Information on EC 3.5.3.12 - agmatine deiminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.5.3.12
-
RECOMMENDED NAME
GeneOntology No.
agmatine deiminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
agmatine + H2O = N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
agmatine + H2O = N-carbamoylputrescine + NH3
show the reaction diagram
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
Q8GWW7
agmatine + H2O = N-carbamoylputrescine + NH3
show the reaction diagram
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
show the reaction diagram
like other GME hydrolases the enzyme possesses a high pKa active site Cys, suggesting that the enzyme employs a reverse protonation mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
C-N bond cleavage
Q8GWW7
-
C-N bond cleavage
-
-
hydrolysis
-
involved in agmatine deiminase system
hydrolysis of C-N bond of an amidino group
Q8GWW7
-
hydrolysis of C-N bond of an amidino group
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway)
-
Metabolic pathways
-
putrescine biosynthesis II
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AgDI
Enterococcus faecalis ATCC 11700
-
-
-
AgDI
Enterococcus faecalis SD10
Q837U5
-
-
AgDI
Lactobacillus hilgardii X1B
-
-
-
agmatine amidinohydrolase
-
-
-
-
agmatine amidinohydrolase
-
-
agmatine deiminase
Q8GWW7
-
agmatine deiminase
-
-
agmatine deiminase
Bacillus cereus ATCC 14579, Bacillus cereus CECT 148
-
-
-
agmatine deiminase
-
-
agmatine deiminase
-
-
agmatine deiminase
Enterococcus faecalis ATCC 11700, Enterococcus faecalis ATCC11700
-
-
-
agmatine deiminase
-
-
agmatine deiminase
Lactobacillus hilgardii X1B
-
;
-
agmatine deiminase
-
-
agmatine deiminase
-
-
agmatine deiminase
Q5KR05
-
agmatine deiminase
-
-
agmatine deiminase
Streptococcus criceti AHT
-
-
-
agmatine deiminase
-
-
agmatine deiminase
Streptococcus downei 33748
-
-
-
agmatine deiminase
-
-
agmatine deiminase
-
-
-
agmatine deiminaseHpAgD
-
-
agmatine iminohydrolase
-
-
agu2A
Q02J61, Q02J64
-
AguA
-
gene name
AguA
-
gene name
-
AguA
-
gene name
AguA
Enterococcus faecalis ATCC 11700
-
gene name
-
AguA
-
gene name
AguA
Lactobacillus hilgardii X1B
-
gene name
-
AguA
-
gene name
AguA
-
gene name
aguA protein
-
-
aguA2
-
gene name
aguA2
Lactobacillus hilgardii X1B
-
gene name
-
putrescine synthase
-
-
putrescine synthase
-
-
additional information
Q8GWW7
enzyme belongs to the family of C-N-hydrolases
CAS REGISTRY NUMBER
COMMENTARY
37289-17-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene At5g08170
GenBank
Manually annotated by BRENDA team
gene T22D6
GenBank
Manually annotated by BRENDA team
groundnut, L. cv Punjab-1
-
-
Manually annotated by BRENDA team
oat, L. var. Black Supreme
-
-
Manually annotated by BRENDA team
strain CECT 148
-
-
Manually annotated by BRENDA team
Bacillus cereus CECT 148
strain CECT 148
-
-
Manually annotated by BRENDA team
brussels sprouts, var. gemmifera Zenker; cabbage, L. var. capitata L.
-
-
Manually annotated by BRENDA team
gene Cj0949c
SwissProt
Manually annotated by BRENDA team
gene CC0211
SwissProt
Manually annotated by BRENDA team
PBCV-1, gene A638R
SwissProt
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
cv. Tokiwajibae
-
-
Manually annotated by BRENDA team
ATCC 11700
-
-
Manually annotated by BRENDA team
strain ATCC11700
-
-
Manually annotated by BRENDA team
strain SD10
SwissProt
Manually annotated by BRENDA team
Enterococcus faecalis ATCC 11700
-
-
-
Manually annotated by BRENDA team
Enterococcus faecalis ATCC11700
strain ATCC11700
-
-
Manually annotated by BRENDA team
Enterococcus faecalis SD10
strain SD10
SwissProt
Manually annotated by BRENDA team
phycobiont/mycobiont, enzyme localized in the mycobiont, growing on Quercus pyrenaica
-
-
Manually annotated by BRENDA team
soybean, L.
