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Information on EC 3.5.3.12 - agmatine deiminase
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EC Tree
3.5.3.12 agmatine deiminaseIUBMB Comments
The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.
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Word Map
- 3.5.3.12
- ornithine
-
biogenic
-
agdis
- n-carbamoylputrescine
- tyramine
- cremoris
- medicine
-
one-component
- hilgardii
-
cheeses
- drug development
- nutrition
- analysis
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
agmatine deiminase, agmatine iminohydrolase, agua1, agua2, putrescine synthase, agua protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AgD
AgDI
agmatine amidinohydrolase
agmatine deiminase
AguA
AguA1
aguA2
putrescine synthase
additional information
enzyme belongs to the family of C-N-hydrolases
agmatine amidinohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
agmatine + H2O = N-carbamoylputrescine + NH3
-
-
-
-
agmatine + H2O = N-carbamoylputrescine + NH3
the enzyme does not show activity of EC 2.1.3.3, ornithine carbamoyltransferase, EC 2.1.3.6, putrescine carbamoyltransferase, and EC 2.7.2.2, carbamate kinase, while putrescine synthase is a multifunctional enzyme, overview
-
agmatine + H2O = N-carbamoylputrescine + NH3
the plant enzyme also catalyzes the reactions of EC 2.1.3.3, ornithine carbamoyltransferase, EC 2.1.3.6, putrescine carbamoyltransferase, and EC 2.7.2.2, carbamate kinase, thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively, Cys180 and Cys366 are involved in catalysis but are not essential, residues are located in the substrate binding pocket
agmatine + H2O = N-carbamoylputrescine + NH3
like other GME hydrolases the enzyme possesses a high pKa active site Cys, suggesting that the enzyme employs a reverse protonation mechanism
-
agmatine + H2O = N-carbamoylputrescine + NH3
like other GME hydrolases the enzyme possesses a high pKa active site Cys, suggesting that the enzyme employs a reverse protonation mechanism
-
agmatine + H2O = N-carbamoylputrescine + NH3
like other GME hydrolases the enzyme possesses a high pKa active site Cys, suggesting that the enzyme employs a reverse protonation mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
C-N bond cleavage
hydrolysis of C-N bond of an amidino group
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
agmatine iminohydrolase
The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively.
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CAS REGISTRY NUMBER
COMMENTARY
37289-17-1
-
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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
agmatine + H2O
putrescine + ?
25 mM, assay at pH 6.5, 10 min, 40°C
-
-
?
N-carbamoylputrescine + phosphate
putrescine + carbamoyl phosphate
-
-
-
r
agmatine + H2O
N-carbamoylputrescine + NH3
highly specific for
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
Campylobacter jejuni subsp. jejuni serotype O:2
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
Campylobacter jejuni subsp. jejuni serotype O:2
the enzyme is involved in the biosynthesis of polyamines
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in the biosynthesis of polyamines
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
highly specific for agmatine
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in putrescine biosynthesis
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in putrescine biosynthesis
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
highly specific for agmatine
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
major products. Ammonia and N-carbamoylputrescine are produced in approximately equimolar amounts
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
aguBA operon induced by a promoter in the aguR-aguB intergenic region
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
sole substrate for AguA
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
Pseudomonas aeruginosa is an organism with high putrescine production activity compared to other microorganisms, overview
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
agmatine deiminase system (AgDS)
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
assay at pH 5.5 or pH 7.0
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
agmatine deiminase system (AgDS)
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
assay at pH 6.5, 28°C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + ornithine + H2O + phosphate
putrescine + citrulline + NH3 + phosphate
-
-
-
?
agmatine + ornithine + H2O + phosphate
putrescine + citrulline + NH3 + phosphate
-
-
-
?
agmatine + ornithine + H2O + phosphate
putrescine + citrulline + NH3 + phosphate
-
-
-
?
additional information
?
