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agmatine-L-Arg + H2O
N5-carbamoyl-N2-[4-(carbamoylamino)butyl]-L-ornithine + NH3
-
3.2% activity compared to L-Arg
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
Boc-Gln-Arg-Arg-MCA + H2O
? + NH3
-
-
-
-
?
bradykinin-L-Arg + H2O
bradykinin-L-citrulline + NH3
-
18.8% activity compared to L-Arg
-
-
?
D-Arg + H2O
?
-
26.4% activity compared to L-Arg
-
-
?
D-Arg + H2O
D-citrulline + NH3
-
0.38% of the activity with L-Arg
-
-
?
guanidine + H2O
urea + NH3
-
-
-
-
?
homoarginine + H2O
(2S)-2-amino-6-[(aminocarbonyl)amino]hexanoic acid + NH3
-
50% activity compared to L-Arg
-
-
?
KRPPGFSPL + H2O
L-lysyl-N5-carbamoyl-L-ornithyl-L-prolyl-L-prolylglycyl-L-phenylalanyl-L-seryl-L-prolyl-L-leucine + NH3
-
3.1% activity compared to L-Arg
-
-
?
L-alpha-amino-beta-guanidinepropionic acid + H2O
2-amino-3-carbamoylpropionic acid + NH3
-
-
-
-
?
L-alpha-amino-beta-guanidinopropionic acid + H2O
2-amino-3-carbamoylpropionic acid + NH3
-
-
-
-
?
L-alpha-amino-gamma-guanidinobutyric acid + H2O
2-amino-4-carbamoylbutanoic acid + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
L-Arg + H2O
L-citrulline + NH3
L-arginine + H2O
L-citrulline + NH3
L-arginine ethyl ester + H2O
?
L-arginine hydroxamate + H2O
?
-
68.2% activity compared to L-Arg
-
-
?
L-argininic acid + H2O
(2S)-5-[(aminocarbonyl)amino]-2-hydroxypentanoic acid + NH3
-
0.032% of the activity with L-Arg
-
-
?
L-canavanine + H2O
(2S)-2-amino-4-[[(aminocarbonyl)amino]oxy]butanoic acid + NH3
-
2.3% of the activity with L-Arg
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
L-canavanine + H2O
O-ureidohomoserine + NH3
-
via enzyme Cys-bound S-alkyl-thiouronium intermediate, residues Asp166 and Asp280 are involved, overview
product identification by mass spectrometry
-
?
L-canavanine-L-Arg + H2O
O-ureido-L-homoserine + NH3
-
2.5% activity compared to L-Arg
-
-
?
L-homoarginine + H2O
(2S)-2-amino-6-[(aminocarbonyl)amino]hexanoic acid + NH3
-
0.05% of the activity with L-Arg
-
-
?
L-nitroarginine + H2O
NH3 + nitrocitrulline
-
-
-
-
?
L-Pro-L-Arg-L-Phe + H2O
?
-
3.4% activity compared to L-Arg
-
-
?
L-Pro-L-Phe-L-Arg + H2O
?
-
78.2% activity compared to L-Arg
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
N-alpha-benzoyl-L-arginine ethyl ester + H2O
N-alpha-benzoyl-L-citrulline methyl ester + NH3
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
?
Nalpha-methyl-L-Arg + H2O
Nalpha-methyl-L-citrulline + NH3
-
0.75% of the activity with L-Arg
-
-
?
Nomega-amino-Arg + H2O
L-citrulline + hydrazine
-
-
-
?
Nomega-amino-L-arginine + H2O
hydrazine + L-citrulline
Nomega-amino-L-arginine + H2O
L-citrulline + hydrazine
-
-
-
?
Nomega-hydroxy-L-arginine + H2O
Nomega-hydroxy-L-citrulline + NH3
-
2.1% activity compared to L-Arg
-
-
?
Nomega-methyl-Arg + H2O
L-citrulline + methylamine
-
-
-
?
Nomega-methyl-L-arginine + H2O
L-citrulline + methylamine
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
additional information
?
-
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
-
8.1% activity compared to L-Arg
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
-
8.1% activity compared to L-Arg
-
-
?
L-alanine + H2O
? + NH3
-
-
-
-
?
L-alanine + H2O
? + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
caffeine markedly increases the formation of arginine deiminase when dextrin, but not maltotriose, serves as the energy source
-
-
?
L-Arg + H2O
citrulline + NH3
-
caffeine markedly increases the formation of arginine deiminase when dextrin, but not maltotriose, serves as the energy source
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
enzyme of catabolism of Arg to citrulline in the arginine dihydrolase pathway
-
?
L-Arg + H2O
citrulline + NH3
-
enzyme of the arginine dihydrolase pathway. Arginine metabolism via this pathway plays a significant role in energy metabolism by providing a site for anaerobic substrate level phosphorylation
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
Lentilactobacillus hilgardii Microenos HP
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
in vivo and in vitro anti-tumor activities for 6 kinds of mouse ascites tumor cell lines
-
-
?
L-Arg + H2O
citrulline + NH3
-
cytostatic activity, the enzyme-induced arginine depletion may inhibit protein synthesis and results in the protection of apoptotic cell death that requires new protein synthesis
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
the recombinant enzyme inhibits the growth of two mouse cells lines hepatoma MH134 and fibrosarcoma Meth A
-
-
?
L-Arg + H2O
citrulline + NH3
-
deletion of the essential nutrient L-Arg by arginine deiminase significantly inhibits cell growth and activation in T lymphoblasts, accompanied by the induction of apoptotic cell death
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
alternate energy pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
100% activity
-
-
?
L-Arg + H2O
citrulline + NH3
-
100% activity
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
-
catabolism of Arg by arginine deiminase pathway
-
-
?
L-Arg + H2O
citrulline + NH3
-
potent inhibition of proliferation of human T cells by streptococcal cell extract is due to activity of arginine deiminase
-
-
?
L-Arg + H2O
citrulline + NH3
-
enzyme of catabolism of Arg to citrulline in the arginine dihydrolase pathway
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
ir
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
Lentilactobacillus hilgardii Microenos HP
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
ir
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-Arg + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview, ADI is a potential anti-angiogenic agent and is effective in the treatment of leukemia
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
the enzyme reduces extracellular arginine, which inhibits viral replication, ADI bound to PEG 20 000 probably reduces hepatitis C virus viral titers through nitric oxide-dependent effects
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
the enzyme is involved in the arginine metabolism, e.g. in strain Lp60, which accumulates L-citrulline, the precursor of the carcinogen ethyl-carbamate, showing high activity, while the activity of ornithine transcarbamylase is low
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
the enzyme is involved in the arginine metabolism, e.g. in strain Lp60, which accumulates L-citrulline, the precursor of the carcinogen ethyl-carbamate, showing high activity, while the activity of ornithine transcarbamylase is low
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
ADI is the key enzyme of the ADI pathway
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
arginine catabolism
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
arginine catabolism
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
ADi shows inhibitory ability on the proliferation of mouse melanoma cells
-
-
ir
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
substrate binding abilities of recombinant wild-type and mutant enzymes, substrate binding induces structural changes, overview
-
-
ir
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
arginine deiminase enhances human MCF-7 cell radiosensitivity by inducing changes in the expression of cell cycle-related proteins, e.g. upregulation of CDK inhibitors p21 and p27 and downregulation of c-Myc, ammonia is not involved, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
ir
L-arginine + H2O
L-citrulline + NH3
specific for
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
via enzyme Cys-bound S-alkyl-thiouronium intermediate, residues Asp166 and Asp280 are involved, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
via enzyme Cys-bound S-alkyl-thiouronium intermediate, substrate binding and enzyme-intermediate structure of wild-type and mutant enzymes, modeling, overview
-
-
ir
L-arginine + H2O
L-citrulline + NH3
ADI catalyzes the first step of the energy-producing arginine degradation pathway found in certain microorganisms, which ultimately leads to ornithine, carbamate, and ATP, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
first step of the arginine deiminase pathway, overview
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine + H2O
L-citrulline + NH3
-
-
-
-
?