-
-
Manually annotated by BRENDA team
sunflower, L. var. Sutton's giant yellow
-
-
Manually annotated by BRENDA team
gene HP0049
-
-
Manually annotated by BRENDA team
barley, L. var. zephyr
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii X1B
-
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii X1B
strain X1B
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii XB
strain XB
-
-
Manually annotated by BRENDA team
Lactobacillus sakei 23K is unable to produce putrescine since no putrescine carbamoyltransferase can be amplified
-
-
Manually annotated by BRENDA team
gene YrfC
SwissProt
Manually annotated by BRENDA team
no activity in Malus sylvestris
apple, Mill. var. Lord lambourne
-
-
Manually annotated by BRENDA team
no activity in Pisum sativum
pea, L. var. Meteor
-
-
Manually annotated by BRENDA team
no activity in Secale cereale
rye, L.
-
-
Manually annotated by BRENDA team
no activity in Streptococcus gordonii
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus sanguinis
genospecies 1
-
-
Manually annotated by BRENDA team
no activity in Triticum aestivum
wheat, var. Atle
-
-
Manually annotated by BRENDA team
rice
-
-
Manually annotated by BRENDA team
strain PAO1, CECT 4122
UniProt
Manually annotated by BRENDA team
isoform agu2A
UniProt
Manually annotated by BRENDA team
isoform agu2A'
UniProt
Manually annotated by BRENDA team
Rhodococcus sp. C-x
C-x
-
-
Manually annotated by BRENDA team
Soja hispida
-
-
-
Manually annotated by BRENDA team
strain AHT
-
-
Manually annotated by BRENDA team
Streptococcus criceti AHT
strain AHT
-
-
Manually annotated by BRENDA team
strain 33748
-
-
Manually annotated by BRENDA team
Streptococcus downei 33748
strain 33748
-
-
Manually annotated by BRENDA team
strain UA159
-
-
Manually annotated by BRENDA team
strain UA159 and strain GS-5
-
-
Manually annotated by BRENDA team
strain UA159, strain WTZ as construt of lacZ
-
-
Manually annotated by BRENDA team
strain FA-1 and strain BHT
-
-
Manually annotated by BRENDA team
genospecies 2
-
-
Manually annotated by BRENDA team
strain 6715
-
-
Manually annotated by BRENDA team
gene SCC2.08
SwissProt
Manually annotated by BRENDA team
gene XF2442
SwissProt
Manually annotated by BRENDA team
corn, L. variety Hy2x07
-
-
Manually annotated by BRENDA team
L. cv Goldencross Bantam T51
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q02J61, Q02J64
deletion of the agmatine operon agu2ABCA' reduces biofilm production of strain PA14 following addition of exogenous agmatine; deletion of the agmatine operon agu2ABCA', specifically its secreted product Agu2A', reduces biofilm production of strain PA14 following addition of exogenous agmatine
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-SGRGK + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
agmatine + ADP + phosphate
ATP + putrescine + NH3 + CO2
show the reaction diagram
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Soja hispida, Evernia prunastri
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
ir
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Q9I6J9
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Q02J61, Q02J64
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-, Q9ZN18
-
major products. Ammonia and N-carbamoylputrescine are produced in approximately equimolar amounts
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-, Q8GWW7
highly specific for
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
agmatine deiminase system (AgDS)
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
aguBA operon induced by a promoter in the aguR-aguB intergenic region
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
sole substrate for AguA
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-, Q837U5
highly specific for agmatine
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Q9I6J9
Pseudomonas aeruginosa is an organism with high putrescine production activity compared to other microorganisms, overview
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
assay at pH 5.5 or pH 7.0
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Enterococcus faecalis SD10
Q837U5
highly specific for agmatine
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Rhodococcus sp. C-x
-
-, multifunctional enzyme, acts also as putrescine transcarbamylase, putrescine synthase, ornithine transcarbamylase and carbamate kinase
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
agmatine deiminase system (AgDS)
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Lactobacillus hilgardii XB
-
-
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Q9I6J9
assay at pH 6.5, 28C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
-
assay at pH 6.5, 28C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Streptococcus criceti AHT
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Bacillus cereus CECT 148
-
assay at pH 6.5, 28C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Enterococcus faecalis ATCC11700
-
assay at pH 6.5, 28C, 8 h
-
-
ir
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Streptococcus downei 33748
-
assay at pH 6.0, 30 min, reaction terminated by adding 10% trichloracetic acid
-
-
?
