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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q9UWU1
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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: Saccharolobus solfataricus
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
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-
-
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ARGDC
-
-
-
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bADC
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-
-
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
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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
-
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-canavanine
N-(3-aminopropoxy)guanidine + CO2
decarboxylation at 40% of the activity compared with L-arginine
-
-
?
L-arginine
agmatine + CO2
the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
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
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
difluoromethyl-L-arginine
1 mM, 80 °C, 15 min, 64% loss of activity, irreversible inhibition
L-argininamide
1 mM, almost completely abolished arginine decarboxylase activity
O-(4-nitrobenzyl)hydroxylamine
1 mM, 50% inhibition, pyruvoyl group modification
O-Methylhydroxylamine
1 mM, 50% inhibition, pyruvoyl group modification
additional information
1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine
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additional information
-
1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
pH 4.0: about 65% of maximal activity, pH 6.0: optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 (Ser82) 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
-
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
pH 6.0, 10 min, enzyme retains 80% of ist original activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. The phylogeny of the crenarchaeal homologs suggests that the arginine decarboxylase gene evolves from a single duplication of an ancestral S-adenosylmethionine decarboxylase gene early in the crenarchaeota
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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