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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JFI4
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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: Thermococcus kodakarensis
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
-
-
-
-
ARGDC
-
-
-
-
bADC
-
-
-
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Biosynthetic arginine decarboxylase
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-
-
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dADC
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-
-
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Decarboxylase, arginine
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-
-
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L-Arginine decarboxylase
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-
-
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Synthetic arginine decarboxylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
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
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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-arginine
agmatine + CO2
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
no activity with ornithine and lysine
-
-
?
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-arginine
agmatine + CO2
first step of polyamine biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
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additional information
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pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
a gene disruptant lacking arginine decarboxylase is constructed, showing that it grows only in the medium in the presence of agmatine but not in the absence of agmatine. The results indicates that agmatine is essential for the cell growth of Thermococcus kodakaraensis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12600
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
synthesized as an inactive proenzyme
pyruvoyl group formation
the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser44) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 4.1.1.19)
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Release 2023.1 (January 2023)
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