-
substrate specificity, no activity with guanidinoacetic acid, beta-guanidinopropionic acid, gamma-guanidinobutyric acid, L-arginine, L-citrulline, L-glutamine, L-ornithine, N-carbamoyl-beta-alanine, N-carbamoyl-D,L-aspartic acid, putrescine, spermidine, allylcyanide, beta-cyano-L-alanine, indole-3-acetonitrile, 3-phenylpropionitrile
-
-
?
additional information
?
-
-
substrate specificity, no activity with guanidinoacetic acid, beta-guanidinopropionic acid, gamma-guanidinobutyric acid, L-arginine, L-citrulline, L-glutamine, L-ornithine, N-carbamoyl-beta-alanine, N-carbamoyl-D,L-aspartic acid, putrescine, spermidine, allylcyanide, beta-cyano-L-alanine, indole-3-acetonitrile, 3-phenylpropionitrile
-
-
?
additional information
?
-
does not use L-arginine, L-argininamide, or arcaine (1,4-diguanidinobutane) as substrates
-
-
?
additional information
?
-
-
does not use L-arginine, L-argininamide, or arcaine (1,4-diguanidinobutane) as substrates
-
-
?
additional information
?
-
does not use L-arginine, L-argininamide, or arcaine (1,4-diguanidinobutane) as substrates
-
-
?
additional information
?
-
-
arginine, creatine and citrulline are no substrates
-
-
?
additional information
?
-
-
L-arginine does not act as the substrate for isoform AguA1. The recombinant isoform AguA2 shows no deiminase activity
-
-
?
additional information
?
-
-
L-arginine does not act as the substrate for isoform AguA1. The recombinant isoform AguA2 shows no deiminase activity
-
-
?
additional information
?
-
-
no activity with arginine, creatine, creatinine, guanidinoacetate, 3-guanidinopropionate and 4-guanidinobutytrate as substrates
-
-
?
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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
agmatine + H2O
N-carbamoylputrescine + NH3
Campylobacter jejuni subsp. jejuni serotype O:2
the enzyme is involved in the biosynthesis of polyamines
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in the biosynthesis of polyamines
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in putrescine biosynthesis
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the enzyme is involved in putrescine biosynthesis
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
Pseudomonas aeruginosa is an organism with high putrescine production activity compared to other microorganisms, overview
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
succinate
-
at concentration of 0.1 g/l and 1 g/l only about 2% less putrescine production
tyramine
-
at concentration of 0.1 g/l about 2% less putrescine production
additional information
-
no inhibitory effect on isoform AguA1 activity with Fe3+, Mg2+, and Ni2+
-
agmatine
-
AgDS-deficient strain is unable to grow in the presence of 20 mM agmatine, suggesting that AgDS converts a growth-inhibitory substance into products that can enhance acid tolerance
arginine
-
highest inhibitory effect with 10 g/l arginine, up to 80% less putrescine production
arginine
-
highest inhibitory effect with 10 g/l arginine, up to 83% less putrescine production
arginine
-
highest inhibitory effect with 10 g/l arginine, up to 75% less putrescine production
arginine
highest inhibitory effect with 10 g/l arginine, up to 68% less putrescine production
fructose
-
at concentration of 0.1 g/l about 18% less putrescine production, at concentration of 1 g/l about 60% less putrescine production
fructose
-
at concentration of 0.1 g/l about 5% less putrescine production, at concentration of 1 g/l about 30% less putrescine production
fructose
-
at concentration of 0.1 g/l about 5% less putrescine production, at concentration of 1 g/l about 75% less putrescine production
fructose
at concentration of 0.1 g/l about 60% less putrescine production, at concentration of 1 g/l 70% less putrescine production
glucose
-
at concentration of 0.1 g/l about 22% less putrescine production, at concentration of 1 g/l about 70% less putrescine production
glucose
-
at concentration of 0.1 g/l about 8% less putrescine production, at concentration of 1 g/l about 70% less putrescine production
glucose
-
at concentration of 0.1 g/l about 16% less putrescine production, at concentration of 1 g/l about 73% less putrescine production
glucose
at concentration of 0.1 g/l about 10% less putrescine production, at concentration of 1 g/l 19% less putrescine production
N,N'-diguanidinobutane
-
arcain, potential analogue of agmatine, 1 mM 50% inhibition
N-(4-aminobutyl)-2-chloro-ethanimidamide
i.e. ABCA , haloacetamidine-containing agmatine analogue
N-(4-aminobutyl)-2-fluoro-ethanimidamide
i.e. ABFA, haloacetamidine-containing agmatine analogue