L-arginine ethyl ester + H2O
?
-
-
-
?
L-arginine ethyl ester + H2O
?
-
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
-
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
-
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
-
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
-
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
slow substrate, reaction via Cys-alkylthiouronium ion intermediate, two competing pathways follow that branch at the Cys-alkylthiouronium ion intermediate, overview
-
-
?
L-lysine + H2O
? + NH3
-
-
-
-
?
L-lysine + H2O
? + NH3
-
-
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
-
54.5% activity compared to L-Arg
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
-
54.5% activity compared to L-Arg
-
-
?
Nalpha-benzoyl-L-arginine + H2O
?
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
?
-
-
-
?
Nomega-amino-L-arginine + H2O
hydrazine + L-citrulline
-
-
-
?
Nomega-amino-L-arginine + H2O
hydrazine + L-citrulline
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
-
-
-
-
?
additional information
?
-
does not accept agmatine, L-homoarginine, Nalpha-benzoyl-L-arginine ethyl ester as substrate
-
-
?
additional information
?
-
-
does not accept agmatine, L-homoarginine, Nalpha-benzoyl-L-arginine ethyl ester as substrate
-
-
?
additional information
?
-
does not accept agmatine, L-homoarginine, Nalpha-benzoyl-L-arginine ethyl ester as substrate
-
-
?
additional information
?
-
-
anti-tumor activity of arginine deiminase via arginine deprivation in retinoblastoma, overview
-
-
?
additional information
?
-
-
arginine deiminase formulated with polyethyleneglycol specifically inhibits growth of cell lines lacking argininosuccinate synthetase, inducing caspase activation and induction of apoptosis
-
-
?
additional information
?
-
-
the recombinant enzyme reduces inducible nitric oxide synthase-mediated neurotoxicity in a coculture of neurons and microglia
-
-
?
additional information
?
-
-
ADI has anti-cancer activity by causing depletion of L-arginine by reducing the circulating amount, fusion of ADI to 20 kDa PEG improves its pharmaceutical efficiency, overview
-
-
?
additional information
?
-
-
the enzyme shows anti-tumor activity inhibiting growth of several murine and human tumor cell lines in vitro and in vivo
-
-
?
additional information
?
-
-
native and recombinant enzyme shows anti-angiogenic and anti-tumor activity inhibiting growth of several murine and human tumor cell lines in vitro and in vivo, e.g. against human umbilical vein cells, HUVEC
-
-
?
additional information
?
-
-
no activity with Nomega,Nomega-dimethyl-L-arginine
-
-
?
additional information
?
-
-
no activity with Nomega,Nomega-dimethyl-L-arginine
-
-
?
additional information
?
-
structural basis for substrate specificity, overview
-
-
?
additional information
?
-
-
structural basis for substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with agmatine
-
-
?
additional information
?
-
no activity with agmatine
-
-
?
additional information
?
-
the recombinant enzyme shows anti-tumor activity inhibiting growth of human Hep-G2 tumor cell line
-
-
?
additional information
?
-
the recombinant enzyme shows anti-tumor activity inhibiting growth of human Hep-G2 tumor cell line
-
-
?
additional information
?
-
-
the enzyme shows anti-tumor activity in murine leukemia lymphoblasts in vitro
-
-
?
additional information
?
-
-
ArcA inhibits production of a major adhesin, FimA, in Porphyromonas gingivalis
-
-
?
additional information
?
-
-
ArcA inhibits production of a major adhesin, FimA, in Porphyromonas gingivalis
-
-
?
additional information
?
-
-
the arginine deiminase system enables Streptococcus suis to overcome oxygen and nutrient starvation and to tolerate acidic environment. Thus the arginine deiminase system might facilitate Streptococcus suis survival within the different niches of the host and thereby probably contributes to Streptococcus suis pathogenesis
-
-
?
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18
benzoyl-L-arginine ethyl ester
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
9.5 - 12.3
Boc-Gln-Arg-Arg-MCA
0.033
bradykinin antagonist-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.021
bradykinin-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
2.38
L-Alpha-amino-beta-guanidinopropionic acid
-
-
3.03
L-Alpha-amino-gamma-guanidinobutyric acid
-
-
2.1
L-arginine ethyl ester
in 50 mM K+-HEPES (pH 7.5), at 25°C
6.9
L-Arginine hydroxamate
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
6
L-canavanine-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.07
L-Pro-L-Arg-L-Phe
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.089
L-Pro-L-Phe-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.01 - 0.02
N-alpha-benzoyl-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.1 - 30
N-alpha-benzoyl-L-arginine ethyl ester
1.2
Nalpha-methyl-L-Arg
-
-
50
Nomega-amino-Arg
pH 5.6, 25°C, wild-type enzyme
0.002 - 50
Nomega-amino-L-arginine
1.5
Nomega-hydroxy-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
21
Nomega-methyl-Arg
pH 5.6, 25°C, wild-type enzyme
21
Nomega-methyl-L-arginine
pH 5.6, 25°C, wild-type enzyme
additional information
additional information
-
9.5
Boc-Gln-Arg-Arg-MCA
-
pH 8.0, 37°C, dextran-conjugated enzyme
12.3
Boc-Gln-Arg-Arg-MCA
-
pH 8.0, 37°C, soluble enzyme
1.9
D-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
8.66
L-alanine
-
pH 7.0, 45°C, soluble enzyme
15.48
L-alanine
-
pH 7.0, 45°C, PEGylated enzyme
23.21
L-alanine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
0.004
L-Arg
-
-
0.004
L-Arg
-
ammonium assay at 25°C
0.004
L-Arg
-
at pH 7.2, 25°C
0.028
L-Arg
-
ammonium assay at 37°C
0.05
L-Arg
-
strain MR-100
0.06
L-Arg
-
at pH 7.0 and 25°C
0.07
L-Arg
-
strain TV 10
0.09
L-Arg
-
at pH 5.6 and 25°C
0.1 - 0.4
L-Arg
-
citrulline assay
0.14
L-Arg
pH 5.6, 25°C, wild-type enzyme
0.14
L-Arg
at pH 5.6 and 25°C
0.32
L-Arg
-
at pH 6.0 and 25°C
1.1
L-Arg
pH 5.6, 25°C, mutant enzyme E224A
1.2
L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
2.6
L-Arg
pH 5.6, 25°C, mutant enzyme R243A
2.7
L-Arg
pH 5.6, 25°C, mutant enzyme N160A
2.88
L-Arg
-
pH 6.0, 37°C, wild-type
4.2
L-Arg
pH 5.6, 25°C, mutant enzyme E224D
4.8
L-Arg
pH 5.6, 25°C, mutant enzyme R185L
6.9
L-Arg
pH 5.6, 25°C, mutant enzyme R243K
8.7
L-Arg
pH 5.6, 25°C, mutant enzyme R401A
15
L-Arg
pH 5.6, 25°C, mutant enzyme R185A
38
L-Arg
pH 5.6, 25°C, mutant enzyme R243L
0.09
L-arginine
-
pH 7.0, 25°C
0.09
L-arginine
-
pH 5.6, 25°C
0.14
L-arginine
-
pH 5.6, 25°C
0.14
L-arginine
pH 5.6, 25°C
0.14
L-arginine
pH 5.6, 25°C, wild-type enzyme
0.16
L-arginine
-
pH 7.5, 25°C
0.16
L-arginine
in 50 mM K+-HEPES (pH 7.5), at 25°C
0.16
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/R243L
0.24
L-arginine
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.32
L-arginine
-
pH 6.0, 25°C
0.52
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K
0.59
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/S245D
0.62
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/A276W
0.65
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L
0.67
L-arginine
-
pH and temperature not specified in the publication
0.7
L-arginine
-
wild type enzyme, in 0.5 M phosphate buffer, pH 7.4, at 37°C
0.71
L-arginine
-
pH 7.4, 37°C, recombinant mutant D160E
0.92
L-arginine
-
pH 8.0, 37°C, dextran-conjugated enzyme
1.1
L-arginine
pH 5.6, 25°C, mutant E224A
1.2
L-arginine
-
mutant enzyme H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C
1.33
L-arginine
at pH 6.5 and 37°C
2.5
L-arginine
-
mutant enzyme K5T/D44E/H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C
2.6
L-arginine
pH 5.6, 25°C, mutant R243A
2.7
L-arginine
pH 5.6, 25°C, mutant N160A
4.2
L-arginine
pH 5.6, 25°C, mutant E224D
4.8
L-arginine
-
pH 8.0, 37°C, soluble enzyme
4.8
L-arginine
pH 5.6, 25°C, mutant R185L
6
L-arginine
pH and temperature not specified in the publication
6.4
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/F269Y/G292P
6.7
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/G292P