agmatine + H2O
NH3 + N-carbamoylputrescine
show the reaction diagram
Lactobacillus hilgardii X1B
-
assay at pH 6.5, 28C, 8 h
-
-
ir
agmatine + H2O
putrescine + ?
show the reaction diagram
Q5KR05, -
25 mM, assay at pH 6.5, 10 min, 40C
-
-
?
agmatine + ornithine + H2O + phosphate
putrescine + citrulline + NH3 + phosphate
show the reaction diagram
-
-
-
?
agmatine + ornithine + H2O + phosphate
putrescine + citrulline + NH3 + phosphate
show the reaction diagram
-
-
-
?
carbamoyl phosphate + ADP + H2O
ATP + CO2 + NH3
show the reaction diagram
-
-
-
r
carbamoyl phosphate + ornithine
citrulline + phosphate
show the reaction diagram
-
-
-
r
guanidine + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
N-alpha-benzoyl-L-arginine amide + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
N-alpha-benzoyl-L-arginine ethyl ester + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
N-alpha-benzoyl-L-arginine methyl ester + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
N-carbamoylputrescine + phosphate
putrescine + carbamoyl phosphate
show the reaction diagram
-
-
-
r
streptomycin + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
L-arginine + H2O
? + NH3
show the reaction diagram
-, Q9ZN18
-
-
-
?
additional information
?
-
-
arginine, creatine and citrulline are no substrates
-
-
-
additional information
?
-
-, Q8GWW7
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
?
-
-
no activity with arginine, creatine, creatinine, guanidinoacetate, 3-guanidinopropionate and 4-guanidinobutytrate as substrates
-
-
-
additional information
?
-
-, Q837U5
does not use L-arginine, L-argininamide, or arcaine (1,4-diguanidinobutane) as substrates
-
-
-
additional information
?
-
Enterococcus faecalis SD10
Q837U5
does not use L-arginine, L-argininamide, or arcaine (1,4-diguanidinobutane) as substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Soja hispida, Evernia prunastri
-
-
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Q9I6J9
Pseudomonas aeruginosa is an organism with high putrescine production activity compared to other microorganisms, overview
-
-
?
