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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.19 arginine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, pyruvoyl-dependent arginine decarboxylase, atadc2, l-arginine decarboxylase, ptadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ARGDC
-
-
-
-
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic arginine decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-77-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8F9JSR4_PSEAI
636
0
70652
TrEMBL
-
A0A8G3YAC7_PSEAI
636
0
70641
TrEMBL
-
A0A069Q1I4_PSEAI
636
0
70668
TrEMBL
-
A0A8G2NU01_PSEAI
636
0
70696
TrEMBL
-
A0A080VQ65_PSEAI
636
0
70695
TrEMBL
-
A0A2R3J1B7_PSEAI
636
0
70581
TrEMBL
-
A0A485EF37_PSEAI
267
0
28844
TrEMBL
-
A0A6H3GEA5_PSEAI
636
0
70711
TrEMBL
-
A0A8G7CAL9_PSEAI
636
0
70638
TrEMBL
-
A0A367LX92_PSEAI
136
0
15287
TrEMBL
-
A0A8G6K873_PSEAI
636
0
70624
TrEMBL
-
A0A2R3IN26_PSEAI
751
0
82502
TrEMBL
-
A0A8G7LXK2_PSEAI
636
0
70608
TrEMBL
-
A0A367LT35_PSEAI
74
0
7862
TrEMBL
-
A0A8G5TXC2_PSEAI
636
0
70719
TrEMBL
-
A0A8G2VUN3_PSEAI
636
0
70641
TrEMBL
-
A0A8G7PLX9_PSEAI
636
0
70608
TrEMBL
-
A0A431XB26_PSEAI
636
0
70667
TrEMBL
-
A0A4P0TI29_PSEAI
519
0
57578
TrEMBL
-
A0A8E5UW51_PSEAI
636
0
70714
TrEMBL
-
A0A8B5BKE0_PSEAI
636
0
70726
TrEMBL
-
A0A6A9K1Y0_PSEAI
636
0
70625
TrEMBL
-
A0A367LWN1_PSEAI
127
0
14055
TrEMBL
-
A0A367LYF4_PSEAI
125
0
14037
TrEMBL
-
A0A8G4VRZ7_PSEAI
636
0
70682
TrEMBL
-
A0A8G2RPG1_PSEAI
636
0
70654
TrEMBL
-
A0A8G3BRZ7_PSEAI
636
0
70692
TrEMBL
-
A0A3M5EVD4_PSEAI
659
0
73269
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70600, about, recombinant His6-tagged enzyme, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
purified recombinant enzyme, pH 8.4, 10 min, inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain SM10 by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene speA, recombinant expression of His6-tagged enzyme in Escherichia coli strain SM10
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dalluge, J.J.; McCurtain, J.L.; Gilbertsen, A.J.; Kalstabakken, K.A.; Williams, B.J.
Determination of agmatine using isotope dilution UPLC-tandem mass spectrometry application to the characterization of the arginine decarboxylase pathway in Pseudomonas aeruginosa
Anal. Bioanal. Chem.
407
5513-5519
2015
Pseudomonas aeruginosa (A0A0H2ZHZ8), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZHZ8)
Manually annotated by BRENDA team
Paulson, N.B.; Gilbertsen, A.J.; Dalluge, J.J.; Welchlin, C.W.; Hughes, J.; Han, W.; Blackwell, T.S.; Laguna, T.A.; Williams, B.J.
The arginine decarboxylase pathways of host and pathogen interact to impact inflammatory pathways in the lung
PLoS ONE
9
e111441
2014
Homo sapiens, Mus musculus, Pseudomonas aeruginosa (Q9HUX1), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HUX1)
Manually annotated by BRENDA team