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Literature summary for 3.5.3.12 extracted from

  • Jones, J.E.; Dreyton, C.J.; Flick, H.; Causey, C.P.; Thompson, P.R.
    Mechanistic studies of agmatine deiminase from multiple bacterial species (2010), Biochemistry, 49, 9413-9423.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
2-chloroacetamidine
-
Helicobacter pylori
2-chloroacetamidine
-
Porphyromonas gingivalis
2-chloroacetamidine
-
Streptococcus mutans
iodoacetamide
-
Helicobacter pylori
iodoacetamide
-
Porphyromonas gingivalis
iodoacetamide
-
Streptococcus mutans
N-(4-aminobutyl)-2-chloroethanimidamide
-
Helicobacter pylori
N-(4-aminobutyl)-2-chloroethanimidamide
-
Porphyromonas gingivalis
N-(4-aminobutyl)-2-chloroethanimidamide
-
Streptococcus mutans
N-(4-aminobutyl)-2-fluoroethanimidamide inactivation proceeds via a multistep mechanism that requires general acid catalysis Helicobacter pylori
N-(4-aminobutyl)-2-fluoroethanimidamide inactivation proceeds via a multistep mechanism that requires general acid catalysis Porphyromonas gingivalis
N-(4-aminobutyl)-2-fluoroethanimidamide inactivation proceeds via a multistep mechanism that requires general acid catalysis Streptococcus mutans

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-
Porphyromonas gingivalis
-
-
-
Streptococcus mutans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration Helicobacter pylori
the protein is recombinantly expressed, lysed by sonication, and then purified by a combination of anion exchange, heparin affinity, and gel filtration Porphyromonas gingivalis
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

Reaction Comment Organism Reaction ID
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
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agmatine + H2O
-
Helicobacter pylori N-carbamoylputrescine + NH3
-
?
agmatine + H2O
-
Porphyromonas gingivalis N-carbamoylputrescine + NH3
-
?
agmatine + H2O
-
Streptococcus mutans N-carbamoylputrescine + NH3
-
?

Synonyms

Synonyms Comment Organism
agmatine deiminase
-
Porphyromonas gingivalis
agmatine deiminase
-
Streptococcus mutans
agmatine deiminaseHpAgD
-
Helicobacter pylori
PgAgD
-
Porphyromonas gingivalis
SmAgD
-
Streptococcus mutans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Helicobacter pylori
37
-
assay at Porphyromonas gingivalis
37
-
assay at Streptococcus mutans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Helicobacter pylori
8
-
assay at Porphyromonas gingivalis
8
-
assay at Streptococcus mutans

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00026
-
pH 8.0, 37°C Streptococcus mutans N-(4-aminobutyl)-2-chloroethanimidamide
0.00027
-
pH 8.0, 37°C Streptococcus mutans N-(4-aminobutyl)-2-fluoroethanimidamide
0.00087
-
pH 8.0, 37°C Helicobacter pylori N-(4-aminobutyl)-2-chloroethanimidamide
0.0068
-
pH 8.0, 37°C Helicobacter pylori N-(4-aminobutyl)-2-fluoroethanimidamide
0.015
-
pH 8.0, 37°C Porphyromonas gingivalis N-(4-aminobutyl)-2-chloroethanimidamide
0.091
-
pH 8.0, 37°C Porphyromonas gingivalis N-(4-aminobutyl)-2-fluoroethanimidamide