Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Yersinia pestis and UniProt Accession Q8ZHG8

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This record set is specific for:
Yersinia pestis
UNIPROT: Q8ZHG8


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Yersinia pestis

EC NUMBER
COMMENTARY hide
4.1.1.19
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RECOMMENDED NAME
GeneOntology No.
arginine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine = agmatine + CO2
show the reaction diagram
reaction mechanism via geminal diamine intermediate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arginine dependent acid resistance
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L-arginine degradation III (arginine decarboxylase/agmatinase pathway)
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L-arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway)
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putrescine biosynthesis I
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putrescine biosynthesis II
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putrescine biosynthesis IV
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spermidine biosynthesis III
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polyamine pathway
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Arginine and proline metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-77-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene speA
SwissProt
Manually annotated by BRENDA team
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
L-arginine
agmatine + CO2
show the reaction diagram
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
show the reaction diagram
-
-
-
-
?
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
show the reaction diagram
-
-
-
-
?
Ngamma-monomethyl-L-Arg
N-(3-aminopropyl)-N'-methylguanidine + CO2
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q8ZHG8
ADC is the primary polyamine biosynthetic enzyme in the pathway
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-
?
L-arginine
agmatine + CO2
show the reaction diagram
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key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a fold III, pyridoxal 5'-phosphate-dependent enzyme
pyridoxal 5'-phosphate
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required for activity
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
agmatine
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-
guanidine
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L-arginine methyl ester
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L-arginineamide
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L-Argininic acid
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L-canavanine
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L-homoarginine
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Methylguanidine
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N-benzylguanidine
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n-propylguanidine
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Ngamma-methyl-D-arginine
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-Arg
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pH 7.5, 37°C
0.233
L-canavanine
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pH 7.5, 37°C
9.53
L-N5-(iminoethyl)-ornithine
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pH 7.5, 37°C
0.163
Ngamma-methyl-L-arginine
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pH 7.5, 37°C
additional information
additional information
pre-steady-state kinetics of substrate, product, and inhibitor with ADC by single-wavelength stopped-flow spectroscopy, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.46
L-Arg
-
pH 7.5, 37°C
0.11
L-canavanine
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pH 7.5, 37°C
0.419
L-N5-(iminoethyl)-ornithine
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pH 7.5, 37°C
1.22
Ngamma-methyl-L-arginine
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pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.77
agmatine
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pH 7.5, 37°C
0.0206
D-Arg
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pH 7.5, 37°C
3.39
guanidine
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pH 7.5, 37°C
0.897
L-argininamide
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pH 7.5, 37°C
0.189
L-arginine methyl ester
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pH 7.5, 37°C
0.327
L-Argininic acid
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pH 7.5, 37°C
0.427
L-canavanine
-
pH 7.5, 37°C
1.53
L-homoarginine
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pH 7.5, 37°C
3.09
Methylguanidine
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pH 7.5, 37°C
1.4
N-benzylguanidine
-
pH 7.5, 37°C
1.93
n-propylguanidine
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pH 7.5, 37°C
0.168
NG-methyl-D-arginine
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pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
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4 * 74000, crystal structure analysis
163100
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apo-ADC, light-scattering analysis
178000
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holo-ADC, light-scattering analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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in solution at pH 8.0, light-scattering analysis
tetramer
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4 * 74000, crystal structure analysis
additional information
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the presence and absence of Mg2+ and pyridoxal 5’-phosphate
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant protein using His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene speA, expression of His-tagged enzyme in Escherichia coli
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is an attractive target for drug design