agmatine + H2O
N-carbamoylputrescine + NH3
show the reaction diagram
Rhodococcus sp. C-x
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8-Azaguanine
-
-
agmatine
-
above 8 mM slight substrate inhibition
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
arcaine
-
agmatine analogue, strong competitive inhibition
arcaine
-
competitive inhibitor
arcaine
-, Q837U5
competitive inhibitor
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
Q9I6J9
highest inhibitory effect with 10 g/l arginine, up to 68% less putrescine production
cadaverine
-
competitive inhibition
carbohydrate
-
-
-
cationic mercury
-
enzyme 90% inhibited at 0.1 mM
Co2+
-
1 mM 55% inhibition
Cu2+
-
1 mM 100% inhibition
cycloheximide
-
-
Fe2+
-
-
-
Fe2+
Q5KR05, -
1 mM
-
Fe3+
Q5KR05, -
1 mM
-
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
Q9I6J9
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
Q9I6J9
at concentration of 0.1 g/l about 10% less putrescine production, at concentration of 1 g/l 19% less putrescine production
Hg2+
Q5KR05, -
strong inhibitor
iodoacetamide
-
-
iodoacetamide
Q8GWW7
about 70% inhibition at 2 mM, wild-type enzyme
iodoacetamide
Q5KR05, -
strong inhibitor
iodoacetoamide
-
enzyme 95% inhibited at 0.1 mM
L-arginine
-
high concentration
N,N'-diguanidinobutane
-
arcain, potential analogue of agmatine, 1 mM 50% inhibition
N,N'-diguanidinobutane
-
-
N-(4-aminobutyl)-2-chloro-ethanimidamide
-, Q9ZN18
i.e. ABCA , haloacetamidine-containing agmatine analogue
-
N-(4-aminobutyl)-2-chloroethanimidamide
-
-
-
N-(4-aminobutyl)-2-fluoro-ethanimidamide
-, Q9ZN18
i.e. ABFA, haloacetamidine-containing agmatine analogue
-
N-(4-aminobutyl)-2-fluoroethanimidamide
-
inactivation proceeds via a multistep mechanism that requires general acid catalysis
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
enzyme 12% inhibited at 0.1 mM
Semicarbazide
-
-
Semicarbazide
-
-
spermidine
-
competitive inhibition
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
-
10 mM, 50% inhibition
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
succinate
-
at concentration of 0.1 g/l and 1 g/l only about 2% less putrescine production
tryptamine
-
2.5 mM, 50% inhibition
tyramine
-
at concentration of 0.1 g/l about 2% less putrescine production
Zn2+
-
1 mM 85% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
Q9I6J9
at concentration of 0.1 g/l and 1.0 g/l about 10% more putrescine production
spermidine
Q9I6J9
at concentration of 0.1 g/l about 10% more putrescine production, at concentration of 1 g/l 32% more putrescine production
spermine
Q9I6J9
at concentration of 0.1 g/l about 2% more putrescine production, at concentration of 1 g/l 23% more putrescine production
succinate
-
at concentration of 1 g/l about 5% more putrescine production
succinate
Q9I6J9
at concentration of 0.1 g/l about 15% more putrescine production, at concentration of 1 g/l about 35% more putrescine production
tartaric acid
-
shows a stimulatory effect on activity
tyramine
-
at concentration of 1 g/l about 2% more putrescine production
tyramine
Q9I6J9
at concentration of 0.1 g/l about 15% more putrescine production, at concentration of 1 g/l 20% more putrescine production
L-lactic acid
-
shows a stimulatory effect on activity
additional information
-
ornithine, D-lactic acid, citric acid, L-malic acid, and DL-malic acid do not modify activity
-
additional information
Q9I6J9
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
agmatine
-
-
0.016
-
agmatine
-
pH 7.0, 30C
0.033
-
agmatine
-, Q9ZN18
wild-type, pH 8.0, 37C
0.17
-
agmatine
-, Q9ZN18
mutant D198A, pH 8.0, 37C
0.19
-