N-(4-aminobutyl)-2-fluoroethanimidamide
-
inactivation proceeds via a multistep mechanism that requires general acid catalysis
N-(4-aminobutyl)-2-fluoroethanimidamide
-
inactivation proceeds via a multistep mechanism that requires general acid catalysis
N-(4-aminobutyl)-2-fluoroethanimidamide
-
inactivation proceeds via a multistep mechanism that requires general acid catalysis
spermidine
-
at concentration of 0.1 g/l about 10% less putrescine production, at concentration of 1 g/l about 20% less putrescine production
spermidine
-
at concentration of 0.1 g/l about 18% less putrescine production, at concentration of 1 g/l about 25% less putrescine production
spermidine
-
at concentration of 0.1 g/l about 5% less putrescine production, at concentration of 1 g/l about 23% less putrescine production
spermine
-
at concentration of 0.1 g/l about 10% less putrescine production, at concentration of 1 g/l about 20% less putrescine production
spermine
-
at concentration of 0.1 g/l about 5% less putrescine production, at concentration of 1 g/l about 25% less putrescine production
spermine
-
at concentration of 0.1 g/l about 20% less putrescine production, at concentration of 1 g/l about 25% less putrescine production
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermidine
at concentration of 0.1 g/l about 10% more putrescine production, at concentration of 1 g/l 32% more putrescine production
spermine
at concentration of 0.1 g/l about 2% more putrescine production, at concentration of 1 g/l 23% more putrescine production
histamine
-
at concentration of 0.1 g/l about 2% more putrescine production, at concentration of 1 g/l about 5% more putrescine production
histamine
at concentration of 0.1 g/l and 1.0 g/l about 10% more putrescine production
succinate
at concentration of 0.1 g/l about 15% more putrescine production, at concentration of 1 g/l about 35% more putrescine production
tyramine
-
at concentration of 1 g/l about 2% more putrescine production
tyramine
at concentration of 0.1 g/l about 15% more putrescine production, at concentration of 1 g/l 20% more putrescine production
additional information
-
ornithine, D-lactic acid, citric acid, L-malic acid, and DL-malic acid do not modify activity
-
additional information
-
diverse polyamines and sugars increased putrescine production, e.g. succinic acid increases putrescine production, but does not alter agmatine deimination, overview
-
additional information
diverse polyamines and sugars increased putrescine production, e.g. succinic acid increases putrescine production, but does not alter agmatine deimination, overview
-
additional information
-
2fold higher expression of aguB in presence of 10 mM agmatine, 2fold higher activity at pH 5.5
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Structural and Functional Basis for Targeting Campylobacter jejuni Agmatine Deiminase To Overcome Antibiotic Resistance.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001285
N-alpha-benzoyl-L-arginine amide
mutant D198A, pH 8.0, 37°C
0.0000847
N-alpha-benzoyl-L-arginine ethyl ester
wild-type, pH 8.0, 37°C
0.0001383
N-alpha-benzoyl-L-arginine ethyl ester
mutant D198A, pH 8.0, 37°C
0.0001038
N-alpha-benzoyl-L-arginine methyl ester
wild-type, pH 8.0, 37°C
0.0002183
N-alpha-benzoyl-L-arginine methyl ester
mutant D198A, pH 8.0, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00087
N-(4-aminobutyl)-2-chloro-ethanimidamide
Helicobacter pylori
wild-type, pH 8.0, 37°C
0.0785
N-(4-aminobutyl)-2-chloro-ethanimidamide
Listeria monocytogenes serotype 1/2a
pH 7.5, 25°C
0.0068
N-(4-aminobutyl)-2-fluoro-ethanimidamide
Helicobacter pylori
wild-type, pH 8.0, 37°C
0.146
N-(4-aminobutyl)-2-fluoro-ethanimidamide
Listeria monocytogenes serotype 1/2a
pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.015
0.058
additional information
0.015
-
enzyme activity of shoots grown for 7 days at 25°C in the dark and light respectively
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
additional information
-
assay at pH 6.0, 30 min, reaction stopped by 10% trichloroacetic acid
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
AgD induction clearly enhanced at low pH values, aguA ca. 3.7fold higher in cells grown at pH 5 than that grown at pH 7, stress response pathway of this organism
5.5 - 9.5
pH 5.5: about 60% of maximal activity, pH 9.5: about 65% of maximal activity
6 - 7
-
activity rapidly declining below pH 6.0 and declining less rapidly above pH 7.0
6.5 - 8
-
89% of maximal activity at pH 6.5, 91% of maximal activity at pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 40
-