6.9
L-arginine
pH 5.6, 25°C, mutant R243K
8.67
L-arginine
pH 7.2, 60°C
8.7
L-arginine
pH 5.6, 25°C, mutant R401A
8.76
L-arginine
-
pH 7.0, 45°C, soluble enzyme
9.3
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/F269Y
10.1
L-arginine
pH 6.0, 45°C, wild-type enzyme
11.6
L-arginine
pH 6.0, 45°C, mutant enzyme R15K
12.5
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/G264P
15
L-arginine
pH 5.6, 25°C, mutant R185A
15.57
L-arginine
-
pH 7.0, 45°C, PEGylated enzyme
22.52
L-arginine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
38
L-arginine
pH 5.6, 25°C, mutant R243L
0.044
L-canavanine
-
-
0.7
L-canavanine
pH 5.6, 25°C
1.2
L-canavanine
-
pH 5.6, 25°C
1.9
L-canavanine
-
pH 7.5, 25°C
2.1
L-canavanine
-
pH 6.0, 25°C
2.3
L-canavanine
-
pH 7.0, 25°C
12.34
L-lysine
-
pH 7.0, 45°C, soluble enzyme
15.48
L-lysine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
18.42
L-lysine
-
pH 7.0, 45°C, PEGylated enzyme
0.1
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme F221A/F222A
0.12
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D123N
0.14
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D125A
0.16
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, wild-type enzyme
0.25
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D169A
0.33
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D166A
0.6
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D389A
2.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D177A
3.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E352A
4.4
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme R347
5
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D370A
6.3
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme Q350A
8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D374A
13
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E412A
30
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme W373A
0.002
Nomega-amino-L-arginine
in 50 mM K+-HEPES (pH 7.5), at 25°C
50
Nomega-amino-L-arginine
pH 5.6, 25°C, wild-type enzyme
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes through molecular dynamics and density functional studies
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.019
benzoyl-L-arginine ethyl ester
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.0068
bradykinin antagonist-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.043
bradykinin-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.058
D-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
2.3
L-arginine ethyl ester
in 50 mM K+-HEPES (pH 7.5), at 25°C
0.15
L-Arginine hydroxamate
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.0052
L-canavanine-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.0075
L-Pro-L-Arg-L-Phe
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.17
L-Pro-L-Phe-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.12
N-alpha-benzoyl-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.03 - 2.65
N-alpha-benzoyl-L-arginine ethyl ester
2.5
Nalpha-benzoyl-L-arginine
in 50 mM K+-HEPES (pH 7.5), at 25°C
7
Nomega-amino-Arg
pH 5.6, 25°C, wild-type enzyme
0.58 - 7
Nomega-amino-L-arginine
0.0046
Nomega-hydroxy-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.01
Nomega-methyl-Arg
pH 5.6, 25°C, wild-type enzyme
1
Nomega-methyl-L-arginine
pH 5.6, 25°C, wild-type enzyme
additional information
additional information
-
-
-
0.0024
L-alanine
-
pH 7.0, 45°C, soluble enzyme
0.0034
L-alanine
-
pH 7.0, 45°C, PEGylated enzyme
0.006
L-alanine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
0.00036
L-Arg
pH 5.6, 25°C, mutant enzyme R401L
0.00089
L-Arg
pH 5.6, 25°C, mutant enzyme R243A
0.002
L-Arg
pH 5.6, 25°C, mutant enzyme R243K
0.0021
L-Arg
pH 5.6, 25°C, mutant enzyme E224A
0.0037
L-Arg
pH 5.6, 25°C, mutant enzyme E224D
0.0072
L-Arg
pH 5.6, 25°C, mutant enzyme R401A
0.0084
L-Arg
pH 5.6, 25°C, mutant enzyme R185L
0.009
L-Arg
pH 5.6, 25°C, mutant enzyme R243L
0.021
L-Arg
pH 5.6, 25°C, mutant enzyme N160A
0.089
L-Arg
pH 5.6, 25°C, mutant enzyme R185A
0.22
L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
1.3
L-Arg
-
at pH 5.6 and 25°C
3.2
L-Arg
-
at pH 6.0 and 25°C
3.2
L-Arg
-
at pH 7.0 and 25°C
6.3
L-Arg
pH 5.6, 25°C, wild-type enzyme
6.3
L-Arg
at pH 5.6 and 25°C
0.0041
L-arginine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
0.00475
L-arginine
-
pH 7.0, 45°C, PEGylated enzyme
0.00478
L-arginine
-
pH 7.0, 45°C, soluble enzyme
0.013
L-arginine
-
pH 7.4, 37°C, recombinant mutant D160E
0.151
L-arginine
-
pH 7.4, 37°C, recombinant wild-type enzyme
0.2
L-arginine
pH 7.4, 37°C, wild-type enzyme
0.2
L-arginine
pH 5.6, 25°C, mutant R243L
0.3
L-arginine
pH 5.6, 25°C, mutant R243A
0.3
L-arginine
pH 5.6, 25°C, mutant R243K
0.8
L-arginine
pH 5.6, 25°C, mutant R401A
0.9
L-arginine
pH 5.6, 25°C, mutant E224D
1.3
L-arginine
-
pH 5.6, 25°C
1.8
L-arginine
pH 5.6, 25°C, mutant R185L
1.9
L-arginine
pH 5.6, 25°C, mutant E224A
2.6
L-arginine
-
pH 7.5, 25°C
2.6
L-arginine
in 50 mM K+-HEPES (pH 7.5), at 25°C
3.2
L-arginine
-
pH 6.0, 25°C
4.4
L-arginine
-
pH 7.0, 25°C
5.6
L-arginine
-
wild type enzyme, in 0.5 M phosphate buffer, pH 7.4, at 37°C
5.9
L-arginine
pH 5.6, 25°C, mutant R185A
6.3
L-arginine
pH 5.6, 25°C, wild-type enzyme
6.3
L-arginine
pH 5.6, 25°C
8
L-arginine
pH 5.6, 25°C, mutant N160A
8.1
L-arginine
-
mutant enzyme H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C
11.64
L-arginine
pH 7.4, 37°C, mutant enzyme K5T/D38H/D44E/A128T/E296K/H404R
18.27
L-arginine
pH 7.4, 37°C, mutant enzyme K30R/C37R/G129S/L148P/V291L
20.94
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/A276W
21.1
L-arginine
pH 7.4, 37°C, mutant enzyme K30R/C37R/L148P/V291L
21.27
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K
22.4
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/S245D
22.5
L-arginine
-
mutant enzyme K5T/D44E/H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C
27.2
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L
30.25
L-arginine
pH 7.4, 37°C, mutant enzyme A128T/H404/I410L/D38H/E298K/R243L
35
L-arginine
-
pH and temperature not specified in the publication
268
L-arginine
pH 6.0, 45°C, mutant enzyme R15K
291
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/G264P
309
L-arginine
pH 6.0, 45°C, wild-type enzyme
342
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/F269Y
365
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/F269Y/G292P
371
L-arginine
pH 6.0, 45°C, mutant enzyme R15K/G292P
0.09
L-canavanine
-
pH 5.6, 25°C
0.32
L-canavanine
-
pH 7.5, 25°C
0.42
L-canavanine
-
pH 6.0, 25°C
0.46
L-canavanine
-
pH 7.0, 25°C
0.62
L-canavanine
pH 5.6, 25°C
0.0033
L-lysine
-
pH 7.0, 45°C, enzyme covalently immobilized on dextran
0.004
L-lysine
-
pH 7.0, 45°C, soluble enzyme
0.0043
L-lysine
-
pH 7.0, 45°C, PEGylated enzyme
0.03
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme Q350A
0.1
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E412A
0.2
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme W373A
0.25
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme E352A
0.35
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D166A
0.51
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D389A
0.6
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D370A
0.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D123N
0.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D125A
1.53
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme R347
1.55
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D374A
1.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D169A
1.8
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme F221A/F222A
2.65
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, wild-type enzyme
2.65
N-alpha-benzoyl-L-arginine ethyl ester
pH 7.6, 37°C, mutant enzyme D177A
0.58
Nomega-amino-L-arginine
in 50 mM K+-HEPES (pH 7.5), at 25°C
7
Nomega-amino-L-arginine
pH 5.6, 25°C, wild-type enzyme
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C265S/C336S
-
the mutant is catalytically active
F269P
the conversion rate of L-arginine to L-citrulline at 45°C is 93.2% compared to wild-type enzyme
