BRENDA - Enzyme Database

Mechanistic studies of agmatine deiminase from multiple bacterial species

Jones, J.E.; Dreyton, C.J.; Flick, H.; Causey, C.P.; Thompson, P.R.; Biochemistry 49, 9413-9423 (2010)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.5.3.12
2-chloroacetamidine
-
Helicobacter pylori
3.5.3.12
2-chloroacetamidine
-
Porphyromonas gingivalis
3.5.3.12
2-chloroacetamidine
-
Streptococcus mutans
3.5.3.12
iodoacetamide
-
Helicobacter pylori
3.5.3.12
iodoacetamide
-
Porphyromonas gingivalis
3.5.3.12
iodoacetamide
-
Streptococcus mutans
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Helicobacter pylori
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Porphyromonas gingivalis
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Streptococcus mutans
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Helicobacter pylori
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Porphyromonas gingivalis
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Streptococcus mutans
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.5.3.12
Helicobacter pylori
-
-
-
3.5.3.12
Porphyromonas gingivalis
-
-
-
3.5.3.12
Streptococcus mutans
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Helicobacter pylori
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Porphyromonas gingivalis
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Streptococcus mutans
Reaction
EC Number
Reaction
Commentary
Organism
3.5.3.12
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
Helicobacter pylori
3.5.3.12
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
Porphyromonas gingivalis
3.5.3.12
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
Streptococcus mutans
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.5.3.12
agmatine + H2O
-
718884
Helicobacter pylori
N-carbamoylputrescine + NH3
-
-
-
?
3.5.3.12
agmatine + H2O
-
718884
Porphyromonas gingivalis
N-carbamoylputrescine + NH3
-
-
-
?
3.5.3.12
agmatine + H2O
-
718884
Streptococcus mutans
N-carbamoylputrescine + NH3
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.5.3.12
37
-
assay at
Helicobacter pylori
3.5.3.12
37
-
assay at
Porphyromonas gingivalis
3.5.3.12
37
-
assay at
Streptococcus mutans
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.5.3.12
8
-
assay at
Helicobacter pylori
3.5.3.12
8
-
assay at
Porphyromonas gingivalis
3.5.3.12
8
-
assay at
Streptococcus mutans
IC50 Value
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
3.5.3.12
0.00026
-
pH 8.0, 37°C
Streptococcus mutans
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.00027
-
pH 8.0, 37°C
Streptococcus mutans
N-(4-aminobutyl)-2-fluoroethanimidamide
3.5.3.12
0.00087
-
pH 8.0, 37°C
Helicobacter pylori
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.0068
-
pH 8.0, 37°C
Helicobacter pylori
N-(4-aminobutyl)-2-fluoroethanimidamide
3.5.3.12
0.015
-
pH 8.0, 37°C
Porphyromonas gingivalis
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.091
-
pH 8.0, 37°C
Porphyromonas gingivalis
N-(4-aminobutyl)-2-fluoroethanimidamide
IC50 Value (protein specific)
EC Number
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
3.5.3.12
0.00026
-
pH 8.0, 37°C
Streptococcus mutans
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.00027
-
pH 8.0, 37°C
Streptococcus mutans
N-(4-aminobutyl)-2-fluoroethanimidamide
3.5.3.12
0.00087
-
pH 8.0, 37°C
Helicobacter pylori
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.0068
-
pH 8.0, 37°C
Helicobacter pylori
N-(4-aminobutyl)-2-fluoroethanimidamide
3.5.3.12
0.015
-
pH 8.0, 37°C
Porphyromonas gingivalis
N-(4-aminobutyl)-2-chloroethanimidamide
3.5.3.12
0.091
-
pH 8.0, 37°C
Porphyromonas gingivalis
N-(4-aminobutyl)-2-fluoroethanimidamide
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.5.3.12
2-chloroacetamidine
-
Helicobacter pylori
3.5.3.12
2-chloroacetamidine
-
Porphyromonas gingivalis
3.5.3.12
2-chloroacetamidine
-
Streptococcus mutans
3.5.3.12
iodoacetamide
-
Helicobacter pylori
3.5.3.12
iodoacetamide
-
Porphyromonas gingivalis
3.5.3.12
iodoacetamide
-
Streptococcus mutans
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Helicobacter pylori
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Porphyromonas gingivalis
3.5.3.12
N-(4-aminobutyl)-2-chloroethanimidamide
-
Streptococcus mutans
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Helicobacter pylori
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Porphyromonas gingivalis
3.5.3.12
N-(4-aminobutyl)-2-fluoroethanimidamide
inactivation proceeds via a multistep mechanism that requires general acid catalysis
Streptococcus mutans
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Helicobacter pylori
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Porphyromonas gingivalis
3.5.3.12
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration
Streptococcus mutans
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.5.3.12
agmatine + H2O
-
718884
Helicobacter pylori
N-carbamoylputrescine + NH3
-
-
-
?
3.5.3.12
agmatine + H2O
-
718884
Porphyromonas gingivalis
N-carbamoylputrescine + NH3
-
-
-
?
3.5.3.12
agmatine + H2O
-
718884
Streptococcus mutans
N-carbamoylputrescine + NH3
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.5.3.12
37
-
assay at
Helicobacter pylori
3.5.3.12
37
-
assay at
Porphyromonas gingivalis
3.5.3.12
37
-
assay at
Streptococcus mutans
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.5.3.12
8
-
assay at
Helicobacter pylori
3.5.3.12
8
-
assay at
Porphyromonas gingivalis
3.5.3.12
8
-
assay at
Streptococcus mutans