AgD activity 4fold higher in Streptococcus mutans grown at 42°C than at 37°C, stress response pathway of this organism
5 - 35
-
about 65% activity at 5°C, about 90% activity at 15°C, 100% activity at 25°C, less than 40% activity at 35°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phycobiont/mycobiont, enzyme localized in the mycobiont, growing on Quercus pyrenaica
-
-
brenda
formerly Lactococcus lactis subsp. cremoris GE2-14
UniProt
brenda
Lactobacillus sakei 23K is unable to produce putrescine since no putrescine carbamoyltransferase can be amplified
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform Agu2A' contains a twin-arginine translocation signal at its N-terminus and is secreted to the periplasm
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
deletion of aguA1 significantly impairs Listeria monocytogenes survival both in gastric fluid at pH 2.5 and in mouse stomach
malfunction
-
deletion of aguA1 significantly impairs Listeria monocytogenes survival both in gastric fluid at pH 2.5 and in mouse stomach
-
metabolism
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
metabolism
Campylobacter jejuni subsp. jejuni serotype O:2
the enzyme is involved in the biosynthesis of polyamines
metabolism
-
the enzyme is involved in the biosynthesis of polyamines
-
metabolism
-
the ability of Listeria monocytogenes to survive in extreme environments (i.e. low temperatures and pH) may arise, at least in part, from agmatine catabolism via the agmatine deiminase system. This catabolic pathway utilizes an agmatine deiminase to hydrolyse agmatine into N-carbamoylputrescine, with concomitant release of ammonia, which increases the pH, thus mitigating the ill effects of the acidic environment
-
physiological function
deletion of the agmatine operon agu2ABCA' reduces biofilm production of strain PA14 following addition of exogenous agmatine
physiological function
deletion of the agmatine operon agu2ABCA', specifically its secreted product Agu2A', reduces biofilm production of strain PA14 following addition of exogenous agmatine
physiological function
putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium
physiological function
-
the enzyme is involved in Listeria acid tolerance and contributes to the enhanced adaption to acidic conditions in the host gastrointestinal tract
physiological function
-
the enzyme mediates acid tolerance in Listeria monocytogenes
physiological function
-
the enzyme mediates acid tolerance in Listeria monocytogenes
-
physiological function
Lactococcus cremoris CECT 8666
-
putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium
-
Show AA Sequence and Transmembrane Helices (6166 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
183000
36000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
39900
x * 39900, calculated for mature protein
43000
44000
45000
47000
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
85000
43000
2 * 43000, recombinant His-tagged wild-type enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
additional information
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
dimer
2 * 43000, recombinant His-tagged wild-type enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
cleavage of translocation signal
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of both the unliganded wild-type enzyme and a catalytic mutant of agmatine deiminase with the substrate, agamatine, bound
Campylobacter jejuni subsp. jejuni serotype O:2
hanging drop vapour diffusion method with in 50 mM Tris-HCl, pH 7.45, 1 mM dithiothreitol and 20 mM NaCl
to 2.1 A resolution. Residue D198 is the key residue for agmatine recognition
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C180A
site-directed mutagenesis, conserved catalytically relevant Cys, 35% of wild-type activity, inhibition with iodoacetamide is easier abolished by substrate agmatine
C366A
site-directed mutagenesis, conserved catalytically relevant Cys, 15% of wild-type activity, inhibition with iodoacetamide is easier abolished by substrate agmatine
C315S
C157G
-
the mutant of inactive isoform AguA2 shows wild type enzyme activity
R3G/R4S
mutation of the twin-arginine translocation tat-sequence at the N-terminus. Mutant is hardly secreted to periplasm
additional information
additional information
strain PAO5001, a knockout mutation of Gene PAO0292
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 6
-
agmatine is degraded in a very limited extent when the pH values are close to 2.5, a diminution of activity is observed at pH values above 6.0, at pH values from 3.2 to 3.8, the amount of putrescine formed is 53% and 75% respectively of the maximum amount formed at pH 4.5