G292C
the conversion rate of L-arginine to L-citrulline at 45°C is 96.0% compared to wild-type enzyme
G292D
the conversion rate of L-arginine to L-citrulline at 45°C is 97.5% compared to wild-type enzyme
G292P
the conversion rate of L-arginine to L-citrulline at 45°C is 96.5% compared to wild-type enzyme
R15K
the conversion rate of L-arginine to L-citrulline at 45°C is 95.8% compared to wild-type enzyme
R15K/F269Y/G292P
the triple-site mutant enzyme displays a 2.5fold higher specific enzyme activity (333 U/mg), a lower Km value of 6.4 mM, and a 6.1fold longer half-life (t1/2(45°C): 86.7 min) than wild-type enzyme. The conversion rate of L-arginine to L-citrulline at 45°C is 97.4% compared to wild-type enzyme
G292C
-
the conversion rate of L-arginine to L-citrulline at 45°C is 96.0% compared to wild-type enzyme
-
G292D
-
the conversion rate of L-arginine to L-citrulline at 45°C is 97.5% compared to wild-type enzyme
-
G292P
-
the conversion rate of L-arginine to L-citrulline at 45°C is 96.5% compared to wild-type enzyme
-
R15K
-
the conversion rate of L-arginine to L-citrulline at 45°C is 95.8% compared to wild-type enzyme
-
R15K/F269Y/G292P
-
the triple-site mutant enzyme displays a 2.5fold higher specific enzyme activity (333 U/mg), a lower Km value of 6.4 mM, and a 6.1fold longer half-life (t1/2(45°C): 86.7 min) than wild-type enzyme. The conversion rate of L-arginine to L-citrulline at 45°C is 97.4% compared to wild-type enzyme
-
D123N
2.5fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D125A
2.75fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D166A
85fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D169A
2fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D177A
15fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D370A
220fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D374A
145fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D389A
20fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E352A
1250fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E412A
3300fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
F221A/F222A
1.1fold increase in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
Q350A
2350fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
R347A
fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
W373A
50fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D160E
-
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme
D160E/D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
D160E/E212D
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
E212D
-
site-directed mutagenesis, almost inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
E212D/D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
H268F
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
H268Y
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
R185K
site-directed mutagenesis, unstable mutant enzyme that precipitates
R401L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A128T/H404R/I410L
-
in contrast to wild-type mutant shows very high activity activity at pH 7.4 and pH 6.0, Km (L-Arg) 0.43 at pH 6.0, Km (L-Arg) 0.65 at pH 7.4, pH optimum: 6.5
D38H/A128T/E296K/H404R/I410L/A276W
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/A276W displays tremendous pH and thermal stability
D38H/A128T/E296K/H404R/I410L/R243L
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/R243L exhibits significantly enhanced specific activity and substrate binding affinity, as illustrated by the dramatically reduced Km value (0.16 mmol/l) and a more favorable free energy of L-arginine binding at physiological conditions
D38H/A128T/E296K/H404R/I410L/S245D
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, mutant enzyme D38H/A128T/E296K/H404R/I410L/S245D shows a significantly increased specific activity and a similar Km value at physiological conditions
H404R
-
the mutant shows higher activity (1.8fold) and improved activity ratio at pH 7.4 to 6.4 (4.7fold) compared to the wild type ADI
K30R/C37R/G129S/L148P/V291L
91fold increase in kcat as compared to wild-type enzyme. More than two times reduced S0.5 value compared to mutant K5T/D38H/D44E/A128T/E296K/H404R
K30R/C37R/L148P/V291L
105fold increase in kcat as compared to wild-type enzyme, the mutant is a highly attractive candidate to be used as therapeutic protein for the treatment of arginine-auxotrophic melanomas
K5T/D38H/D44E/A128T/E296K/H404R
58fold increase in kcat as compared to wild-type enzyme
K5T/D44E/H404R
-
at pH 7.4, the mutant has a 4times higher kcat value than the wild type ADI and retains about 50% of its activity relative to its pH optimum (pH 7.0), compared to about 10% in the case of the wild type ADI
R18L
-
mutant shows higher activity than wild-type at pH 7.4 and pH 6.0
V10F
-
mutant shows higher activity than wild-type at pH 7.4 and pH 6.0
D38H/A128T/E296K/H404R/I410L/A276W
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/A276W displays tremendous pH and thermal stability
-
D38H/A128T/E296K/H404R/I410L/R243L
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/R243L exhibits significantly enhanced specific activity and substrate binding affinity, as illustrated by the dramatically reduced Km value (0.16 mmol/l) and a more favorable free energy of L-arginine binding at physiological conditions
-
D38H/A128T/E296K/H404R/I410L/S245D
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, mutant enzyme D38H/A128T/E296K/H404R/I410L/S245D shows a significantly increased specific activity and a similar Km value at physiological conditions
-
C424A
catalytically inactive
C424A
-
catalytically inactive
-
C406A
inactive mutant enzyme
C406A
-
no enzymic activity
C406A
site-directed mutagenesis, inactive mutant
C406A
site-directed mutagenesis, the catalytic residue mutant, substrate binding structure, overview
C406S
inactive mutant enzyme
C406S
-
no enzymic activity
C406S
site-directed mutagenesis, inactive mutant
D166A
inactive mutant enzyme
D166A
site-directed mutagenesis, inactive mutant
D166A
site-directed mutagenesis, the catalytic residue mutant, substrate binding structure, overview
D280A
inactive mutant enzyme
D280A
site-directed mutagenesis, inactive mutant
D280A
site-directed mutagenesis, the catalytic residue mutant, substrate binding structure, overview
E224A
kcat/Km is 23684fold higher than the wild-type value
E224A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E224D
kcat/Km is 50000fold higher than the wild-type value
E224D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H278A
inactive mutant enzyme
H278A
site-directed mutagenesis, inactive mutant
H278A
site-directed mutagenesis, the catalytic residue mutant, substrate binding structure, overview
H278N
inactive mutant enzyme
H278N
site-directed mutagenesis, inactive mutant
H278V
inactive mutant enzyme
H278V
site-directed mutagenesis, inactive mutant
N160A
kcat/Km is 5625fold higher than the wild-type value
N160A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R185A
kcat/Km is 7627fold higher than the wild-type value
R185A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R185L
kcat/Km is 25000fold higher than the wild-type value
R185L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R243A
kcat/Km is 150000fold higher than the wild-type value
R243A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R243K
kcat/Km is 150000fold higher than the wild-type value
R243K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R243L
kcat/Km is 225000fold higher than the wild-type value
R243L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R401A
kcat/Km is 56250fold higher than the wild-type value
R401A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
-
construction of a truncated mutant enzyme with a stop codon TGA instead of a tryptophan codon TGG by site-directed mutagenesis
additional information
-
replacement of substrate binding residues leads to highly reduced activity of the mutant enzymes
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Shibatani, T.; Kakimoto, T.; Chibata, I.
