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

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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:
Yersinia pestis
UNIPROT: Q8ZHG8
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The taxonomic range for the selected organisms is: Yersinia pestis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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L-arginine
=
agmatine
+
CO2
=
+
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, atadc2, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, ptadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADC
-
-
-
-
ARGDC
-
-
-
-
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic 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
-
-
-
-
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
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 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
ADC is the primary polyamine biosynthetic enzyme in the pathway
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
a fold III, pyridoxal 5'-phosphate-dependent enzyme
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required for activity
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
agmatine
-
-
guanidine
-
-
L-arginine methyl ester
-
-
L-arginineamide
-
-
L-argininic acid
-
-
L-canavanine
-
-
L-homoarginine
-
-
methylguanidine
-
-
N-benzylguanidine
-
-
n-propylguanidine
-
-
Ngamma-methyl-D-arginine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-Arg
-
pH 7.5, 37°C
0.233
L-canavanine
-
pH 7.5, 37°C
9.53
L-N5-(iminoethyl)-ornithine
-
pH 7.5, 37°C
0.163
Ngamma-methyl-L-arginine
-
pH 7.5, 37°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.46
L-Arg
-
pH 7.5, 37°C
0.11
L-canavanine
-
pH 7.5, 37°C
0.419
L-N5-(iminoethyl)-ornithine
-
pH 7.5, 37°C
1.22
Ngamma-methyl-L-arginine
-
pH 7.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.77
agmatine
-
pH 7.5, 37°C
0.0206
D-Arg
-
pH 7.5, 37°C
3.39
guanidine
-
pH 7.5, 37°C
0.897
L-argininamide
-
pH 7.5, 37°C
0.189
L-arginine methyl ester
-
pH 7.5, 37°C
0.327
L-argininic acid
-
pH 7.5, 37°C
0.427
L-canavanine
-
pH 7.5, 37°C
1.53
L-homoarginine
-
pH 7.5, 37°C
3.09
methylguanidine
-
pH 7.5, 37°C
1.4
N-benzylguanidine
-
pH 7.5, 37°C
1.93
n-propylguanidine
-
pH 7.5, 37°C
0.168
NG-methyl-D-arginine
-
pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene speA
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SPEA_YERPE
659
0
74104
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
163100
-
apo-ADC, light-scattering analysis
178000
-
holo-ADC, light-scattering analysis
74000
-
4 * 74000, crystal structure analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
in solution at pH 8.0, light-scattering analysis
tetramer
-
4 * 74000, crystal structure analysis
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the presence and absence of Mg2+ and pyridoxal 5’-phosphate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant protein using His-tag
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is an attractive target for drug design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Balbo, P.B.; Patel, C.N.; Sell, K.G.; Adcock, R.S.; Neelakantan, S.; Crooks, P.A.; Oliveira, M.A.
Spectrophotometric and steady-state kinetic analysis of the biosynthetic arginine decarboxylase of Yersinia pestis utilizing arginine analogues as inhibitors and alternative substrates
Biochemistry
42
15189-15196
2003
Yersinia pestis
Manually annotated by BRENDA team
Patel, C.N.; Adcock, R.S.; Sell, K.G.; Oliveira, M.A.
Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme
Acta Crystallogr. Sect. D
60
2396-2398
2004
Yersinia pestis
Manually annotated by BRENDA team
Counts, K.G.; Wong, I.; Oliveira, M.A.
Investigating the geminal diamine intermediate of Yersinia pestis arginine decarboxylase with substrate, product, and inhibitors using single wavelength stopped-flow spectroscopy
Biochemistry
46
379-386
2007
Yersinia pestis (Q8ZHG8), Yersinia pestis
Manually annotated by BRENDA team