687349
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
55
-
retains 44% activity when exposed for 10 min, completely inactivated at 60°C under the same conditions
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable even in presence of glycerol, dithiothreitol and Mg2+, freeze-thawing and dialysis lead to considerable loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, purified enzyme lost 30% of the activity in 3 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme purified from shoots grown in the dark by DE52 column chromatography, Sephadex G-100 column chromatography and agmatine-epoxy-Sepharose 6B column chromatography
-
HisTrap Ni-affinity column chromatography and Superdex 200 HR gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by Ni2+-chelate affinity chromatography
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
-
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
-
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression as C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
expression in Escherichia coli
expression of the wild-type enzyme and the C315S mutant enzyme in Escherichia coli BL21 (DE3)
Campylobacter jejuni subsp. jejuni serotype O:2
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is transcriptionally activated by AguR
expression is 9fold increased in the presence of tyrosine
induction of the agmatine deiminase system requires agmatine and is optimal at low pH. The VicRK, ComDE, and CiaRH two-component systems influence agmatine deiminase system gene expression in response to acidic and thermal stresses
-
presence of an alternate agmatine operon in the Pseudomonas aeruginosa strain PA14 named agu2ABCA that contains two genes for agmatine deiminases, agu2A and agu2A'. This operon is present in 25% of clinical Pseudomonas aeruginosa isolates. Agmatine induces expression of the operon during the stationary phase of growth and during biofilm growth and agu2ABCA' provides only weak complementation of aguBA, which is induced during log phase
presence of an alternate agmatine operon in the Pseudomonas aeruginosa strain PA14 named agu2ABCA' that contains two genes for agmatine deiminases, agu2A and agu2A'. This operon is present in 25% of clinical Pseudomonas aeruginosa isolates. Agmatine induces expression of the operon during the stationary phase of growth and during biofilm growth and agu2ABCA' provides only weak complementation of aguBA, which is induced during log phase
repressed by carbon source
transcription is significantly induced at pH 5.0
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a multiplex PCR method for the simultaneous detection of four genes involved in the production of histamine, i.e. histidine decarboxylase hdc, tyramine, i.e.tyrosine decarboxylase tyrdc, and putrescine, via either ornithine decarboxylase odc, or agmatine deiminase agdi. A collection of 810 lactic acid bacteria strains isolated from wine and cider was screened. The most frequent gene corresponds to the agdi gene detected in 112 strains, 14% of all lactic acid bacteria strains, of 10 different lactic acid bacteria species
drug development
food industry
-
development of a multiplex PCR method for the simultaneous detection of four genes involved in the production of histamine, i.e. histidine decarboxylase hdc, tyramine, i.e.tyrosine decarboxylase tyrdc, and putrescine, via either ornithine decarboxylase odc, or agmatine deiminase agdi. A collection of 810 lactic acid bacteria strains isolated from wine and cider was screened. The most frequent gene corresponds to the agdi gene detected in 112 strains, 14% of all lactic acid bacteria strains, of 10 different lactic acid bacteria species
medicine
nutrition
drug development
Campylobacter jejuni subsp. jejuni serotype O:2
Campylobacter jejuni agmatine deiminase is a potentially important target for combatting antibiotic resistance
drug development
-
Campylobacter jejuni agmatine deiminase is a potentially important target for combatting antibiotic resistance
-
medicine
-
developing of an analytic method for agmatine, being an important reagent for medical research
medicine
-
developing of an analytic method for agmatine, being an important reagent for medical research
-
nutrition
-
developing of an analytic method for agmatine, being an important reagent for food research
nutrition
-
developing of an analytic method for agmatine, being an important reagent for food research
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Le Rudulier, D.; Goas, G.