Crystallization and properties of L-arginine deiminase of Pseudomonas putida
J. Biol. Chem.
250
4580-4583
1975
Pseudomonas putida
brenda
Kakimoto, T.; Shibatani, T.; Chibata, I.
Crystallization of L-arginine-deiminase from Pseudomonas putida
FEBS Lett.
19
166-168
1971
Pseudomonas putida
brenda
Fenske, J.D.; Kenny, G.E.
Role of arginine deiminase in growth of Mycoplasma hominis
J. Bacteriol.
126
501-510
1976
Mycoplasmopsis arginini, Mycoplasma arthritidis, Mycoplasmopsis fermentans, Mycoplasmopsis gallinarum, Mycoplasma gallisepticum, Mycoplasma hominis, Mycoplasma hominis 14027, Mycoplasmopsis arginini G230, Mycoplasmopsis arginini 67-166
brenda
Weickmann, J.L.; Fahrney, D.E.
Arginine deiminase from Mycoplasma arthritidis. Evidence for multiple forms
J. Biol. Chem.
252
2615-2620
1977
Mycoplasma arthritidis
brenda
Smith, D.W.; Fahrney, D.E.
Catalysis by arginine deiminase: evidence for a covalent intermediate
Biochem. Biophys. Res. Commun.
83
101-106
1978
Mycoplasma arthritidis
brenda
Weickmann, J.L.; Himmel, M.E.; Smith, D.W.; Fahrney, D.E.
Arginine deiminase: demonstration of two active sites and possible half-of-the-sites reactivity
Biochem. Biophys. Res. Commun.
83
107-113
1978
Mycoplasma arthritidis
brenda
Weickmann, J.L.; Himmel, M.E.; Squire, P.G.; Fahrney, D.E.
Arginine deiminase from Mycoplasma arthritidis. Properties of the enzyme from log phase cultures
J. Biol. Chem.
253
6010-6015
1978
Mycoplasma arthritidis
brenda
Smith, D.W.; Ganaway, R.L.; Fahrney, D.E.
Arginine deiminase from Mycoplasma arthritidis. Structure-activity relationships among substrates and competitive inhibitors
J. Biol. Chem.
253
6016-6020
1978
Mycoplasma arthritidis
brenda
Shibatani, T.; Kakimoto, T.; Chibata, I.
Subunit and amino acid composition of L-arginine deiminase of Pseudomonas putida
FEBS Lett.
96
389-391
1978
Pseudomonas putida
brenda
Park, B.S.; Hirotani, A.; Nakano, Y.; Kitaoka, S.
Purification and some properties of arginine deiminase in Euglena gracilis Z
Agric. Biol. Chem.
48
483-489
1984
Euglena gracilis
-
brenda
Manca de Nadra, M.C.; Pesce de Ruiz Holgado, A.A.; Oliver, G.
Isolation and properties of arginine deiminase in Lactobacillus buchneri NCDO110
J. Appl. Biochem.
6
184-187
1984
Lentilactobacillus buchneri, Lentilactobacillus buchneri NCDO110
-
brenda
Sacks, L.E.
Increased formation of arginine deiminase by Clostridium perfringens FD-1 growing in the presence of caffeine
Experientia
41
1435-1437
1984
Clostridium perfringens, Clostridium perfringens FD-1
brenda
Lin, J.S.L.
Arginine deiminase of Mycoplasma hominis: cytoplasmic and membrane-associated forms
J. Gen. Microbiol.
132
1467-1474
1986
Mycoplasma hominis
brenda
Hiraoka, B.Y.; Harada, M.; Fukasawa, K.; Mogi, M.
Intracellular localization of the arginine deiminase pathway in Streptococcus mitis
Curr. Microbiol.
15
81-84
1987
Streptococcus mitis
-
brenda
Knodler, L.A.; Sekyere, E.O.; Stewart, T.S.; Schofield, P.J.; Edwards, M.R.
Cloning and expression of a prokaryotic enzyme, arginine deiminase, from primitive eukaryote Giardia intestinalis
J. Biol. Chem.
273
4470-4477
1998
Giardia intestinalis (Q27657), Giardia intestinalis
brenda
Komada, Y.; Zhang, X.L.; Zhou, Y.W.; Ido, M.; Azuma, E.
Apoptotic cell death of human T lymphoblastoid cells induced by arginine deiminase
Int. J. Hematol.
65
129-141
1997
Mycoplasmopsis arginini
brenda
Kang, S.W.; Kang, H.; Park, I.S.; Choi, S.H.; Shin, K.H.; Chun, Y.S.; Chun, G.B.; Min, B.H.
Cytoprotective effect of arginine deiminase on taxol-induced apoptosis in DU145 human prostate cancer cells
Mol. Cells
10
331-337
2000
Mycoplasmopsis arginini
brenda
Liu, S.Q.; Pritchard, G.G.; Hardman, M.J.; Pilone, G.J.
Occurrence of arginine deiminase pathway enzymes in arginine catabolism by wine lactic acid bacteria
Appl. Environ. Microbiol.
61
310-316
1995
Levilactobacillus brevis, Lentilactobacillus buchneri, Lentilactobacillus hilgardii, Oenococcus oeni, no activity in Lactobacillus brevis, no activity in Lactobacillus delbrueckii, no activity in Lactobacillus plantarum, no activity in Oenococcus oeni, no activity in Pediococcus sp., Oenococcus oeni MCW, Oenococcus oeni Microenos B2, Oenococcus oeni Microoenos B, Oenococcus oeni DSIR-C, Oenococcus oeni DSIR-B, Oenococcus oeni DSIR-A, Lentilactobacillus hilgardii Microenos HP, Oenococcus oeni OENO, Levilactobacillus brevis EQUILAIT, Oenococcus oeni L181, Oenococcus oeni Er1a, Oenococcus oeni 252, Oenococcus oeni 1008, Oenococcus oeni 2043, Oenococcus oeni ML34, no activity in Lactobacillus delbrueckii CUC-1, no activity in Lactobacillus brevis ML30, Oenococcus oeni 122, Levilactobacillus brevis 250, Oenococcus oeni PSU-1, Oenococcus oeni Vinoflora Oenos, Oenococcus oeni Ey2d, Lentilactobacillus buchneri CUC-3, Oenococcus oeni 2035
brenda
Yarlett, N.; Martinez, M.P.; Moharrami, M.A.; Tachezy, J.
