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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Helicobacter pylori and UniProt Accession O25176
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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: Helicobacter pylori
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, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, atadc2, ptadc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADC
-
-
-
-
ARGDC
-
-
-
-
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic arginine decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
difluoromethylornithine
1-(4-amino-5,5-difluoropentyl)guanidine + CO2
over 90% activity compared to L-arginine
-
-
?
L-ornithine
putrescine + CO2
about 90% activity compared to 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
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
the cofactor binding residues are conserved
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
required for catalysis, divalent metal ions are essential for activity, the metal binding residues are conserved
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
arginine decarboxylases belong to a family of fold III PLP (pyridoxal 5'-phosphate)-dependent decarboxylases
metabolism
L-arginine formed by ADC may be transported out from cytosol to extracellular milieu by a transporter protein, AdiC. The metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment
physiological function
additional information
physiological function
Helicobacter pylori uses arginine in an acid response mechanism required for its growth in acid conditions
physiological function
the metabolism of L-arginine by ADC in Helicobacter pylori might be crucial for its survival in the acidic environment. To neutralize the pH of the stomach, it transports L-arginine (+1 charge) into the cell and agmatine (+2 charge) out of the cell, which results in the export of 1 proton during each turnover and thus the bacteria can survive in the acidic environment
additional information
Cys487, a conserved residue located at the active-site, is involved in the catalysis, with a pKa value of about 7.2. The homology model of the protein shows conserved alpha/beta TIM barrel and beta-sandwich domains, which are characteristic features of fold III decarboxylases. Cys487 has a marginal role in the stability. Helicobacter pylori ADC homology modeling and docking studies, overview
additional information
-
Cys487, a conserved residue located at the active-site, is involved in the catalysis, with a pKa value of about 7.2. The homology model of the protein shows conserved alpha/beta TIM barrel and beta-sandwich domains, which are characteristic features of fold III decarboxylases. Cys487 has a marginal role in the stability. Helicobacter pylori ADC homology modeling and docking studies, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C487A
site-directed mutagenesis, the mutant shows less than 10% of wild-type activity, but only slightly reduced temperature stability compared to wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ADC, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA and protein expression are acutely induced by acid stress. Transcriptional factor Fur regulates the expression of the speA gene in the acid response
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valenzuela, M.; Caceres, A.; Almarza, O.; Bravo, D.; Soto, S.; Cerda, O.; Toledo, H.
Characterization of the arginine decarboxylase gene (ORF HP0422, speA) involved in acid tolerance in Helicobacter pylori
Helicobacter
19
182-193
2014
Helicobacter pylori (O25176), Helicobacter pylori, Helicobacter pylori ATCC 700392 (O25176)
Alam, M.; Srivastava, A.; Dutta, A.; Sau, A.K.
Biochemical and biophysical studies of Helicobacter pylori arginine decarboxylase, an enzyme important for acid adaptation in host
IUBMB Life
70
658-669
2018
Helicobacter pylori (O25176), Helicobacter pylori, Helicobacter pylori ATCC 700392 / 26695 (O25176)
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Release 2023.1 (January 2023)
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