Biogenese de la N-carbamylputrescine et de la putrescine dans les plantules de Glycine max (L.) Merr
Physiol. Veg.
18
609-616
1980
Glycine max, Zea mays
-
brenda
Smith, T.A.
Agmatine iminohydrolase in maize
Phytochemistry
8
2111-2117
1969
Avena sativa, Brassica oleracea, Helianthus annuus, Hordeum vulgare, no activity in Malus sylvestris, no activity in Pisum sativum, no activity in Secale cereale, no activity in Triticum aestivum, Zea mays
-
brenda
Sindhu, R.K.; Desai, H.V.
Purification and properties of agmatine iminohydrolase from groundnut cotyledons
Phytochemistry
18
1937-1938
1979
Arachis hypogaea, Escherichia coli, Helianthus annuus, Zea mays
-
brenda
Yanagisawa, H.; Suzuki, Y.
Corn agmatine iminohydrolase. Purification and properties
Plant Physiol.
67
697-700
1981
Arachis hypogaea, Helianthus annuus, Zea mays
brenda
Srivenugopal, K.S.; Adiga, P.R.
Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)
J. Biol. Chem.
256
9532-9541
1981
Lathyrus sativus
brenda
Simon, J.P.; Stalon, V.
Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis
J. Bacteriol.
11
676-681
1982
Enterococcus faecalis
-
brenda
Legaz, M.E.; Iglesias, A.; Vicente, C.
Regulation of agmatine iminohydrolase of Evernia prunastri by L-arginine metabolites
Z. Pflanzenphysiol.
110
53-59
1983
Evernia prunastri, Glycine max, Hordeum vulgare, Lathyrus sativus, Soja hispida, Zea mays
-
brenda
Chaudhuri, M.M.; Ghosh, B.
Agmatine deiminase in rice seedlings
Phytochemistry
24
2433-2435
1985
Arachis hypogaea, Helianthus annuus, Hordeum vulgare, Nicotiana tabacum, Oryza sativa, Zea mays
-
brenda
Prasad, G.L.; Adiga, P.R.
Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis
J. Biosci.
10
373-391
1986
Cucumis sativus, Lathyrus sativus
-
brenda
Park, K.H.; Cho, Y.D.
Purification of monomeric agmatine iminohydrolase from soybean
Biochem. Biophys. Res. Commun.
174
32-36
1991
Glycine max, Oryza sativa, Zea mays
brenda
Shoeb, S.M.; Shimizu, E.; Yorifuji, T.
Differential enzymatic measurement of agmatine, putrescine, and diguanidinobutane
Biosci. Biotechnol. Biochem.
60
69-72
1996
Rhodococcus sp., Rhodococcus sp. C-x
-
brenda
Nakada, Y.; Itoh, Y.
Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway
Microbiology
149
707-714
2003
Pseudomonas aeruginosa
brenda
Janowitz, T.; Kneifel, H.; Piotrowski, M.
Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants
FEBS Lett.
544
258-261
2003
Arabidopsis thaliana (Q8GWW7), Arabidopsis thaliana
brenda
Sakakibara, Y.; Yanagisawa, H.
Agmatine deiminase from cucumber seedlings is a mono-specific enzyme: purification and characteristics
Protein Expr. Purif.
30
88-93
2003
Cucumis sativus
brenda
Nakada, Y.; Jiang, Y.; Nishijyo, T.; Itoh, Y.; Lu, C.D.
Molecular characterization and regulation of the aguBA operon, responsible for agmatine utilization in Pseudomonas aeruginosa PAO1
J. Bacteriol.
183
6517-6524
2001
Pseudomonas aeruginosa (Q9I6J9)
brenda
Griswold, A.R.; Jameson-Lee, M.; Burne, R.A.
Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159
J. Bacteriol.
188
834-841
2006
Streptococcus mutans, Streptococcus mutans UA159
brenda
Yanagisawa, H.
Agmatine deiminase from maize shoots: purification and properties
Phytochemistry
56
643-647
2001
Zea mays
brenda
Llacer, J.L.; Polo, L.M.; Tavarez, S.; Alarcon, B.; Hilario, R.; Rubio, V.
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction
J. Bacteriol.
189
1254-1265
2007
Enterococcus faecalis (Q837U5), Enterococcus faecalis, Enterococcus faecalis ATCC 700802 (Q837U5)
brenda
Liao, S.; Poonpairoj, P.; Ko, K.; Takatuska, Y.; Yamaguchi, Y.; Abe, N.; Kaneko, J.; Kamio, Y.
Occurrence of agmatine pathway for putrescine synthesis in Selenomonas ruminatium
Biosci. Biotechnol. Biochem.
72
445-455
2008
Selenomonas ruminantium (Q5KR05), Selenomonas ruminantium
brenda
Arena, M.E.; Landete, J.M.; Manca de Nadra, M.C.; Pardo, I.; Ferrer, S.
Factors affecting the production of putrescine from agmatine by Lactobacillus hilgardii XB isolated from wine
J. Appl. Microbiol.
105
158-165
2008
Lentilactobacillus hilgardii, Lentilactobacillus hilgardii XB
brenda
Landete, J.M.; Arena, M.E.; Pardo, I.; Manca de Nadra, M.C.; Ferrer, S.
Comparative survey of putrescine production from agmatine deamination in different bacteria
Food Microbiol.
25
882-887
2008
Bacillus cereus, Enterococcus faecalis, Lentilactobacillus hilgardii, Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9I6J9), Bacillus cereus CECT 148, Enterococcus faecalis ATCC 11700, Lentilactobacillus hilgardii X1B
brenda
Liu, Y.; Zeng, L.; Burne, R.A.
AguR is required for induction of the Streptococcus mutans agmatine deiminase system by low pH and agmatine
Appl. Environ. Microbiol.
75
2629-2637
2009
Streptococcus mutans
brenda
Griswold, A.R.; Nascimento, M.M.; Burne, R.A.
Distribution, regulation and role of the agmatine deiminase system in mutans streptococci
Oral Microbiol. Immunol.
24
79-82
2009
Streptococcus mutans, Streptococcus oralis, Streptococcus ratti, Streptococcus salivarius, Streptococcus sanguinis, Streptococcus sobrinus, Streptococcus criceti, Streptococcus downei, no activity in Streptococcus sanguinis, no activity in Streptococcus gordonii, Streptococcus criceti AHT, Streptococcus sobrinus 6715, Streptococcus downei 33748
brenda
Jones, J.E.; Causey, C.P.; Lovelace, L.; Knuckley, B.; Flick, H.; Lebioda, L.; Thompson, P.R.
Characterization and inactivation of an agmatine deiminase from Helicobacter pylori
Bioorg. Chem.
38
62-73
2010
Helicobacter pylori (Q9ZN18), Helicobacter pylori
brenda
Coton, M.; Romano, A.; Spano, G.; Ziegler, K.; Vetrana, C.; Desmarais, C.; Lonvaud-Funel, A.; Lucas, P.; Coton, E.
Occurrence of biogenic amine-forming lactic acid bacteria in wine and cider
Food Microbiol.
27
1078-1085
2010
Bacteria
brenda
Liu, Y.; Burne, R.A.
Multiple two-component systems of Streptococcus mutans regulate agmatine deiminase gene expression and stress tolerance
J. Bacteriol.
191
7363-7366
2009
Streptococcus mutans
brenda
Williams, B.J.; Du, R.H.; Calcutt, M.W.; Abdolrasulnia, R.; Christman, B.W.; Blackwell, T.S.
Discovery of an operon that participates in agmatine metabolism and regulates biofilm formation in Pseudomonas aeruginosa
Mol. Microbiol.