The contribution of the arginine dihydrolase pathway to energy metabolism by Trichomonas vaginalis
Mol. Biochem. Parasitol.
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117-125
1996
Trichomonas vaginalis
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Monstadt, G.M.; Holldorf, A.W.
Arginine deiminase from Halobacterium salinarium. Purification and properties
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Halobacterium salinarum
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Takaku, H.; Takase, M.; Abe, S.i.; Hayashi, H.; Miyazaki, K.
In vivo anti-tumor activity of arginine deiminase purified from Mycoplasma arginini
Int. J. Cancer
51
244-249
1992
Mycoplasmopsis arginini, Pseudomonas putida
brenda
Sugimura, K.; Fukuda, S.; Wada, Y.; Taniai, M.; Suzuki, M.; Kimura, T.; Ohno, T.; Yamamoto, K.; Azuma, I.
Identification and purification of arginine deiminase that originated from Mycoplasma arginini
Infect. Immun.
58
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Mycoplasmopsis arginini
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Degnan, B.A.; Palmer, J.M.; Robson, T.; Jones, C.E.D.; Fischer, M.; Glanville, M.; Mellor, G.D.; Diamond, A.G.; Kehoe, M.A.; Goodacre, J.A.
Inhibition of human peripheral blood mononuclear cell proliferation by Streptococcus pyogenes cell extract is associated with arginine deiminase activity
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Mycoplasmopsis arginini, Streptococcus pyogenes
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Schofield, P.J.; Costello, M.; Edwards, M.R.; OSullivan, W.J.
The arginine dihydrolase pathway is present in Giardia intestinalis
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Giardia intestinalis
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Misawa, S.; Aoshima, M.; Takaku, H.; Matsumoto, M.; Hayashi, H.
High-level expression of Mycoplasma arginine deiminase in Escherichia coli and its efficient renaturation as an anti-tumor enzyme
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Mycoplasmopsis arginini
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Gong, H.; Zoelzer, F.; von Recklinghausen, G.; Havers, W.; Schweigerer, L.
Arginine deiminase inhibits proliferation of human leukemia cells more potently than asparaginase by inducing cell cycle arrest and apoptosis
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Mycoplasmopsis arginini
brenda
Oudjama, Y.; Tricot, C.; Stalon, V.; Wouters, J.
Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase
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Pseudomonas aeruginosa
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Lu, X.; Galkin, A.; Herzberg, O.; Dunaway-Mariano, D.
Arginine deiminase uses an active-site cysteine in nucleophilic catalysis of L-arginine hydrolysis
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Pseudomonas aeruginosa
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Galkin, A.; Kulakova, L.; Sarikaya, E.; Lim, K.; Howard, A.; Herzberg, O.
Structural insight into arginine degradation by arginine deiminase, an antibacterial and parasite drug target
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279
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Pseudomonas aeruginosa
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Das, K.; Butler, G.H.; Kwiatkowski, V.; Clark, A.D., Jr.; Yadav, P.; Arnold, E.
Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism
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657-667
2004
Mycoplasmopsis arginini (P23793), Mycoplasmopsis arginini
brenda
Lu, X.; Li, L.; Wu, R.; Feng, X.; Li, Z.; Yang, H.; Wang, C.; Guo, H.; Galkin, A.; Herzberg, O.; Mariano, P.S.; Martin, B.M.; Dunaway-Mariano, D.
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function
Biochemistry
45
1162-1172
2006
Pseudomonas aeruginosa, Pseudomonas aeruginosa (P13981)
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Budin-Verneuil, A.; Maguin, E.; Auffray, Y.; Ehrlich, D.S.; Pichereau, V.
Genetic structure and transcriptional analysis of the arginine deiminase (ADI) cluster in Lactococcus lactis MG1363
Can. J. Microbiol.
52
617-622
2006
Lactococcus lactis
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Lu, X.; Li, L.; Feng, X.; Wu, Y.; Dunaway-Mariano, D.; Engen, J.R.; Mariano, P.S.
L-Canavanine is a time-controlled mechanism-based inhibitor of Pseudomonas aeruginosa arginine deiminase
J. Am. Chem. Soc.
127
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Pseudomonas aeruginosa
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Gruening, P.; Fulde, M.; Valentin-Weigand, P.; Goethe, R.
Structure, regulation, and putative function of the arginine deiminase system of Streptococcus suis
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Streptococcus suis
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Kubo, M.; Nishitsuji, H.; Kurihara, K.; Hayashi, T.; Masuda, T.; Kannagi, M.
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87
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Mycoplasmopsis arginini
brenda
Nehme, B.; Ganga, M.A.; Lonvaud-Funel, A.
The arginine deiminase locus of Oenococcus oeni includes a putative arginyl-tRNA synthetase ArgS2 at its 3-end
Appl. Microbiol. Biotechnol.
70
590-597
2006
Oenococcus oeni, Oenococcus oeni IOEB 8406
brenda
Galkin, A.; Lu, X.; Dunaway-Mariano, D.; Herzberg, O.
Crystal structures representing the Michaelis complex and the thiouronium reaction intermediate of Pseudomonas aeruginosa arginine deiminase
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280
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Pseudomonas aeruginosa (P13981), Pseudomonas aeruginosa
brenda
Spano, G.; Massa, S.; Arena, M.E.; Manca de Nadra, M.C.
Arginine metabolism in wine Lactobacillus plantarum: in vitro activities of the enzymes arginine deiminase (ADI) and ornithine transcarbamilase (OTCase).
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Lactiplantibacillus plantarum
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Wang, M.; Basu, A.; Palm, T.; Hua, J.; Youngster, S.; Hwang, L.; Liu, H.C.; Li, X.; Peng, P.; Zhang, Y.; Zhao, H.; Zhang, Z.; Longley, C.; Mehlig, M.; Borowski, V.; Sai, P.; Viswanathan, M.; Jang, E.; Petti, G.; Liu, S.; Yang, K.; Filpula, D.
Engineering an arginine catabolizing bioconjugate: Biochemical and pharmacological characterization of PEGylated derivatives of arginine deiminase from Mycoplasma arthritidis
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Mycoplasma arthritidis
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Ni, Y.; Schwaneberg, U.; Sun, Z.
Arginine deiminase, a potential anti-tumor drug
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261
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Giardia intestinalis, Halobacterium salinarum, Homo sapiens, Lactococcus lactis ssp. lactis, Mycoplasmopsis arginini, Mycoplasma hominis, Pseudomonas aeruginosa, Pseudomonas putida, Streptococcus sanguinis, Pseudomonas plecoglossicida (A7LKB0), Pseudomonas plecoglossicida CGMCC 2039 (A7LKB0)
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Feun, L.; Savaraj, N.
Pegylated arginine deiminase: a novel anticancer enzyme agent
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2006
Mycoplasma hominis
brenda
Li, L.; Li, Z.; Chen, D.; Lu, X.; Feng, X.; Wright, E.C.; Solberg, N.O.; Dunaway-Mariano, D.; Mariano, P.S.; Galkin, A.; Kulakova, L.; Herzberg, O.; Green-Church, K.B.; Zhang, L.
Inactivation of microbial arginine deiminases by L-canavanine
J. Am. Chem. Soc.
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2008
Bacillus cereus, Burkholderia mallei, Escherichia coli, Giardia intestinalis, Pseudomonas aeruginosa, Pseudomonas aeruginosa (P13981)
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Louw, C.; Gordon, A.; Johnston, N.; Mollatt, C.; Bradley, G.; Whiteley, C.G.