agmatine
-
-
0.76
-
agmatine
-
-
0.8
-
agmatine
-
-
2.5
-
agmatine
-
-
6.67
-
agmatine
Q5KR05, -
-
15
-
agmatine
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0047
-
agmatine
-, Q9ZN18
mutant D198A, pH 8.0, 37C
0.082
-
agmatine
-, Q9ZN18
wild-type, pH 8.0, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000038
-
Ac-SGRGK
-, Q9ZN18
wild-type, pH 8.0, 37C
0
0.0000235
-
Ac-SGRGK
-, Q9ZN18
mutant D198A, pH 8.0, 37C
0
0.0283
-
agmatine
-, Q9ZN18
mutant D198A, pH 8.0, 37C
6544
0.136
-
agmatine
Q02J61, Q02J64
pH 9.0, 25C
6544
2.45
-
agmatine
-, Q9ZN18
wild-type, pH 8.0, 37C
6544
2.624
-
agmatine
Q02J61, Q02J64
pH 9.0, 37C
6544
0.0000678
-
guanidine
-, Q9ZN18
mutant D198A, pH 8.0, 37C
11192
0.0000812
-
guanidine
-, Q9ZN18
wild-type, pH 8.0, 37C
11192
0.000017
-
L-arginine
-, Q9ZN18
wild-type, pH 8.0, 37C
12093
0.000149
-
L-arginine
-, Q9ZN18
mutant D198A, pH 8.0, 37C
12093
0.000072
-
N-alpha-benzoyl-L-arginine amide
-, Q9ZN18
wild-type, pH 8.0, 37C
0
0.0001285
-
N-alpha-benzoyl-L-arginine amide
-, Q9ZN18
mutant D198A, pH 8.0, 37C
0
0.0000847
-
N-alpha-benzoyl-L-arginine ethyl ester
-, Q9ZN18
wild-type, pH 8.0, 37C
22200
0.0001383
-
N-alpha-benzoyl-L-arginine ethyl ester
-, Q9ZN18
mutant D198A, pH 8.0, 37C
22200
0.0001038
-
N-alpha-benzoyl-L-arginine methyl ester
-, Q9ZN18
wild-type, pH 8.0, 37C
22202
0.0002183
-
N-alpha-benzoyl-L-arginine methyl ester
-, Q9ZN18
mutant D198A, pH 8.0, 37C
22202
0.000033
-
streptomycin
-, Q9ZN18
mutant D198A, pH 8.0, 37C
16731
0.0000377
-
streptomycin
-, Q9ZN18
wild-type, pH 8.0, 37C
16731
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0033
-
arcaine
-
-
0.0071
-
arcaine
-
pH 7.0, 30C
0.028
-
arcaine
-, Q837U5
at 37C
10
-
spermine
-
-
2.5
-
tryptamine
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.013
-
Co2+
-, Q9ZN18
wild-type, pH 8.0, 37C
0.00087
-
N-(4-aminobutyl)-2-chloro-ethanimidamide
-, Q9ZN18
wild-type, pH 8.0, 37C
-
0.00026
-
N-(4-aminobutyl)-2-chloroethanimidamide
-
pH 8.0, 37C
-
0.00087
-
N-(4-aminobutyl)-2-chloroethanimidamide
-
pH 8.0, 37C
-
0.015
-
N-(4-aminobutyl)-2-chloroethanimidamide
-
pH 8.0, 37C
-
0.0068
-
N-(4-aminobutyl)-2-fluoro-ethanimidamide
-, Q9ZN18
wild-type, pH 8.0, 37C
-
0.00027
-
N-(4-aminobutyl)-2-fluoroethanimidamide
-
pH 8.0, 37C
-
0.0068
-
N-(4-aminobutyl)-2-fluoroethanimidamide
-
pH 8.0, 37C
-
0.091
-
N-(4-aminobutyl)-2-fluoroethanimidamide
-
pH 8.0, 37C
-
0.1
-
Ni2+
-, Q9ZN18
wild-type, pH 8.0, 37C
0.03
-
Zn2+
-, Q9ZN18
wild-type, pH 8.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
-
-
strain FA-1, 25 mM glucose, without agmatine
0.004
-
-
strain FA-1, 25 mM galactose, without agmatine
0.006
-
-
25 mM glucose + 10 mM agmatine
0.0097
-
-
25 mM sorbitol + 10 mM agmatine
0.01
-
-
crude extract of enzyme
0.01055
-
Q02J61, Q02J64
pH 9.0, 25C
0.0109
-
-
25 mM sorbitol + 10 mM agmatine
0.015
-
-
enzyme activity of shoots grown for 7 days at 25C in the dark and light respectively
0.015
-
Q02J61, Q02J64
pH 9.0, 37C
0.016
-
-
25 mM glucose + 10 mM agmatine
0.02
-
-
strain FA-1, 250 mM glucose, without agmatine
0.03
-
-
strain FA-1, 250 mM glucose + 10 mM agmatine
0.032
-
-
strain FA-1, 25 mM glucose + 10 mM agmatine
0.034
-
-
strain FA-1, 25 mM galactose + 10 mM agmatine
0.04
-
-
strain FA-1, 250 mM galactose, without agmatine
0.052
-
-
strain BHT, 25 mM glucose + 10 mM agmatine
0.058
-
-
strain UA159, 25 mM glucose + 10 mM agmatine
0.058
-
-
strain FA-1, 250 mM galactose + 10 mM agmatine
0.078
-
-
strain GS-5, 25 mM galactose + 10 mM agmatine
0.102
-
-
strain FA-1, 25 mM glucose + 10 mM agmatine
0.135
-
-
-
0.17
-
-
strain UA159, 25 mM sorbitol + 10 mM agmatine