76
104-119
2010
Pseudomonas aeruginosa PA14 (A0A0H2Z743), Pseudomonas aeruginosa PA14 (A0A0H2Z8C6)
brenda
Jones, J.E.; Dreyton, C.J.; Flick, H.; Causey, C.P.; Thompson, P.R.
Mechanistic studies of agmatine deiminase from multiple bacterial species
Biochemistry
49
9413-9423
2010
Porphyromonas gingivalis, Helicobacter pylori, Streptococcus mutans
brenda
Landete, J.M.; Arena, M.E.; Pardo, I.; Manca de Nadra, M.C.; Ferrer, S.
The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase
Int. Microbiol.
13
169-177
2010
Bacillus cereus, Enterococcus faecalis, Lentilactobacillus hilgardii, Latilactobacillus sakei, Pseudomonas aeruginosa, Bacillus cereus ATCC 14579, Enterococcus faecalis ATCC 11700, Lentilactobacillus hilgardii X1B
brenda
del Rio, B.; Linares, D.M.; Ladero, V.; Redruello, B.; Fernandez, M.; Martin, M.C.; Alvarez, M.A.
Putrescine production via the agmatine deiminase pathway increases the growth of Lactococcus lactis and causes the alkalinization of the culture medium
Appl. Microbiol. Biotechnol.
99
897-905
2015
Lactococcus cremoris (S0F349), Lactococcus cremoris CECT 8666 (S0F349)
brenda
Marchenko, M.; Thomson, A.; Ellis, T.N.; Knuckley, B.; Causey, C.P.
Development of a clickable activity-based protein profiling (ABPP) probe for agmatine deiminases
Bioorg. Med. Chem.
23
2159-2167
2015
Streptococcus mutans, Streptococcus mutans UA159
brenda
Cheng, C.; Chen, J.; Fang, C.; Xia, Y.; Shan, Y.; Liu, Y.; Wen, G.; Song, H.; Fang, W.
Listeria monocytogenes aguA1, but not aguA2, encodes a functional agmatine deiminase: biochemical characterization of its catalytic properties and roles in acid tolerance
J. Biol. Chem.
288
26606-26615
2013
Listeria monocytogenes, Listeria monocytogenes 10403S
brenda
Chen, J.; Chen, F.; Cheng, C.; Fang, W.
Prevalence of the lmo0036-0043 gene cluster encoding arginine deiminase and agmatine deiminase systems in Listeria monocytogenes
New Microbiol.
36
187-192
2013
Listeria monocytogenes
brenda
Suarez, C.; Espariz, M.; Blancato, V.S.; Magni, C.
Expression of the agmatine deiminase pathway in Enterococcus faecalis is activated by the AguR regulator and repressed by CcpA and PTS(Man) systems
PLoS ONE
8
e76170
2013
Enterococcus faecalis, Enterococcus faecalis JH2-2
brenda
Perez, M.; Ladero, V.; Del Rio, B.; Redruello, B.; de Jong, A.; Kuipers, O.; Kok, J.; Martin, M.C.; Fernandez, M.; Alvarez, M.A.
The relationship among tyrosine decarboxylase and agmatine deiminase pathways in Enterococcus faecalis
Front. Microbiol.
8
2107
2017
Enterococcus faecalis (Q837U5), Enterococcus faecalis ATCC 700802 (Q837U5)
brenda
Soares, C.A.; Knuckley, B.
Mechanistic studies of the agmatine deiminase from Listeria monocytogenes
Biochem. J.
473
1553-1561
2016
Listeria monocytogenes serotype 1/2a (A0A0H3G8U9), Listeria monocytogenes serotype 1/2a 10403S (A0A0H3G8U9)
brenda
Shek, R.; Dattmore, D.A.; Stives, D.P.; Jackson, A.L.; Chatfield, C.H.; Hicks, K.A.; French, J.B.
Structural and functional basis for targeting Campylobacter jejuni agmatine deiminase to overcome antibiotic resistance
Biochemistry
56
6734-6742
2017
Campylobacter jejuni subsp. jejuni serotype O:2 (Q0P9V0), Campylobacter jejuni subsp. jejuni serotype O:2 ATCC 700819 (Q0P9V0)
brenda
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