Arginine deiminases: therapeutic tools in the etiology and pathogenesis of Alzheimers disease
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22
121-126
2007
Pseudomonas aeruginosa
brenda
Izzo, F.; Montella, M.; Orlando, A.P.; Nasti, G.; Beneduce, G.; Castello, G.; Cremona, F.; Ensor, C.M.; Holtzberg, F.W.; Bomalaski, J.S.; Clark, M.A.; Curley, S.A.; Orlando, R.; Scordino, F.; Korba, B.E.
Pegylated arginine deiminase lowers hepatitis C viral titers and inhibits nitric oxide synthesis
J. Gastroenterol. Hepatol.
22
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2007
Homo sapiens
brenda
Park, H.; Lee, J.B.; Shim, Y.J.; Shin, Y.J.; Jeong, S.Y.; Oh, J.; Park, G.H.; Lee, K.H.; Min, B.H.
Arginine deiminase enhances MCF-7 cell radiosensitivity by inducing changes in the expression of cell cycle-related proteins
Mol. Cells
25
305-311
2008
Mycoplasmopsis arginini
brenda
Kim, J.H.; Kim, J.H.; Yu, Y.S.; Kim, D.H.; Min, B.H.; Kim, K.W.
Anti-tumor activity of arginine deiminase via arginine deprivation in retinoblastoma
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18
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2007
Homo sapiens
brenda
Kim, J.E.; Jeong, D.W.; Lee, H.J.
Expression, purification, and characterization of arginine deiminase from Lactococcus lactis ssp. lactis ATCC 7962 in Escherichia coli BL21
Protein Expr. Purif.
53
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2007
Lactococcus lactis subsp. lactis (Q2HYA0)
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Wei, Y.; Zhou, H.; Sun, Y.; He, Y.; Luo, Y.
Insight into the catalytic mechanism of arginine deiminase: functional studies on the crucial sites
Proteins
66
740-750
2007
Mycoplasma hominis
brenda
Bowles, T.L.; Kim, R.; Galante, J.; Parsons, C.M.; Virudachalam, S.; Kung, H.J.; Bold, R.J.
Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase
Int. J. Cancer
123
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2008
Homo sapiens
brenda
Liu, Y.; Dong, Y.; Chen, Y.Y.; Burne, R.A.
Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes
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74
5023-5030
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Streptococcus gordonii
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Li, L.; Li, Z.; Wang, C.; Xu, D.; Mariano, P.S.; Guo, H.; Dunaway-Mariano, D.
The electrostatic driving force for nucleophilic catalysis in L-arginine deiminase: a combined experimental and theoretical study
Biochemistry
47
4721-4732
2008
Bacillus cereus, Burkholderia mallei, Escherichia coli, Pseudomonas aeruginosa (P13981)
brenda
Ni, Y.; Li, Z.; Sun, Z.; Zheng, P.; Liu, Y.; Zhu, L.; Schwaneberg, U.
Expression of arginine deiminase from Pseudomonas plecoglossicida CGMCC2039 in Escherichia coli and its anti-tumor activity
Curr. Microbiol.
58
593-598
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Pseudomonas plecoglossicida (A7LKB0), Pseudomonas plecoglossicida, Pseudomonas plecoglossicida CGMCC2039 (A7LKB0)
brenda
Ryan, S.; Begley, M.; Gahan, C.G.; Hill, C.
Molecular characterization of the arginine deiminase system in Listeria monocytogenes: regulation and role in acid tolerance
Environ. Microbiol.
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Listeria monocytogenes
brenda
Lafay, B.; Ruimy, R.; de Traubenberg, C.R.; Breittmayer, V.; Gauthier, M.J.; Christen, R.
Roseobacter algicola sp. nov., a new marine bacterium isolated from the phycosphere of the toxin-producing dinoflagellate Prorocentrum lima
Int. J. Syst. Bacteriol.
45
290-296
1995
no activity in Marinovum algicola, no activity in Marinovum algicola ATCC 51442
brenda
Ruiz-Ponte, C.; Cilia, V.; Lambert, C.; Nicolas, J.L.
Roseobacter gallaeciensis sp. nov., a new marine bacterium isolated from rearings and collectors of the scallop Pecten maximus
Int. J. Syst. Bacteriol.
48 Pt 2
537-542
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no activity in Phaeobacter gallaeciensis BS107
brenda
Lau, S.C.; Tsoi, M.M.; Li, X.; Plakhotnikova, I.; Wu, M.; Wong, P.K.; Qian, P.Y.
Loktanella hongkongensis sp. nov., a novel member of the alpha-Proteobacteria originating from marine biofilms in Hong Kong waters
Int. J. Syst. Evol. Microbiol.
54
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no activity in Loktanella hongkongensis
brenda
Lin, X.; Lamont, R.J.; Wu, J.; Xie, H.
Role of differential expression of streptococcal arginine deiminase in inhibition of fimA expression in Porphyromonas gingivalis
J. Bacteriol.
190
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Streptococcus cristatus, Streptococcus cristatus CC5A
brenda
Yu, H.H.; Wu, F.L.; Lin, S.E.; Shen, L.J.
Recombinant arginine deiminase reduces inducible nitric oxide synthase iNOS-mediated neurotoxicity in a coculture of neurons and microglia
J. Neurosci. Res.
86
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2008
Homo sapiens
brenda
Rodriguez, S.B.; Stitt, B.L.; Ash, D.E.
Expression of peptidylarginine deiminase from Porphyromonas gingivalis in Escherichia coli: enzyme purification and characterization
Arch. Biochem. Biophys.
488
14-22
2009
Porphyromonas gingivalis, Porphyromonas gingivalis BAA-308-5 (W83)
brenda
Li, Z.; Kulakova, L.; Li, L.; Galkin, A.; Zhao, Z.; Nash, T.E.; Mariano, P.S.; Herzberg, O.; Dunaway-Mariano, D.
Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia
Bioorg. Chem.
37
149-161
2009
Giardia intestinalis (Q27657), Giardia intestinalis, Giardia intestinalis isolate WB, clone 1267 (Q27657)
brenda
Kim, J.E.; Kim, S.Y.; Lee, K.W.; Lee, H.J.
Arginine deiminase originating from Lactococcus lactis ssp. lactis American Type Culture Collection (ATCC) 7962 induces G1-phase cell-cycle arrest and apoptosis in SNU-1 stomach adenocarcinoma cells
Br. J. Nutr.
102
1469-1476
2009
Lactococcus lactis subsp. lactis (Q2HYA0), Lactococcus lactis subsp. lactis ATCC 7962 (Q2HYA0)
brenda
Zhu, L.; Tee, K.L.; Roccatano, D.; Sonmez, B.; Ni, Y.; Sun, Z.H.; Schwaneberg, U.
Directed evolution of an antitumor drug (arginine deiminase PpADI) for increased activity at physiological pH
ChemBioChem
11
691-697
2010
Pseudomonas plecoglossicida
brenda
Pereira, C.I.; San Romao, M.V.; Lolkema, J.S.; Crespo, M.T.
Weissella halotolerans W22 combines arginine deiminase and ornithine decarboxylation pathways and converts arginine to putrescine
J. Appl. Microbiol.
107
1894-1902
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Weissella halotolerans, Weissella halotolerans W22
brenda
Glazer, E.S.; Piccirillo, M.; Albino, V.; Di Giacomo, R.; Palaia, R.; Mastro, A.A.; Beneduce, G.; Castello, G.; De Rosa, V.; Petrillo, A.; Ascierto, P.A.; Curley, S.A.; Izzo, F.
