-6781
1971
Escherichia coli
Moore, R.C.; Boyle, S.M.
Cyclic AMP inhibits and putrescine represses expression of the speA gene encoding biosynthetic arginine decarboxylase
J. Bacteriol.
173
3615-3621
1991
Escherichia coli
Rodriguez, B.R.; Carroll, D.W.; Mitchell, D.; Momany, C.; Hackert, M.L.
Crystallization of biosynthetic arginine decarboxylase from Escherichia coli
Acta Crystallogr. Sect. D
50
175-177
1994
Escherichia coli
Giles, T.N.; Graham, D.E.
Characterization of an acid-dependent arginine decarboxylase enzyme from Chlamydophila pneumoniae
J. Bacteriol.
189
7376-7383
2007
Chlamydia pneumoniae, Escherichia coli (P28629), Escherichia coli, Chlamydia pneumoniae Kajaani 6
Bi, H.; Sun, L.; Fukamachi, T.; Saito, H.; Kobayashi, H.
HU participates in expression of a specific set of genes required for growth and survival at acidic pH in Escherichia coli
Curr. Microbiol.
58
443-448
2009
Escherichia coli
Andrell, J.; Hicks, M.G.; Palmer, T.; Carpenter, E.P.; Iwata, S.; Maher, M.J.
Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity
Biochemistry
48
3915-3927
2009
Escherichia coli (P28629), Escherichia coli
Song, J.; Zhou, C.; Liu, R.; Wu, X.; Wu, D.; Hu, X.; Ding, Y.
Expression and purification of recombinant arginine decarboxylase (SpeA) from Escherichia coli
Mol. Biol. Rep.
37
1823-1829
2010
Escherichia coli
Forouhar, F.; Lew, S.; Seetharaman, J.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Tong, L.
Structures of bacterial biosynthetic arginine decarboxylases
Acta Crystallogr. Sect. F
66
1562-1566
2010
Escherichia coli (P21170), Escherichia coli, Campylobacter jejuni (Q0PAC6), Campylobacter jejuni, Campylobacter jejuni NCTC 11168 (Q0PAC6)
Sun, X.; Song, W.; Liu, L.
Enzymatic production of agmatine by recombinant arginine decarboxylase
J. Mol. Catal. B
121
1-8
2015
Escherichia coli (P21170)
-
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