0.4762
-
-
strain UA159, 25 mM galactose + 10 mM agmatine
2.64
-
-
-
5.9
-
-
cells in stationary phase of growth
14.5
-
-
purified enzyme
26.4
-
Q8GWW7
purified recombinant wild-type enzyme
32.2
-
-
purified enzyme
47.31
-
-
-
172.2
-
-
-
876.3
-
-
-
additional information
-
Q9I6J9
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
-
5.5
-
-
2fold higher actitity compared with enzyme activity at pH 7.0
6.5
7.5
-
-
6.5
-
-
-
6.5
-
-
-
6.5
-
Q5KR05, -
assay at
6.5
-
Q9I6J9
assay at; in vivo assay at
7.5
-
-
-
7.5
-
-
putrescine transcarbamylase and carbamate kinase function
8
-
-
ornithine transcarbamylase function
8
-
-
in Tris-HCl buffer
8.8
-
-
agmatine iminohydrolase function
additional information
-
-
assay at pH 6.0, 30 min, reaction stopped by 10% trichloroacetic acid
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
10.5
-
-
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
6
7
-
activity rapidly declining below pH 6.0 and declining less rapidly above pH 7.0
6
-
-
purified enzyme shows 85% of maximum activity
6.5
8
-
89% of maximal activity at pH 6.5, 91% of maximal activity at pH 8.0
8
-
-
purified enzyme shows 85% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28
-
Q9I6J9
assay at; in vivo assay at
30
-
-
assay at
35
40
Q8GWW7
-
40
-
Q5KR05, -
assay at
50
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
40
-
AgD activity 4fold higher in Streptococcus mutans grown at 42C than at 37C, stress response pathway of this organism
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q02J61, Q02J64
isoform Agu2A' contains a twin-arginine translocation signal at its N-terminus and is secreted to the periplasm
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41190
-
-
calculated from sequence data
45000
-
Q5KR05, -
gel filtration; SDS-PAGE
46000
-
-, Q837U5
SDS-PAGE
55000
-
-
gel filtration, PAGE
56000
-
-
gel filtration, Sephadex G-200
67000
-
-
gel filtration
70000
-
-
gel filtration
75000
-
-
gel filtration
81000
-
Q8GWW7
recombinant His-tagged wild-type enzyme, gel filtration
82000
-
-
gel filtration
85000
-
-
gel filtration
85000
-
-
-
85000
-
-
cross linkage
89000
-
-
gel filtration
150000
-
-
gel filtration
183000
-
-
gel filtration
183000
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q02J61, Q02J64
x * 39900, calculated for mature protein
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 95000, SDS-PAGE
dimer
-
-
dimer
-
-
dimer
Q8GWW7
2 * 43000, recombinant His-tagged wild-type enzyme, SDS-PAGE
heterodimer
-
1 * 43500 + 1 * 44000, SDS-PAGE
homodimer
-
2 * 43000, SDS-PAGE
monomer
-
1 * 55000, single polypeptide chain, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
oligomer
-
1 * 66000 + 1 * 48000 + 1 * 44000 + 1 * 15000, SDS-PAGE
tetramer
-, Q837U5
X-ray crystallography and gel filtration
tetramer
Enterococcus faecalis SD10
-
X-ray crystallography and gel filtration
-
monomer
Q5KR05, -
-
additional information
-
x * 36000, deglycosylated enzyme, SDS-PAGE, x * 47000, glycosylated enzyme, SDS-PAGE, monomer or dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
N-glycosylation
proteolytic modification
Q02J61, Q02J64
cleavage of translocation signal
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapour diffusion method with in 50 mM Tris-HCl, pH 7.45, 1 mM dithiothreitol and 20 mM NaCl
-, Q837U5
to 2.1 A resolution. Residue D198 is the key residue for agmatine recognition
-, Q9ZN18
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
6
9
Q5KR05, -
30 min, temperature below 40C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