Phase II study of pegylated arginine deiminase for nonresectable and metastatic hepatocellular carcinoma
J. Clin. Oncol.
28
2220-2226
2010
Mycoplasma sp.
brenda
Rimaux, T.; Riviere, A.; Illeghems, K.; Weckx, S.; De Vuyst, L.; Leroy, F.
Expression of the arginine deiminase pathway genes in Lactobacillus sakei is strain dependent and is affected by the environmental pH
Appl. Environ. Microbiol.
78
4874-4883
2012
Latilactobacillus sakei
brenda
Ni, Y.; Liu, Y.; Schwaneberg, U.; Zhu, L.; Li, N.; Li, L.; Sun, Z.
Rapid evolution of arginine deiminase for improved anti-tumor activity
Appl. Microbiol. Biotechnol.
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2011
Pseudomonas plecoglossicida
brenda
Zhuo, W.; Song, X.; Zhou, H.; Luo, Y.
Arginine deiminase modulates endothelial tip cells via excessive synthesis of reactive oxygen species
Biochem. Soc. Trans.
39
1376-1381
2011
Homo sapiens
brenda
Kelly, M.P.; Jungbluth, A.A.; Wu, B.W.; Bomalaski, J.; Old, L.J.; Ritter, G.
Arginine deiminase PEG20 inhibits growth of small cell lung cancers lacking expression of argininosuccinate synthetase
Br. J. Cancer
106
324-332
2012
Homo sapiens
brenda
Rimaux, T.; Vrancken, G.; Pothakos, V.; Maes, D.; De Vuyst, L.; Leroy, F.
The kinetics of the arginine deiminase pathway in the meat starter culture Lactobacillus sakei CTC 494 are pH-dependent
Food Microbiol.
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2011
Latilactobacillus sakei
brenda
Chantratita, N.; Tandhavanant, S.; Wikraiphat, C.; Trunck, L.A.; Rholl, D.A.; Thanwisai, A.; Saiprom, N.; Limmathurotsakul, D.; Korbsrisate, S.; Day, N.P.; Schweizer, H.P.; Peacock, S.J.
Proteomic analysis of colony morphology variants of Burkholderia pseudomallei defines a role for the arginine deiminase system in bacterial survival
J. Proteomics
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2012
Burkholderia pseudomallei
brenda
Gallego, P.; Planell, R.; Benach, J.; Querol, E.; Perez-Pons, J.A.; Reverter, D.
Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans
PLoS ONE
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2012
Malacoplasma penetrans (Q8EVF6), Malacoplasma penetrans HF-2 (Q8EVF6)
brenda
Hering, S.; Sieg, A.; Kreikemeyer, B.; Fiedler, T.
Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49
Protein Expr. Purif.
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2013
Streptococcus pyogenes (B5XMC3), Streptococcus pyogenes
brenda
Slade, D.J.; Fang, P.; Dreyton, C.J.; Zhang, Y.; Fuhrmann, J.; Rempel, D.; Bax, B.D.; Coonrod, S.A.; Lewis, H.D.; Guo, M.; Gross, M.L.; Thompson, P.R.
Protein arginine deiminase 2 binds calcium in an ordered fashion implications for inhibitor design
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Homo sapiens (Q9Y2J8)
brenda
Jamil, S.; Liu, M.H.; Liu, Y.M.; Han, R.Z.; Xu, G.C.; Ni, Y.
Hydrophobic mutagenesis and semi-rational engineering of arginine deiminase for markedly enhanced stability and catalytic efficiency
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176
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2015
Pseudomonas plecoglossicida (A7LKB0), Pseudomonas plecoglossicida, Pseudomonas plecoglossicida CGMCC2039 (A7LKB0)
brenda
Cheng, F.; Zhu, L.; Lue, H.; Bernhagen, J.; Schwaneberg, U.
Directed arginine deiminase evolution for efficient inhibition of arginine-auxotrophic melanomas
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99
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2015
Pseudomonas plecoglossicida (A7LKB0), Pseudomonas plecoglossicida
brenda
Starikova, E.A.; Sokolov, A.V.; Vlasenko, A.Y.; Burova, L.A.; Freidlin, I.S.; Vasilyev, V.B.
Biochemical and biological activity of arginine deiminase from Streptococcus pyogenes M22
Biochem. Cell Biol.
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2016
Streptococcus pyogenes, Streptococcus pyogenes M22
brenda
El-Sayed, A.; Hassan, M.; Nada, H.
Purification, immobilization, and biochemical characterization of L-arginine deiminase from thermophilic Aspergillus fumigatus KJ434941 Anticancer activity in vitro
Biotechnol. Prog.
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2015
Aspergillus fumigatus, Aspergillus fumigatus KJ434941
brenda
Xiong, L.; Teng, J.L.; Watt, R.M.; Liu, C.; Lau, S.K.; Woo, P.C.
Molecular characterization of arginine deiminase pathway in Laribacter hongkongensis and unique regulation of arginine catabolism and anabolism by multiple environmental stresses
Environ. Microbiol.
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2015
Laribacter hongkongensis (C1DD78), Laribacter hongkongensis (C1DD83), Laribacter hongkongensis, Laribacter hongkongensis HLHK9 (C1DD78), Laribacter hongkongensis HLHK9 (C1DD83)
brenda
El-Sayed, A.; Shindia, A.; Zeid, A.; Yassin, A.; Sitohy, M.; Sitohy, B.
Aspergillus nidulans thermostable arginine deiminase-Dextran conjugates with enhanced molecular stability, proteolytic resistance, pharmacokinetic properties and anticancer activity
Enzyme Microb. Technol.
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Aspergillus nidulans
brenda
Cai, X.; Jiang, H.; Zhang, T.; Jiang, B.; Mu, W.; Miao, M.
Thermostability and specific-activity enhancement of an arginine deiminase from Enterococcus faecalis SK23.001 via semirational design for L-citrulline production
J. Agric. Food Chem.
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2018
Enterococcus faecalis (A0A3G2YMH7), Enterococcus faecalis, Enterococcus faecalis SK23.001 (A0A3G2YMH7)
brenda
Trejo-Soto, P.J.; Aguayo-Ortiz, R.; Yepez-Mulia, L.; Hernandez-Campos, A.; Medina-Franco, J.L.; Castillo, R.
Insights into the structure and inhibition of Giardia intestinalis arginine deiminase homology modeling, docking, and molecular dynamics studies
J. Biomol. Struct. Dyn.
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732-748
2016
Giardia intestinalis (Q27657), Giardia intestinalis
brenda
Patil, M.D.; Rathod, V.P.; Bihade, U.R.; Banerjee, U.C.
Purification and characterization of arginine deiminase from Pseudomonas putida Structural insights of the differential affinities of L-arginine analogues
J. Biosci. Bioeng.
127
129-137
2019
Pseudomonas putida (Q88P52), Pseudomonas putida, Pseudomonas putida ATCC 47054 (Q88P52)
brenda
Subramanian, V.; Knight, J.S.; Parelkar, S.; Anguish, L.; Coonrod, S.A.; Kaplan, M.J.; Thompson, P.R.
Design, synthesis, and biological evaluation of tetrazole analogs of Cl-amidine as protein arginine deiminase inhibitors
J. Med. Chem.
58
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2015
Homo sapiens (Q9Y2J8)
brenda
Kaur, B.; Kaur, R.
Purification of a dimeric arginine deiminase from Enterococcus faecium GR7 and study of its anti-cancerous activity
Protein Expr. Purif.
125
53-60
2016
Enterococcus faecium, Enterococcus faecium GR7
brenda