purified enzyme stable for two months
33
-
-
50% loss of activity after heating for 15 min
40
-
Q5KR05, -
below 40C stable for 30 min, pH 6.0-9.0
40
-
-
above 40C a noticeable diminution of activity is observed
43
-
-
activity reduced by 50% on heating for 15 min
50
-
-
exposure for 10 min, decrease of 50% in the activity
55
-
-
retains 44% activity when exposed for 10 min, completely inactivated at 60C under the same conditions
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
highly unstable
-
highly unstable even in presence of glycerol, dithiothreitol and Mg2+, freeze-thawing and dialysis lead to considerable loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, purified enzyme, 2 months, stable
-
4C, purified enzyme lost 30% of the activity in 3 days
-
4C purified enzyme lost all component activities within 48 h
-
-20C purified enzyme lost 40% activity within 15 days
-
4C, purified enzyme lost 30% of the activity in 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by Ni2+-chelate affinity chromatography
Q8GWW7
2470fold
-
HisTrap Ni-affinity column chromatography and Superdex 200 HR gel filtration
-, Q837U5
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
-
strain PAO4495, 21fold purified to near homogeneity, gel filtration
-
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
-
enzyme purified from shoots grown in the dark by DE52 column chromatography, Sephadex G-100 column chromatography and agmatine-epoxy-Sepharose 6B column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA and amino acid sequence determination and analysis, expression as C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli
Q8GWW7
expressed in Escherichia coli BL21 (DE3) cells
-, Q837U5
expression in Escherichia coli
-, Q9ZN18
expression of wild type PAO1 in Escherichia coli XL1-Blue
-
expression in Escherichia coli
Q02J61, Q02J64
expression in Escherichia coli strain DE3
Q5KR05, -
expression in Escherichia coli DH10B
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
Q02J61, Q02J64
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
Q02J61, Q02J64
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C180A
Q8GWW7
site-directed mutagenesis, conserved catalytically relevant Cys, 35% of wild-type activity, inhibition with iodoacetamide is easier abolished by substrate agmatine
C364G
Q02J61, Q02J64
complete loss of activity
R3G/R4S
Q02J61, Q02J64
mutation of the twin-arginine translocation tat-sequence at the N-terminus. Mutant is hardly secreted to periplasm
C361A
Q5KR05, -
20% enzyme activity of wild-type enzyme
C366A
Q8GWW7
site-directed mutagenesis, conserved catalytically relevant Cys, 15% of wild-type activity, inhibition with iodoacetamide is easier abolished by substrate agmatine
additional information
-
mutant strain PAO4541
additional information
-
strain PAO5001, a knockout mutation of Gene PAO0292
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
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
-
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
medicine
Rhodococcus sp. C-x
-
developing of an analytic method for agmatine, being an important reagent for medical research
-
nutrition
Rhodococcus sp. C-x
-
developing of an analytic method for agmatine, being an important reagent for food research
-
medicine
-
remove of dental plaque biofilms
medicine
Streptococcus criceti AHT
-
remove of dental plaque biofilms
-
medicine
-
remove of dental plaque biofilms
medicine
Streptococcus downei 33748
-
remove of dental plaque biofilms
-
medicine
-
remove of dental plaque biofilms
medicine
-
remove of dental plaque biofilms
-